38 results on '"H. Hermel"'
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2. CARDIAC SARCOIDOSIS PATIENTS WHO MEET THE 1993 AND 2006 JAPANESE DIAGNOSTIC CRITERIA ARE MORE LIKELY TO HAVE ADVERSE OUTCOMES
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Shilpa Jasti, Muhammad Afzal, Steven Jack Kalbfleisch, Kenneth A. Ellenbogen, Frank M. Bogun, Alexandru B. Chicos, Henri Roukoz, Peter J. Zimetbaum, Francis Murgatroyd, Mikhail Torosoff, Marc Judson, Pyotr G. Platonov, Adarsh K. Bhan, Lynda E. Rosenfeld, David B. De Lurgio, Ann C. Garlitski, Melody H. Hermel, Vasanth Vedantham, Kyoko Soejima, Timm-Michael L. Dickfeld, Xiaokui Gu, Eric Puroll, Thomas C. Crawford, and Jordana Kron
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Cardiology and Cardiovascular Medicine - Published
- 2022
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3. TRADITIONAL RISK FACTORS INCREASE THE RISK OF POOR OUTCOMES IN PATIENTS WITH CARDIAC SARCOIDOSIS
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Shilpa Jasti, Muhammad Afzal, Steven Jack Kalbfleisch, Kenneth A. Ellenbogen, Frank M. Bogun, Alexandru B. Chicos, Henri Roukoz, Peter J. Zimetbaum, Francis Murgatroyd, Mikhail Torosoff, Marc Judson, Pyotr G. Platonov, Adarsh K. Bhan, Lynda E. Rosenfeld, David B. De Lurgio, Ann C. Garlitski, Melody H. Hermel, Vasanth Vedantham, Kyoko Soejima, Timm-Michael L. Dickfeld, Xiaokui Gu, Eric Puroll, Thomas C. Crawford, and Jordana Kron
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Cardiology and Cardiovascular Medicine - Published
- 2022
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4. Progress in gastrointestinal cancer immunotherapy
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David J. Hermel, Melody H. Hermel, and Darren S. Sigal
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Cancer Research ,Oncology ,Radiology, Nuclear Medicine and imaging - Published
- 2017
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5. Mental stress peripheral vascular reactivity is elevated in women with coronary vascular dysfunction: Results from the NHLBI-sponsored Cardiac Autonomic Nervous System (CANS) study
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David Hermel, Amit J. Shah, Puja K. Mehta, Amir Lerman, Margo Minissian, Galen Cook-Wiens, Chrisandra Shufelt, Michael R. Irwin, David S. Krantz, Melody H. Hermel, C. Noel Bairey Merz, Michael D. Nelson, Sailaja Marpuri, Elizabeth A. Martin, Ayman Alkhoder, and Janet Wei
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Coronary Artery Disease ,030204 cardiovascular system & hematology ,Cardiorespiratory Medicine and Haematology ,Chest pain ,Cardiovascular ,Coronary artery disease ,0302 clinical medicine ,and Blood Institute (U.S.) ,2.1 Biological and endogenous factors ,Aetiology ,Lung ,Pain Research ,Cold pressor test ,Women heart disease ,Middle Aged ,Peripheral ,Cold Temperature ,Mental stress ,Heart Disease ,Mental Health ,Microvascular dysfunction ,Cardiology ,Public Health and Health Services ,Female ,medicine.symptom ,Cardiology and Cardiovascular Medicine ,medicine.medical_specialty ,Ischemia ,Hyperemia ,Stress ,Autonomic Nervous System ,Article ,03 medical and health sciences ,Clinical Research ,Internal medicine ,Behavioral and Social Science ,medicine ,Humans ,Reactive hyperemia ,Aged ,business.industry ,National Heart ,medicine.disease ,United States ,Surgery ,Autonomic nervous system ,Good Health and Well Being ,Cardiovascular System & Hematology ,Vasoconstriction ,Psychological ,business ,National Heart, Lung, and Blood Institute (U.S.) ,Vascular reactivity ,030217 neurology & neurosurgery ,Stress, Psychological - Abstract
BackgroundWomen with chest pain, ischemia, and no obstructive coronary artery disease often have coronary vascular dysfunction (CVaD). Peripheral vascular reactivity to mental stress may contribute mechanistic understanding of stress-induced ischemia in women with CVaD.Methods62 women (41 CVaD and 21 controls) underwent mental stress testing (MST) with anger recall, mental arithmetic, and forehead cold pressor (COP) challenge. Emotional arousal was measured (Likert scale). Reactive hyperemia index (RHI) was calculated before and after MST by peripheral arterial tonometry (PAT). Stress PAT ratio (SPR) of pulse amplitude during stress to rest was obtained to measure vasoconstriction. Wilcoxson rank sum test was used for analysis.ResultsMean age of CVaD and control groups was 58±9 and 55±10years (p=0.73). Baseline RHI correlated with coronary endothelial function (r=0.36, p=0.03) and inversely with RHI change post-MST (r=-0.51, p
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- 2017
6. Contributory presentations/posters
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N. Manoj, V. R. Srinivas, A. Surolia, M. Vijayan, K. Suguna, R. Ravishankar, R. Schwarzenbacher, K. Zeth, null Diederichs, G. M. Kostner, A. Gries, P. Laggner, R. Prassl, null Madhusudan, Pearl Akamine, Nguyen-huu Xuong, Susan S. Taylor, M. Bidva Sagar, K. Saikrishnan, S. Roy, K. Purnapatre, P. Handa, U. Varshney, B. K. Biswal, N. Sukumar, J. K. Mohana Rao, A. Johnson, Vasantha Pattabhi, S. Sri Krishna, Mira Sastri, H. S. Savithri, M. R. N. Murthy, Bindu Pillai, null Kannan, M. V. Hosur, Mukesh Kumar, Swati Patwardhan, K. K. Kannan, B. Padmanabhaa, S. Sasaki-Sugio, M. Nukaga, T. Matsuzaki, S. Karthikevan, S. Sharma, A. K. Sharma, M. Paramasivam, P. Kumar, J. A. Khan, S. Yadav, A. Srinivasan, T. P. Singh, S. Gourinath, Neelima Alam, A. Srintvasan, Vikas Chandra, Punit Kaur, Ch. Betzel, S. Ghosh, A. K. Bera, S. Bhattacharya, S. Chakraborty, A. K. Pal, B. P. Mukhopadhyay, I. Dey, U. Haldar, Asok Baneriee, Jozef Sevcik, Adriana Solovicova, K. Sekar, M. Sundaralingam, N. Genov, Dong-cai Liang, Tao Jiang, Ji-ping Zhang, Wen-rui Chang, Wolfgang Jahnke, Marcel Blommers, S. C. Panchal, R. V. Hosur, Bindu Pillay, Puniti Mathur, S. Srivatsun, Ratan Mani Joshi, N. R. Jaganathan, V. S. Chauhan, H. S. Atreya, S. C. Sahu, K. V. R. Chary, Girjesh Govil, Elisabeth Adjadj, Éric Quinjou, Nadia Izadi-Pruneyre, Yves Blouquit, Joël Mispelter, Bernadette Heyd, Guilhem Lerat, Philippe Milnard, Michel Desmadreil, Y. Lin, B. D. Nageswara Rao, Vidva Raghunathan, Mei H. Chau, Prashant Pesais, Sudha Srivastava, Evans Coutinho, Anil Saran, Leizl F. Sapico, Jayson Gesme, Herbert Lijima, Raymond Paxton, Thamarapu Srikrishnan, C. R. Grace, G. Nagenagowda, A. M. Lynn, Sudha M. Cowsik, Sarata C. Sahu, S. Chauhan, A. Bhattacharya, G. Govil, Anil Kumar, Maurizio Pellecchia, Erik R. P. Zuiderweg, Keiichi Kawano, Tomoyasu Aizawa, Naoki Fujitani, Yoichi Hayakawa, Atsushi Ohnishi, Tadayasu Ohkubo, Yasuhiro Kumaki, Kunio Hikichi, Katsutoshi Nitta, V. Rani Parvathy, R. M. Kini, Takumi Koshiba, Yoshihiro Kobashigawa, Min Yao, Makoto Demura, Astushi Nakagawa, Isao Tanaka, Kunihiro Kuwajima, Jens Linge, Seán O. Donoghue, Michael Nilges, G. Chakshusmathi, Girish S. Ratnaparkhi, P. K. Madhu, R. Varadarajan, C. Tetreau, M. Tourbez, D. Lavalette, M. Manno, P. L. San Biagio, V. Martorana, A. Emanuele, S. M. Vaiana, D. Bulone, M. B. Palma-Vittorelli, M. U. Palma, V. D. Trivedi, S. F. Cheng, W. J. Chien, S. H. Yang, S. Francis, D. K. Chang, Renn Batra, Michael A. Geeves, Dietmar J. Manstein, Joanna Trvlska, Pawel Grochowski, Maciej Geller, K. Ginalski, P. Grochowski, B. Lesyng, P. Lavalette, Y. Blouquit, D. Roccatano, A. Amadei, A. Di Nola, H. J. C. Berendsen, Bosco Ho, P. M. G. Curmi, H. Berry, D. Lairez, E. Pauthe, J. Pelta, V. Kothekar, Shakti Sahi, M. Srinivasan, Anil K. Singh, Kartha S. Madhusudnan, Fateh S. Nandel, Harpreet Kaur, Balwinder Singh, D. V. S. Jain, K. Anton Feenstra, Herman J. C. Berendsen, F. Tama, Y. -H. Sanejouand, N. Go, Deepak Sharma, Sunita Sharma, Santosh Pasha, Samir K. Brahmachari, R. Viiavaraghavan, Jyoti Makker, Sharmisllia Dey, S. Kumar, G. S. Lakshmikanth, G. Krishnamoorthy, V. M. Mazhul, E. M. Zaitseva, Borys Kierdaszuk, J. Widengren, B. Terry, Ü. Mets, R. Rigler, R. Swaminathan, S. Thamotharan, N. Yathindra, Y. Shibata, H. Chosrowjan, N. Mataga, I. Morisima, Tania Chakraharty, Ming Xiao, Roger Cooke, Paul Selvin, C. Branca, A. Faraone, S. Magazù, G. Maisano, P. Migliardo, V. Villari, Digambar V. Behere, M. Sharique Zahida Waheed Deva, M. Brunori, F. Cutruzzolà, Q. H. Gibson, C. Savino, C. Travaglini-Allocatelli, B. Vallone, Swati Prasad, Shyamalava Mazumdar, Samaresh Mitra, P. Soto, R. Fayad, I. E. Sukovataya, N. A. Tyulkova, Sh. V. Mamedov, B. Aktas, M. Canturk, B. Aksakal, R. Yilgin, K. I. Bogutska, N. S. Miroshnichenko, S. Chacko, M. DiSanto, J. A. Hypolite, Y-M. Zheng, A. J. Wein, M. Wojciechowski, T. Grycuk, J. Antosiewicz, Marc A. Ceruso, Alfredo Di Nola, Subhasis Bandvopadhvay, Bishnu P. Chatterjee, Devapriva Choudhury, Andrew Thompson, Vivian Stojanoff, Jerome Pinkner, Scott Hultgren, Stefan Khight, Delphine Flatters, Julia Goodfellow, Fumi Takazawatt, Minoru Kanehisa, Masaki Sasai, Hironori Nakamura, Wang Bao Han, Yuan Zheng, Wang Zhi Xin, Pan xin Min, Vlnod Bhakuni, Sangeeta Kulkarni, Atta Ahmad, Koodathingal Prakash, Shashi Prajapati, Alexey Surin, Tomoharu Matsumoto, Li Yang, Yuki Nakagawa, Kazumoto Kimura, Yoshiyuki Amemiya, Gennady V. Semisotnov, Hiroshi Kihara, Saad Tayyab, Salman Muzammil, Yogesh Kumar, Vinod Bhakuni, Monica Sundd, Suman Kundu, M. V. Jagannadham, Medicherla V. Jagannadham, Bina Chandani, Ruby Dhar, Lalankumar Sinha, Deepti Warrier, Sonam Mehrotra, Purnima Khandelwal, Subhendu Seth, Y. U. Sasidhar, C. Ratna Prabha, Arun Gidwani, K. P. Madhusudan, Akira R. Kinjo, Ken Nishikawa, Suvobrata Chakravarty, Raghavan Varadarajan, K. Noyelle, P. Haezebrouck, M. Joniau, H. Van Dael, Sheffali Dash, Indra Brata Jha, Rajiv Bhat, Prasanna Mohanty, A. K. Bandyopadhyay, H. M. Sonawat, Ch. Mohan Rao, Siddhartha Datta, K. Rajaraman, B. Raman, T. Ramakrishna, A. Pande, J. Pande, S. Betts, N. Asherie, O. Ogun, J. King, G. Benedek, I. V. Sokolova, G. S. Kalacheva, Masashi Sonoyama, Yasunori Yokoyama, Kunihiro Taira, Shigeki Mitaku, Chicko Nakazawal, Takanori Sasakil, Yuri Mukai, Naoki Kamo, Seema Dalal, Lynne Regan, Shigeki Mituku, Mihir Roychoudhury, Devesh Kumar, Dénes Lőrinczv, Franciska Könczöl, László Farkas, Joseph Belagyi, Christoph Schick, Christy A. Thomson, Vettai S. Ananthanarayanan, E. G. Alirzayeva, S. N. Baba-Zade, M. Michael Gromiha, M. Oobatake, H. Kono, J. An, H. Uedaira, A. Sarai, Kazufumi Takano, Yuriko Yamagata, Katsuhide Yutani, Gouri S. Jas, Victor Muñoz, James Hofrichter, William A. Eaton, Jonathan Penoyar, Philip T. Lo Verde, J. Kardos, Á. Bódi, I. Venekei, P. Závodszky, L. Gráf, András Szilágyi, Péter Závodszky, R. D. Allan, J. Walshaw, D. N. Woolfson, Jun Funahashi, Savan Gupta, M. Mangoni, P. Roccatano, Gosu Ramachandraiah, Nagasuma R. Chandra, Barbara Ciani, Derek N. Woolfson, Usha B. Nair, Kanwal J. Kaur, Dinakar M. Salunke, Chittoor P. Swaminathan, Avadhesha Surolia, A. Pramanik, P. Jonasson, G. Kratz, O. T. Jansson, P. -Å. Nygren, S. Ståhl, K. Ekberg, B. -L. Johansson, S. Uhlén, M. Uhlén, H. Jörnvall, J. Wahren, Karin Welfle, Rolf Misselwitz, Wolfgang Höhne, Heinz Welfle, L. G. Mitskevich, N. V. Fedurkina, B. I. Kurganov, Gotam K. Jarori, Haripada Maity, J. Guharay, B. Sengupta, P. K. Sengupta, K. Sridevi, S. R. Kasturi, S. P. Gupta, Gunjan Agarwal, Suzanne Kwong, Robin W. Briehl, O. I. Ismailova, N, A. Tyulkova, C. Hariharan, D. Pines, E. Pines, M. Zamai, R. Cohen-Luria, A. Yayon, A. H. Parola, M. J. Padya, G. A. Spooner, D. N. Woolfeon, Panchan Bakshi, D. K. Bharadwaj, U. Sharma, N. Srivastava, R. Barthwal, N. R. Jagannathan, Keiko Matsuda, Takaaki Nishioka, Nobuhiro Go, T. Aita, S. Urata, Y. Husimi, Mainak Majumder, Nicola G. A. Abrescia, Lucy Malinina, Juan A. Subirana, Juan Aymami, Ramón Eritxa, Miquel Coll, B. J. Premraj, R. Thenmalarchelvi, P. Satheesh Kumar, N. Gautham, Lou -Sing Kan, null Ming-Hou, Shwu-Bin Lin, Tapas Sana, Kanal B. Roy, N. Bruant, D. Flatters, R. Lavery, D. Genest, Remo Rons, Heinz Sklenar, Richard Lavery, Sudip Kundu, Dhananjay Bhattacharyya, Debashree Bandyopadhyay, Ashoke Ranjan Thakur, Rabi Majumdar, F. Barceló, J. Portugal, Sunita Ramanathan, B. J. Rao, Mahua Gliosli, N. Vinay Kumar, Umesh Varshney, Shashank S. Pataskar, R. Sarojini, S. Selvasekarapandian, P. Kolandaivel, S. Sukumar, P. Kolmdaivel, Motilal Maiti, Anjana Sen, Suman Das, Elisa Del Terra, Chiara Suraci, Silvia Diviacco, Franco Quadrifoglio, Luigi Xodo, Arghya Ray, G. Karthikeyan, Kandala V. R. Chary, Basuthkar J. Rao, Anwer Mujeeb, Thomas L. James, N. Kasyanenko, E. E. F. Haya, A. Bogdanov, A. Zanina, M. R. Bugs, M. L. Cornélio, M. Ye. Tolstorukov, Nitish K. Sanval, S. N. Tiwari, Nitish K. Sanyal, Mihir Roy Choudhury, P. K. Patel, Neel S. Bhavesh, Anna Gabrielian, Stefan Wennmalm, Lars Edman, Rudolf Rigler, B. Constantinescu, L. Radu, I. Radulcscu, D. Gazdaru, Sebastian Wärmländer, Mikael Leijon, Setsuyuki Aoki, Takao Kondo, Masahiro Ishiura, V. A. Pashinskaya, M. V. Kosevich, V. S. Shelkovsky, Yu. P. Blagoy, Ji-hua Wang, R. Malathi, K. Chandrasekhar, E. R. Kandimalla, S. Agrawal, V. K. Rastogi, M. Alcolea Palafox, Chatar Singh, A. D. Beniaminov, S. A. Bondarenko, E. M. Zdobnov, E. E. Minyat, N. B. Ulyanov, V. I. Ivanov, J. S. Singh, Kailas D. Sonawane, Henri Grosjean, Ravindra Tewari, Uddhavesh B. Sonavane, Annie Morin, Elizabeth A. Doherty, Jennifer A. Doudna, H. Tochio, S. Sato, H. Matsuo, M. Shirakawa, Y. Kyogoku, B. Javaram, Surjit B. Dixit, Piyush Shukla, Parul Kalra, Achintya Das, Kevin McConnell, David L. Beveridge, W. H. Sawyer, R. Y. S. Chan, J. F. Eccelston, Yuling Yan, B. E. Davidson, Eimer Tuite, Bengt Norden, Peter Nielsen, Masayuki Takahashi, Anirban Ghosh, Manju Bansal, Frauke Christ, Hubert Thole, Wolfgang Wende, Alfred Pingoud, Vera Pingoud, Pratibha Mehta Luthra, Ramesh Chandra, Ranjan Sen, Rodney King, Robert Weisberg, Olaf F. A. Larsen, Jos Berends, Hans A. Heus, Cornelis W. Hilbers, Ivo H. M. van Stokkum, Bas Gobets, Rienk van Grondelle, Herbert van Amerongen, HE. Sngrvan, Yu. S. Babayan, N. V. Khudaverdian, M. Gromiha, F. Pichierri, M. Aida, P. Prabakaran, K. Sayano, Saulius Serva, Eglė Merkienė, Giedrius Vilkaitis, Elmar Weinhold, Saulius Klimašauskas, Eleonora Marsich, Antonella Bandiera, Giorgio Manzini, G. Potikyan, V. Arakelyan, Yu. Babayan, Alex Ninaber, Julia M. Goodfellow, Yoichiro Ito, Shigeru Ohta, Yuzuru Husimi, J. Usukura, H. Tagami, H. Aiba, Mougli Suarez, Elia Nunes, Deborah Keszenman, E. Carmen Candreva, Per Thyberg, Zeno Földes-Papp, Amita Joshi, Dinesh Singh, M. R. Rajeswari, null Ira, M. Pregetter, H. Amenitsch, J. Chapman, B. N. Pandev, K. P. Mishra, E. E. Pohl, J. Sun, I. I. Agapov, A. G. Tonevitsky, P. Pohl, S. M. Dennison, G. P. Gorbeako, T. S. Dynbko, N. Pappavee, A. K. Mishra, Prieto Manuel, Almeida Rodrigo, Loura Luis, L. Ya. Gendel, S. Przestalski, J. Kuczera, H. Kleszczyńska, T. Kral, E. A. Chernitsky, O. A. Senkovich, V. V. Rosin, Y. M. Allakhverdieva, G. C. Papageorgiou, R. A. Gasanov, Calin Apetrei, Tudor Savopol, Marius Balea, D. Cucu, D. Mihailescu, K. V. Ramanathan, Goran Bačić, Nicolas Sajot, Norbert Garnier, Serge Crouzy, Monique Genest, Z. S. Várkonyi, O. Zsiros, T. Farkas, Z. Combos, Sophie Cribier, I. F. Fraceto, S. Schreier, A. Spisni, F. de Paula, F. Sevšek, G. Gomišček, V. Arrigler, S. Svetina, B. Žekš, Fumimasa Nomura, Miki Nagata, Kingo Takiguchi, Hirokazu Hotani, Lata Panicker, P. S. Parvathanathan, A. Ishino, A. Saitoh, H. Hotani, K. Takiguchi, S. Afonin, A. Takahashi, Y. Nakato, T. Takizawa, Dipti Marathe, Kent Jørgensen, Satinder S. Rawat, R. Rukmini, Amitabha Chattopadhyay, M. Šentiurc, J. Štrancar, Z. Stolič, K. Filipin, S. Pečar, S. C. Biswas, Satyen Sana, Anunay Samanta, Koji Kinoshita, Masahito Yamazaki, Tetsuhiko Ohba, Tai Kiuchi, null Yoshitoshi, null Kamakura, Akira Goto, Takaaki Kumeta, Kazuo Ohki, I. P. Sugar, T. E. Thompson, K. K. Thompson, R. L. Biltonen, Y. Suezaki, H. Ichinose, M. Akivama, S. Matuoka, K. Tsuchihashi, S. Gasa, P. Mattjus, J. G. Molotkovsky, H. M. Pike, R. E. Brown, Ashish Arora, Jörg H. Kleinschmidt, Lukas K. Tamm, O. G. Luneva, K. E. Kruglyakova, V. A. Fedin, O. S. Kuptsoya, J. W. Borst, N. V. Visser, A. J. W. G. Visser, T. S. Dyubko, Toshihiko Ogihara, Kiyoshi Mishima, A. L. Shvaleva, N. Č. Radenović, P. M. Minić, M. G. Jeremić, Č. N. Radenović, T. F. Aripov, E. T. Tadjibaeva, O. N. Vagina, M. V. Zamaraeva, B. A. Salakhutdinov, A. Cole, M. Poppofl, C. Naylor, R. Titball, A. K. Basak, J. T. Eaton, C. E. Naylor, N. Justin, D. S. Moss, R. W. Titball, F. Nomura, M. Nagata, S. Ishjkawa, S. Takahashi, Kaoru Obuchi, Erich Staudegger, Manfred Kriechbaum, Robert I. Lehrer, Alan J. Waring, Karl Lohner, Susanne Gangl, Bernd Mayer, Gottfried Köhler, J. Shobini, Z. Guttenberg, B. Lortz, B. Hu, E. Sackmann, N. M. Kozlova, L. M. Lukyanenko, A. N. Antonovich, E. I. Slobozhanina, Andrey V. Krylov, Yuri N. Antonenko, Elena A. Kotova, Alexander A. Yaroslavov, Subhendu Ghosh, Amal K. Bera, Sudipto Das, Eva Urbánková, Masood Jelokhani-Niaraki, Karl Freeman, Petr Jezek, P. B. Usmanov, A. Ongarbaev, A. K. Tonkikh, Peter Pohl, Sapar M. Saparov, P. Harikumar, J. P. Reeves, S. Rao, S. K. Sikdar, A. S. Ghatpande, C. Corsso, A. C. Campos de Carvalho, W. A. Varanda, C. ElHamel, E. Dé, N. Saint, G. Molle, Anurae Varshney, M. K. Mathew, E. Loots, E. Y. Isacoff, Michiki Kasai, Naohiro Yamaguchi, Paramita Ghosh, Joseph Tigyi, Gabor Tigyi, Karoly Liliom, Ricardo Miledi, Maja R. Djurisic, Pavle R. Andjus, Indira H. Shrivastava, M. S. P. Sansom, C. Barrias, P. F. Oliveira, A. C. Mauricio, A. M. Rebelo da Costa, I. A. Lopes, S. V. Fedorovich, V. S. Chubanov, M. V. Sholukh, S. V. Konev, N. Fedirko, V. Manko, M. Klevets, N. Shvinka, B. S. Prabhananda, Mamata H. Kombrabail, S. Aravamudhan, Berenice Venegas-Cotero, Ivan Ortega Blake, Zhi-hong Zhang, Xiao-jian Hu, Han-qing Zhou, Wei-ying Cheng, Hang-fang Feng, L. O. Dubitsky, L. S. Vovkanvch, I. A. Zalyvsky, E. Savio-Galimberti, P. Bonazzola, J. E. Ponce-Homos, Mario Parisi, Claudia Capurro, Roxana Toriano, Laxma G. Ready, Larry R. Jones, David D. Thomas, B. A. Tashmukhamedov, B. T. Sagdullaev, D. Heitzmann, R. Warth, M. Bleich, R. Greger, K. T. G. Ferreira, H. G. Ferreira, Orna Zagoory, Essa Alfahel, Abraham H. Parola, Zvi Priel, H. Hama-Inaba, R. Wang, K. Choi, T. Nakajima, K. Haginoya, M. Mori, H. Ohyama, O. Yukawa, I. Hayata, Nanda B. Joshi, Sridhar K. Kannurpatti, Preeti G. Joshi, Mau Sinha, Xun Shen, Tianhui Hu, Ling Bei, Menno L. W. Knetsch, Nicole Schäfers, John Sandblom, Juris Galvanovskis, Roxana Pologea-Moraru, Eugenia Kovacs, Alexandra Dinu, S. H. Sanghvi, V. Jazbinšek, G. Thiel, W. Müller, G. Wübeller, Z. Tronteli, Leš Fajmut, Marko Marhl, Milan Brumen, I. D. Volotovski, S. G. Sokolovski, M. R. Knight, Alexei N. Vasil’ev, Alexander V. Chalyi, P. Sharma, P. J. Steinbach, M. Sharma, N. D. Amin, J. Barchir, R. W. Albers, H. C. Pant, M. Balasubramanyam, M. Condrescu, J. P. Gardner, Shamci Monajembashi, Gotz Pilarczyk, K. O. Greulich, F. M. El-Refaei, M. M. Talaat, A. I. El-Awadi, F. M. Ali, Ivan Tahradník, Jana Pavelková, Alexandra Zahradniková, Boris S. Zhorov, Vettai S. Ananthanaravanan, M. Ch. Michailov, E. Neu, W. Seidenbusch, E. Gornik, D. Martin, U. Welscher, D. G. Weiss, B. R. Pattnaik, A. Jellali, V. Forster, D. Hicks, J. Sahel, H. Dreyfus, S. Picaud, Hong-Wei Wang, Sen-fang Sui, Pradeep K. Luther, John Barry, Ed Morris, John Squire, C. Sivakama Sundari, D. Balasubramanian, K. Veluraia, T. Hema Thanka Christlet, M. Xavier Suresh, V. Laretta-Garde, Dubravka Krilov, Nataša Stojanović, Janko N. Herak, Ravi Jasuja, Maria Ivanova, Rossen Mirchev, Frank A. Ferrone, David Stopar, Ruud B. Spruijt, Cor J. A. M. Wolfs, Marcus A. Hemminga, G. Arcovito, M. De Spirito, Rajendra K. Agrawal, Amy B. Heagle, Pawel Penczek, Robert Grassucci, Joachim Frank, Manjuli R. Sharma, Loice H. Jeyakumar, Sidney Fleischer, Terence Wagenknecht, Carlo Knupp, Peter M. G. Munro, Eric Ezra, John M. Squire, Koji Ichihara, Hidefumi Kitazawa, Yusuke Iguchi, Tomohiko J. Itoh, Greta Pifat, Marina Kveder, Slavko Pečar, Milan Schara, Deepak Nair, Kavita Singh, Kanury V. S. Rao, Kanwaljeet Kaur, Deepti Jain, B. Sundaravadivel, Manisha Goel, D. M. Salunke, E. I. Kovalenko, G. N. Semenkova, S. N. Cherenkevich, T. Lakshmanan, D. Sriram, S. Srinivasan, D. Loganathan, T. S. Ramalingam, J. A. Lebrón, P. J. Bjorkman, A. K. Singh, T. N. Gayatri, Ernesto R. Caffarena, J. Raul Grigera, Paulo M. Bisch, V. Kiessling, P. Fromherz, K. N. Rao, S. M. Gaikwad, M. I. Khan, C. G. Suresh, P. Kaliannan, M. Elanthiraiyan, K. Chadha, J. Payne, J. L. Ambrus, M. P. N. Nair, Madhavan P. N. Nair, S. Mahajan, K. C. Chadha, R. Hewitt, S. A. Schwartz, J. Bourguignon, M. Faure, C. Cohen-Addad, M. Neuburger, R. Ober, L. Sieker, D. Macherel, R. Douce, D. S. Gurumurthy, S. Velmurugan, Z. Lobo, Ratna S. Phadke, Prashant Desai, I. M. Guseinova, S. Yu. Suleimanov, I. S. Zulfugarov, S. N. Novruzova, J. A. Aliev, M. A. Ismayilov, T. V. Savchenko, D. R. Alieva, Petr Ilík, Roman Kouřil, Hana Bartošková, Jan Nauš, Jvoti U. Gaikwad, Sarah Thomas, P. B. Vidyasagar, G. Garab, I. Simidjiev, S. Rajagopal, Zs. Várkonyi, S. Stoylova, Z. Cseh, E. Papp, L. Mustárdy, A. Holzenburg, R. Bruder, U. K. Genick, T. T. Woo, D. P. Millar, K. Gerwert, E. D. Getzoff, Tamás Jávorfí, Győző Garab, K. Razi Naqvi, Md. Kalimullah, Jyoti Gaikwad, Manoj Semwal, Roman Kouril, Petr Ilik, Man Naus, István Pomozi, Gábor Horváth, Rüdiger Wehner, Gary D. Bernard, Ana Damjanović, Thorsten Ritz, Klaus Schulten, Wang Jushuo, Shan Jixiu, Gong Yandao, Kuang Tingyun, Zhao Nanming, Arvi Freiberg, Kõu Timpmann, Rein Ruus, Neal W. Woodbury, E. V. Nemtseva, N. S. Kudryasheva, A. G. Sizykh, V. N. Shikhov, T. V. Nesterenko, A. A. Tikhomirov, Giorgio Forti, Giovanni Finazzi, Alberto Furia, Romina Paola Barbagallo, S. Iskenderova, R. Agalarov, R. Gasanov, Miyashita Osamu, G. O. Nobuhiro, R. K. Soni, M. Ramrakhiani, Hiromasa Yagi, Kacko Tozawa, Nobuaki Sekino, Tomoyuki Iwabuchi, Masasuke Yoshida, Hideo Akutsu, A. V. Avetisyan, A. D. Kaulen, V. P. Skulachev, B. A. Feniouk, Cécile Breyton, Werner Kühlbrandt, Maria Assarsson, Astrid Gräslund, G. Horváth, B. Libisch, Z. Gombos, N. V. Budagovskaya, N. Kudryasheva, Erisa Harada, Yuki Fukuoka, Tomoaki Ohmura, Arima Fukunishi, Gota Kawai, Kimitsuna Watanabe, Jure Derganc, Bojan Božič, Saša Svetina, Boštjan Žekš, J. F. Y. Hoh, Z. B. Li, G. H. Rossmanith, E. L. de Beer, B. W. Treijtel, P. L. T. M. Frederix, T. Blangè, S. Hénon, F. Galtet, V. Laurent, E. Planus, D. Isabey, L. S. Rath, P. K. Dash, M. K. Raval, C. Ramakrishnan, R. Balaram, Milan Randic, Subhash C. Basak, Marjan Vracko, Ashesh Nandy, Dragan Amic, Drago Beslo, Sonja Nikolic, Nenad Trinajstic, J. Walahaw, Marc F. J. Lensink, Boojala V. B. Reddy, Ilya N. Shindylov, Philip E. Bourne, M. C. Donnamaria, J. de Xammar Oro, J. R. Grigera, Monica Neagu, Adrian Neagu, Matej Praprotnik, Dušanka Janežič, Pekka Mark, Lennart Nilsson, L. La Fata, Laurent E. Dardenne, Araken S. Werneck, Marçal de O. Neto, N. Kannan, S. Vishveshwara, K. Veluraja, Gregory D. Grunwald, Alexandra T. Balaban, Kanika Basak, Brian D. Gute, Denise Mills, David Opitz, Krishnan Balasubramanian, G. I. Mihalas, Diana Lungeanu, G. Macovievici, Raluca Gruia, C. Cortez-Maghelly, B. Dalcin, E. P. Passos, S. Blesic, M. Ljubisavljevic, S. Milosevic, D. J. Stratimirovic, Nandita Bachhawat, Shekhar C. Mande, A. Nandy, Ayumu Saito, Koichi Nishigaki, Mohammed Naimuddin, Takatsugu Hirokawa, Mitsuo Ono, Hirotomo Takaesu, M. I. El Gohary, Abdalla S. Ahmed, A. M. Eissa, Hiroshi Nakashima, G. P. S. Raghava, N. Kurgalvuk, O. Goryn, Bernard S. Gerstman, E. V. Gritsenko, N. N. Remmel, O. M. Maznyak, V. A. Kratasyuk, E. N. Esimbekova, D. Tchitchkan, S. Koulchitsky, A. Tikhonov, A. German, Y. Pesotskaya, S. Pashkevich, S. Pletnev, V. Kulchitsky, Umamaheswar Duvvuri, Sridhar Charagundla, Rahim Rizi, John S. Leigh, Ravinder Reddy, Mahesh Kumar, O. Coshic, P. K. Julka, O. K. Rath, NR. Jagannathan, Karina Roxana Iliescu, Maria Sajin, Nicolcta Moisoi, Ileana Petcu, A. I. Kuzmenko, R. P. Morozova, I. A. Nikolenko, G. V. Donchenko, M. K. Rahman, M. M. Ahmed, Takehiro Watanabe, Y. Rubin, H. Gilboa, R. Sharony, R. Ammar, G. Uretzky, M. Khubchandani, H. N. Mallick, V. Mohan Kumar, Arijitt Borthakur, Erik M. Shapiro, M. Gulnaz Begum, Mahaveer N. Degaonkar, S. Govindasamy, Ivan Dimitrov, T. A. Kumosani, W. Bild, I. Stefanescu, G. Titescu, R. Iliescu, C. Lupusoru, V. Nastasa, I. Haulica, Gopal Khetawat, N. Faraday, M. Nealen, S. Noga, P. F. Bray, T. V. Ananieva, E. A. Lycholat, MV. Kosevich, S. G. Stepanyan, S. V. Antonyuk, R. Khachatryan, H. Arakelian, A. Kumar, S. Ayrapetyan, V. Mkheyan, S. Agadjanyan, A. Khachatryan, S. S. Rajan, V. Kabaleeswaran, Geetha Gopalakrishnan, T. R. Govindachari, Meera Ramrakhiani, Phillip Lowe, Andrew Badley, David C. Cullen, H. Hermel, W. Schmahl, H. Möhwald, Nirmalya Majumdar, Joydip Das, András Dér, Loránd Kelemen, László Oroszi, András Hámori, Jeremy J. Ramsden, Pál Ormos, D. Savitri, Chanchal K. Mitra, Toshio Yanagida, Seiji Esaki, Yuji Kimura, Tomoyuki Nishida, Yosiyuki Sowa, M. Radu, V. K. Koltover, Ya. I. Estrin, L. A. Kasumova, V. P. Bubnov, E. E. Laukhina, Rajiv Dotta, M. Degaonkar, P. Raghunathan, Rama Jayasundar, Pavel Novák, Milan Marko, Ivan Zahradník, Hiroaki Hirata, Hidetake Miyata, J. Balaji, P. Sengupta, S. Maiti, M. Gonsalves, A. L. Barker, J. V. Macpherson, D. O’Hare, C. P. Winlove, P. R. Unwin, R. Phillip, S. Banerjee, G. Ravindra Kumar, K. Nagayaka, R. Danev, S. Sugitani, K. Murata, Michael Gősch, H. Blom, P. Thyberg, Z. Földes-Papp, G. Björk, J. Holm, T. Heino, Masashi Yokochi, Fuyuhiko Inagaki, Masami Kusunoki, E. K. Matthews, J. Pines, Yu. P. Chukova, Vitaly K. Koltover, Geetanjali Bansal, Uma Singh, M. P. Bansal, Kotoko Nakata, Tastuya Nakano, Tsuguchika Kaminuma, B. P. S. Kang, U. Singh, Bonn Kirn, Neja Potocnik, Vito Stare, Latal Shukla, V. Natarajan, T. P. A. Devasagayam, M. D. Sastry, P. C. Kesavan, R. Sayfutdinov, V. V. Adamovich, D. Yu. Rogozin, A. G. Degermendzhy, C. L. Khetrapal, G. A. Nagana Gowda, Kedar Nath Ghimire, Ishida Masaru, H. Fujita, S. Ishiwata, Y. Kishimoto, S. Kawahara, M. Suzuki, H. Mori, M. Mishina, Y. Kirino, H. Ohshima, A. S. Dukhin, V. N. Shilov, P. J. Goetz, and R. K. Mishra
- Subjects
0303 health sciences ,biology ,General Medicine ,010402 general chemistry ,01 natural sciences ,Horseradish peroxidase ,General Biochemistry, Genetics and Molecular Biology ,0104 chemical sciences ,03 medical and health sciences ,Biochemistry ,Manganese porphyrin ,biology.protein ,Enzyme reconstitution ,General Agricultural and Biological Sciences ,030304 developmental biology - Published
- 1999
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7. Effect of the secondary structure of poly-L-lysine on the adsorption at the water/dodecane interface
- Author
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H. Hermel and Reinhard Miller
- Subjects
Circular dichroism ,Aqueous solution ,Chromatography ,Polymers and Plastics ,Dodecane ,Random coil ,Surface tension ,chemistry.chemical_compound ,Colloid and Surface Chemistry ,Adsorption ,chemistry ,Chemical engineering ,Materials Chemistry ,Molecule ,Physical and Theoretical Chemistry ,Protein secondary structure - Abstract
The adsorption of poly-L-lysine of different conformation (α-helix, β-sheet and random coil) at the water/dodecane interface has been studied by interfacial tension measurements using the drop volume method. The experimental adsorption isotherms provide information about a critical aggregation concentration, the maximum interfacial tension depressionΔγmax and the minimum area A occupied by adsorbed molecules at the interface. Differences inΔγmax exist between α-helix and β-sheet and, moreover, in the area values between random-coil on the one side and α-helix and β-sheet on the other hand.
- Published
- 1995
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8. On the relation between the molecular mass distribution of gelatin and its ability to stabilize emulsions
- Author
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H. J. Müller and H. Hermel
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Coalescence (physics) ,food.ingredient ,Polymers and Plastics ,Molecular mass ,Chemistry ,Dodecane ,Analytical chemistry ,Gelatin ,Gel permeation chromatography ,chemistry.chemical_compound ,Colloid and Surface Chemistry ,food ,Oil droplet ,Emulsion ,Materials Chemistry ,Molar mass distribution ,Physical and Theoretical Chemistry - Abstract
The relation between the molecular mass distribution of gelatin and its effectiveness in stabilizing emulsions of dibutyl phthalate and dodecane in water have been investigated. The molecular mass distribution was determined using gel permeation chromatography. The ability of gelatin samples to stabilize emulsions was investigated by observing the coalescence of macroscopic oil droplets in a special device. The results show that all samples with a content of more than 30 wt.-% in the low-molecular mass range are good stabilizers, whereas the stabilizing ability is diminished drastically by decreasing the low molecular mass content below 30 wt.-%. Mechanisms for the stabilization and rupture of the thin water film between the oil droplets are discussed, especially in the case of gelatin adsorption layers at the film interfaces. A model is given for the qualitative explanation of the dependence of the stabilizing ability of gelatins on the molecular mass distribution.
- Published
- 1994
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9. Water-dependent matrix orientation in thin gelatin layers
- Author
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H. Hermel and A. Seeboth
- Subjects
Materials science ,food.ingredient ,Metals and Alloys ,Mineralogy ,Surfaces and Interfaces ,Orientation (graph theory) ,Gelatin ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,Matrix (mathematics) ,food ,Materials Chemistry ,Composite material ,Layer (electronics) ,Water content - Abstract
Thin gelatin layers form a matrix with fibrils of preferred orientation. This orientation depends on the thickness of the layer. Moreover, the moisture content in the nominally dry layers varies according to their thickness. These correlations are discussed.
- Published
- 1993
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10. Protein-dispersed liquid crystals
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A. Seeboth and H. Hermel
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food.ingredient ,Chromatography ,Polymers and Plastics ,Chemistry ,Supramolecular chemistry ,General Chemistry ,Gelatin ,Surfaces, Coatings and Films ,food ,Molecular level ,Chemical engineering ,Liquid crystal ,Phase (matter) ,Gelatin matrix ,Materials Chemistry ,Molecule ,Triple helix - Abstract
Nematic liquid crystals (LC) were embedded in a highly structured gelatin film as the discrete phase in the form of droplets. Thereby, the gelatin matrix forces a preferred orientation of the LC molecules in the droplets, initiated by the interaction between the triple helices of gelatin and the LC at the interface protein/LC. This is explained on a molecular level by the formation of a supramolecular structure at the interface, which is a germ for the continued preferred orientation of the mesogenes inside the droplets.
- Published
- 1992
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11. Photochemically Induced Modification of Polymer Dispersed Liquid Crystals with Photochromic Stilbene. Photoreactions in Liquid Crystals (Part 8)
- Author
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H. Hermel, J. Stumpe, O. Zaplo, and A. Seeboth
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chemistry.chemical_classification ,Materials science ,food.ingredient ,Doping ,Polymer ,Condensed Matter Physics ,Photochemistry ,Gelatin ,Cis trans isomerization ,Photochromism ,food ,chemistry ,Liquid crystal ,Stilbene dye ,Photosensitive polymer - Abstract
Photosensitive polymer dispersed liquid crystals (PDLC) were prepared using the nematic mixture E-5 doped with 2 wt-% photochromic stilbene dye in a gelatin binder. The stilbene undergoes E-Z photo...
- Published
- 1992
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12. Thermal behaviour and structure of gelatin layers with embedded liquid crystals
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H. Hermel, A. Seeboth, and G. Kretzschmar
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food.ingredient ,Materials science ,Chromatography ,Isotropy ,Metals and Alloys ,Mesophase ,Surfaces and Interfaces ,Gelatin ,Thermotropic crystal ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,food ,Chemical engineering ,Liquid crystal ,Phase (matter) ,Thermal ,Gelatin matrix ,Materials Chemistry - Abstract
Our investigations show that low molecular weight thermotropic liquid crystals (LCs) can be embedded as a separate phase in a gelatin matrix. The transition from the nematic mesophase into the isotropic phase for the encapsulated LC is determined by measuring the voltaic potential difference Δ V as a function of the temperature. The interactions between LC and gelatin have been investigated for both cold- and hot-dried gelatin layers and a satisfactory structure scheme is given. Furthermore, we also characterize the thermal behaviour of pure gelatin layers using the Δ V method.
- Published
- 1991
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13. Configuration transition in thin gelatin layers
- Author
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A. Seeboth and H. Hermel
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Materials science ,food.ingredient ,food ,Moisture ,Phase (matter) ,Mesogen ,Orientation (geometry) ,Molecule ,Composite material ,Layer (electronics) ,Gelatin ,Matrix (geology) - Abstract
By cold-drying thin gelatin layers form a matrix with triplehelical fibrils of preferred orientation. This orientation is variable and depends on the thickness of the layer. Indeed, this is no typical effect of the layer thickness, but it is related to the residual water content (moisture) in the nominally dry layers. These correlations are be discussed. The results are of interest for the orientation of the mesogenic phase of LC molecules dispersed as droplets in the gelatin layers.
- Published
- 2008
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14. Studies on Gelatin Crosslinked with Substituted Triazine
- Author
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H. Hermel and A. Jahn
- Subjects
food.ingredient ,Molecular mass ,General Arts and Humanities ,General Physics and Astronomy ,Alkylation ,Gelatin ,Viscosity ,chemistry.chemical_compound ,food ,chemistry ,Polymer chemistry ,medicine ,Swelling ,medicine.symptom ,Mass fraction ,Triazine - Abstract
The swelling of differently crosslinked gelatin layers, which were hardened with substituted triazines has been studied. Thereby a direct influence of the molecular mass distribution of gelatin could not be found, but an effect of the different numbers of N-terminal groups could be detected, using a low-molecular mass and a high-molecular mass fraction of the same gelatin. If the number of N-terminal groups was diminished by about 25%, by alkylation with a sulphobetaine, the differences in swelling disappeared. Furthermore, the alkylation reduces the brittleness of the gelatin layer and the interaction of the gelatin with hydtvphilic colour couplers (so-called coupler viscosity).
- Published
- 1992
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15. Moisture, Triple-Helical Content and Brittleness of Gelatin Layers
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H. Herbrich, C. Roth, H. Legutke, H. Hermel, E. Buderl, and R. Wetzel
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Lattice dynamics ,Materials science ,food.ingredient ,Moisture ,General Arts and Humanities ,General Physics and Astronomy ,Mineralogy ,engineering.material ,Gelatin ,Multiple layer ,food ,Brittleness ,engineering ,Biopolymer ,Elasticity (economics) ,Composite material ,Water content - Abstract
The triple-helical content of gelatin measured in dilute solution correlates with the brittleness of its cold-dried layer. The brittleness of the layer is low and, accordingly, its elasticity is high for a small triple-helical content of the gelatin and vice versa. This effect is discussed on the basis of the moisture in the gelatin layer. Triple-helical domains contain part of it as “structural” water. The residue is “layer” water which determines the elasticity of the gelatin layer.
- Published
- 1991
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16. A New Consideration of the Molecular Mass-Viscosity Correlation of Gelatin
- Author
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H.-J. Wappler and H. Hermel
- Subjects
Viscosity ,food.ingredient ,food ,Molecular mass ,Chemistry ,General Arts and Humanities ,Polymer chemistry ,Analytical chemistry ,General Physics and Astronomy ,Molecule ,Gelatin - Abstract
Differential series of extracted gelatin often have a different molecular mass-viscosity correlation, even if they are produced according to the same process. We have found indications of the molecular structure of the extracted gelatin from the easily measurable solution viscosity n and the weight average of the molecular mass Mw/n. Thereby, the differences in the Mw/n ratio between the different series can be explained.
- Published
- 1993
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17. The investigation of PD-L1 expression as a prognostic marker for uterine sarcoma.
- Author
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V. S. Sukhin, S. V. Danyliuk, O. N. Sukhina, A. V. Zadnepryanniy, D. Lindquist, H. Hermelin, and M. Tarján
- Subjects
саркома матки ,експресія пухлинного маркеру ,PD-L1 ,прогностичний фактор ,Biology (General) ,QH301-705.5 - Abstract
Background. The uterine sarcoma is a rare tumor with the unpredictable, aggressive clinical behavior. Medical science relies on the development of reliable tumor markers, on the basis of which the optimal treatment program can be chosen, and will be also possible to make a prognosis. The hyperexpression of PD-L1 in many cases correlates with unfavorable prognosis of the disease and is an important prognostic biomarker for some types of tumors: melanoma, kidney cancer, non-small cell lung cancer. The role of PD-L1 expression, as a tumor marker in sarcoma, remains unclear. Objective. The investigation of PD-L1 expression as a prognostic tumor marker for uterine sarcoma. Methods. There have been selected 30 uterine sarcoma patients stage I-II (T1-2NxM0), for immunohistochemistry analyze of PD-L1 expression. Depending on the morphological tumor types all the patients were distributed: leiomyosarcoma (LMS) - 20.0%, endometrial stromal sarcoma (ESS) - 46.7%, undifferentiated sarcoma (HC) - 33.3%. Results. Our results showed that 73.3 % of patients with uterine sarcoma exhibited low expression level of PD-L1. The moderate level and overexpression of PD-L1 were observed in undifferentiated and endometrial stromal sarcoma - 13.3 and 6.7 %, respectively. At further follow-up of patients with PD-L1 expression, the relapse of the disease was detected in 50.0 % of cases. Conclusion. The PD-L1 expression in tumor tissue, regardless of its level, is considered to be an unfavorable prognostic factor for uterine sarcoma patients. In case of moderate expression level of PD-L1, so as at its overexpression, the tumor progression was detected in 83.3% of uterine sarcoma patients.
- Published
- 2018
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18. The modification of the triple helical structure of gelatin in aqueous solution I. The influence of anionic surfactants, pH-value, and temperature
- Author
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R. Wüstneck, E. Buder, H. Hermel, and R. Wetzel
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chemistry.chemical_classification ,Circular dichroism ,food.ingredient ,Chromatography ,Aqueous solution ,Polymers and Plastics ,Chemistry ,Sodium ,Analytical chemistry ,chemistry.chemical_element ,Gelatin ,Colloid and Surface Chemistry ,food ,Materials Chemistry ,Physical and Theoretical Chemistry ,Protein secondary structure ,Alkyl ,Triple helix - Abstract
The modification of the triple helical structure in aqueous gelatin solutions by changing pH and adding alkyl sulphates at 298 K and after rechilling the solution to 283 K was investigated by CD-measurement. At 298 K the triple helical content at the IEP of the gelatin has its maximum value. It is only weakly affected by adding sodium dodecyl sulphate (SDDS) at concentrations
- Published
- 1988
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19. Beeinflussung der Oberfl�cheneigenschaften des Systems Gelatine + Tensid durch die Art der Gelatine
- Author
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H. Hermel, G. Kretzschmar, and R. Wüstneck
- Subjects
Colloid and Surface Chemistry ,Polymers and Plastics ,Chemistry ,Complex formation ,Polymer chemistry ,Materials Chemistry ,Physical and Theoretical Chemistry - Abstract
Adsorptionsschichten tensidmodifizierter Gelatinelosungen verschiedener Molmasseverteilung und unterschiedlichen Aschegehaltes wurden durch Messung der Oberflachenspannung und oberflachenrheologischer Kriechdeformationskurven charakterisiert. Die Oberflachenspannungsisothermen der Gelatinesysteme mit geringem Aschegehalt und einer engen Molmasseverteilung weisen bei Tensidkonzentrationen unterhalb der CMC der ionogenen Tenside einen Knickpunkt auf. Die ausgepragt viskoplastischen Eigenschaften der Phasengrenzschicht in diesem Bereich bestatigen die Existenz einer gesattigten Adsorptionsschicht, bestehend aus Gelatine-Tensid-Komplexen hoher Grenzflachenaktivitat. Die Konstanz der Oberflachenspannung bei gleichzeitigen geringem Abfall der Ober-flachenviskositat bei weiterer Erhohung der Tensidkonzentration weist einerseits auf die Komplexbildung nach einem diskreten Mechanismus und andererseits auf die Ausdehnung der Phasengrenzschicht in Bereiche der Subphase hin. Bei Tensidkonzentrationen oberhalb der CMC der Tenside erreicht die Oberflachenspannung Werte, die denen des gelatinefreien Tensidsystems entsprechen, verbunden mit einer Verringerung der Oberflachenviskositat um mehrere Grosenordnungen. Die Ergebnisse der Untersuchungen der Systeme, welche eine Gelatine mit einer breiten Molmasseverteilung bei gleichzeitig geringem Aschegehalt beinhalten, zeigen, das das maximale Bindungsvermogen der Gelatine von der Molmasseverteilung vernachlassigbar gering beeinflust wird. Demgegenuber weisen die Oberflachenspannungsisothermen fur die Ausbildung von Mehrfachgleichgewichten von Komplexen unterschiedlicher Grenflachenaktivitat charakteristische Anderungen des Kurvenverlaufs auf. Ein hoher Aschegehalt bewirkt eine Verschiebung der Oberflachenspannungsisotherme zu geringeren Tensidkonzentrationen. Im Bereich des Plateaus der Oberflachenspannungsisotherme und der maximalen Oberflachenviskositat kommt es bei Anwesenheit eines kationogenen Tensids zu einer Fallung unloslicher Komplexe. Die spezifische Wirkung des hohen Aschegehaltes entspricht der eines entsprechenden Elektrolytzusatzes.
- Published
- 1984
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20. The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of nonionic surfactants
- Author
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R. W�stneck, E. Buder, R. Wetzel, and H. Hermel
- Subjects
Colloid and Surface Chemistry ,Polymers and Plastics ,Materials Chemistry ,Physical and Theoretical Chemistry - Published
- 1989
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21. Conformations of different gelatins in solutions and in films an analysis of circular dichroism (CD) measurements
- Author
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R. Wetzel, A. Huttner, H. Hermel, and E. Buder
- Subjects
Circular dichroism ,food.ingredient ,Polymers and Plastics ,Chemistry ,Stereochemistry ,medicine.disease ,Gelatin ,Isothermal process ,Hysteresis ,Crystallography ,Colloid and Surface Chemistry ,food ,Materials Chemistry ,medicine ,Peptide bond ,Denaturation (biochemistry) ,Dehydration ,Physical and Theoretical Chemistry ,Triple helix - Abstract
The structural behaviour of gelatins from different raw materials and manufacturing processes at thermal denaturation and isothermal dehydration and rehydration is investigated by CD. At both thermal denaturation and isothermal dehydration with all gelatins examined, the triple helix content decreases. Simultaneously, the appearance of cis peptide bonds is observed. At rehydration, a structural hysteresis occurs, the reconstitution of the triple helix structure being correlated with a decrease in the content of cis peptide bonds. The possibility of the formation of chain reversals upon destruction of the triple helix is discussed.
- Published
- 1987
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22. Technologische Beeinflussung der Struktur und Eigenschaften von Glasfäden. Teil III: Porositäsuchungen an ausgelaugten Glasfäden
- Author
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H.‐J. Jacobasch, J. Seifert, H. Hermel, and R. Barthel
- Subjects
Polymers and Plastics ,Chemistry ,General Chemical Engineering - Published
- 1981
- Full Text
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23. The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of cationic surfactants
- Author
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R. Wüstneck, R. Wetzel, E. Buder, and H. Hermel
- Subjects
Ammonium bromide ,Circular dichroism ,food.ingredient ,Aqueous solution ,Polymers and Plastics ,Cationic polymerization ,Oligomer ,Gelatin ,chemistry.chemical_compound ,Colloid and Surface Chemistry ,food ,Pulmonary surfactant ,chemistry ,Polymer chemistry ,Materials Chemistry ,Organic chemistry ,Coagulation (water treatment) ,Physical and Theoretical Chemistry - Abstract
The interaction between cationic surfactants (hexadecyl and dodecyl trimethyl ammonium bromide) and gelatin was characterized by measuring the circular dichroism. The interaction between the cationic surfactants and gelatin is weak in comparison to that of anionic surfactants. When the concentration of cationic surfactants is sufficiently low, refolding of the gelatin-strands to the triple helical structure by rechilling the solution from 298 K to 283 K is complete. The triple helical content of the solution is affected more strongly by the cationic surfactants in acidic solution than at pHs 7 or 10. The interaction depends on the apolar group of the surfactant and is found to be stronger for DTAB than for CTAB at 298 K. Coagulation of the hydrophobic gelatin-cationic surfactant complexes does not comprise that pan of gelatin which is able to refold the triple helical structure. Therefore, the gelatin-strands of lower molecular weights are thought to react favorably with the surfactant ions.
- Published
- 1989
- Full Text
- View/download PDF
24. Eine Methode zur Isolierung von Katalase aus Rinderleber ohne Anwendung organischer Lösungsmittel
- Author
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H. Schiller, H. Hermel, and R. Havemann
- Subjects
Physical and Theoretical Chemistry - Published
- 1960
- Full Text
- View/download PDF
25. Über den mechanismus der katalase-wasserstoffperoxid-reaktion II. Die aktivitätszentren der katalase und ihre wirkungs-weise
- Author
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H. Hermel and R. Havemann
- Subjects
biology ,Inorganic chemistry ,chemistry.chemical_element ,Biochemistry ,Medicinal chemistry ,Redox ,Peroxide ,Oxygen ,Dissociation (chemistry) ,Cofactor ,chemistry.chemical_compound ,chemistry ,Catalase ,biology.protein ,Hydroxide ,Heme - Abstract
1. 1. Besides the prosthetic groups, disulfide, sulfhydryl and basic groups in the protein component of catalase are active centers for the reaction with H 2 O 2 . The disulfide and sulfhydryl groups behave as a redox system acting upon H 2 O 2 . The basic groups interact with the prosthetic groups. This influences the binding strength of the peroxide, which is combined with the Fe + of the prosthetic group. It is discussed which groups in the protein component could be responsible for the heme-protein interaction. 2. 2. The actual activity of catalase may be derived from the measured activity-pH relationship by elimination of the five intermediate equilibria. These are: the dissociation of peroxide, the dissociation of catalase hydroxide, the dissociation of catalase peroxide, the pH dependence of the redox potential and the pH dependence of latent sulfhydryl groups. The actual catalase activity is pH dependent because of heme-protein interaction. 3. 3. With the help of these results the fundamental mechanism of the catalatic reaction may be explained. The oxidation of peroxide to oxygen by the disulfide bridges of catalase is the rate-determining process, the peroxide being combined with the Fe of the heme group. The reaction velocity depends upon the size of the catalase redox potential and the strength of the heme-protein interaction. Values for the magnitude of these quantities are presented
- Published
- 1966
- Full Text
- View/download PDF
26. Über den mechanismus der katalase-wasserstoffperoxid-reaktion I. Der disulfid- und sulfhydrylgehalt der rinderleber-katalase
- Author
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H. Hermel and R. Havemann
- Subjects
biology ,Stereochemistry ,Biochemistry ,Medicinal chemistry ,Cofactor ,Dissociation (chemistry) ,Enzyme assay ,Dissociation constant ,chemistry.chemical_compound ,chemistry ,Catalase ,Oxidizing agent ,biology.protein ,Titration ,Azide - Abstract
1. 1. The amperometrically titratable disulfide and sulfhydryl content of beef-liver catalase is not constant. It changes with enzyme activity, pH and after the action of weak oxidizing agents. As a rule, the ratio disulfide: sulfhydryl increases with increasing enzyme activity. With variation of pH latent sulfhydryl groups are released, and free sulfhydryl groups are masked. The p K of this equilibrium reaction is 7.18. Through the action of oxidizing agents, some sulfhydryl groups can be oxidized to disulfide groups. 2. 2. When the sulfhydryl groups of catalase are blocked by Hg 2+ or C 6 H 5 Hg + a loss of enzyme activity occurs. The loss of activity with increasing Hg 2+ or C 6 H 5 Hg + concentration may be represented as an equilibrium curve. The change of activity on blocking the prosthetic groups with azide can be expressed in the same way. 3. 3. The dissociation of the proton from the sulfhydryl group was followed by electrometric titration. The dissociation constant was found to be 2.00 · 10 −9 M (at 0°).
- Published
- 1966
- Full Text
- View/download PDF
27. Gelatin films with embedded liquid crystals in the conoscopic ray
- Author
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A. Seeboth and H. Hermel
- Subjects
Crystallography ,food.ingredient ,food ,Materials science ,Liquid crystal ,Materials Chemistry ,Metals and Alloys ,Surfaces and Interfaces ,Gelatin ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials - Published
- 1989
- Full Text
- View/download PDF
28. Über einen Fall von Encephalomyelomalacia chronica diffusa bei einem vierjährigen Kinde
- Author
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H. Hermel
- Subjects
Gynecology ,medicine.medical_specialty ,Neurology ,business.industry ,Medicine ,Neurology (clinical) ,business ,Neuroradiology - Abstract
n/a
- Published
- 1920
29. [On the mechanism of the catalase-hydrogen peroxide reaction. I. The disulfide and sulfhydryl content of beef-liver catalase]
- Author
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H, Hermel and R, Havemann
- Subjects
Liver ,Electrochemistry ,Animals ,Cattle ,Hydrogen Peroxide ,Mercury ,Sulfhydryl Compounds ,Hydrogen-Ion Concentration ,Sulfides ,Catalase ,Enzymes - Published
- 1966
30. [On the mechanism of the catalase-hydrogen peroxide reaction. II. The active centers of catalase and their mode of action]
- Author
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H, Hermel and R, Havemann
- Subjects
Liver ,Iron ,Electrochemistry ,Animals ,Cattle ,Heme ,Hydrogen Peroxide ,Sulfhydryl Compounds ,Hydrogen-Ion Concentration ,Sulfides ,Catalase ,Catalysis - Published
- 1966
31. Change and stabilization of the amyloid-beta(1-40) secondary structure by fluorocompounds.
- Author
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Vieira EP, Hermel H, and Möhwald H
- Subjects
- Amino Acid Sequence, Amyloidosis prevention & control, Circular Dichroism, Drug Design, Ethanol chemistry, Humans, Hydrophobic and Hydrophilic Interactions, Microscopy, Atomic Force, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Solutions, Amyloid beta-Peptides chemistry, Peptide Fragments chemistry, Propanols chemistry, Protein Conformation, Trifluoroethanol chemistry
- Abstract
The misfolding of the amyloid peptide, which is the result of a well-known alpha-to-beta transition, causes neurodegenerative disorder. Fluorinated alcohols have been described in the literature as potent solvents which can refold the beta-conformation. The present studies demonstrate the effectiveness of differently fluorinated alcohols for the beta-to-alpha refolding process on fibrillar aggregated amyloid beta(1-40). The regenerated helical structure is shown to be maintained in the absence of the fluoroalcohols, a behaviour which was found to contrast with immunoglobulin. We interpret this difference on the basis of the hydrophilic/hydrophobic domains in the amyloid sequence and present some speculations regarding the free-energy levels of the folded states of both proteins. The effect of the -CF(3) group on the observed conformational changes is interpreted as a result of alterations of the hydration shell of the peptides. Moreover, based on the results achieved with fluoroalcohols, we have used novel fluorinated amphiphiles possessing blood-compatibility properties and studied their effect on amyloid beta(1-40). First results point in the direction of a beta-to-alpha transition. Therefore, the use of fluorine groups in the development of new drugs is considered a new possibility requiring further investigation for the prevention of amyloidosis.
- Published
- 2003
- Full Text
- View/download PDF
32. Amyloid-beta-sheet formation at the air-water interface.
- Author
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Schladitz C, Vieira EP, Hermel H, and Möhwald H
- Subjects
- Air, Amino Acid Sequence, Animals, Biophysical Phenomena, Biophysics, Circular Dichroism, Humans, In Vitro Techniques, Models, Molecular, Molecular Sequence Data, PrPC Proteins chemistry, PrPSc Proteins chemistry, Protein Structure, Secondary, Spectrophotometry, Infrared, Water, Amyloid chemistry
- Abstract
An amyloid(1-40) solution rich in coil, turn, and alpha-helix, but poor in beta-sheet, develops monolayers with a high beta-sheet content when spread at the air-water interface. These monolayers are resistant to repeated compression-dilatation cycles and interaction with trifluoroethanol. The secondary structure motifs were detected by circular dichroism (CD) in solution and with infrared reflection-absorption spectroscopy (IRRAS) at the interface. Hydrophobic influences are discussed for the structure conversion in an effort to understand the completely unknown reason for the natural change of the normal prion protein cellular (PrP(C)) into the abnormal prion protein scrapie (PrP(Sc)).
- Published
- 1999
- Full Text
- View/download PDF
33. Selective staining by the fluorochrome, 5,5-diphenyl-9-ethyl-DiOC2(3). I. Physicochemical studies of dye-dye and dye-tissue interactions.
- Author
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Hermel H, Schmahl W, and Möhwald H
- Subjects
- Carbocyanines chemistry, Fluorescence, Fluorescent Dyes chemistry, Molecular Structure, Solutions, Solvents, Staining and Labeling methods, Carbocyanines metabolism, Fluorescent Dyes metabolism
- Abstract
The 5,5'-diphenyl-9-ethyl-oxacarbocyanine (5,5'-diphenyl-9-ethyl-DiOC2(3); CD) has properties suitable for histological investigations including the spectral range for absorption and fluorescence emission, the values of the corresponding molar coefficients and fluorescence quantum yield. Furthermore, CD remains relatively unchanged over the entire pH range and interacts with protein beta-sheets. The latter fact is detectable spectroscopically as a bathochromic shift. In water-containing media such as the histological stain and washes, CD exists as a monomer, a dimer and in two aggregated states. These differ in their binding affinity to tissue sections, in their solubility in water, alcohol and water/alcohol mixtures, and in their UV/VIS absorption and fluorescence emission. The ratio of the various CD states and the contrast of selectively stained tissue areas can be controlled via the staining conditions and the sequence of the washes. Furthermore, mounting in a xylene-based medium produces a solvatochromic spectral shift of the CD monomer, which leads to a marked elevation in phase contrast.
- Published
- 1999
- Full Text
- View/download PDF
34. Selective staining by the fluorochrome 5,5-diphenyl-9-ethyl-oxacarbocyanine. II. Application to paraffin embedded nervous tissue.
- Author
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Schmahl W, Hermel H, Matiasek K, and Möhwald H
- Subjects
- Animals, Cats, Paraffin Embedding, Staining and Labeling methods, Brain anatomy & histology, Carbocyanines chemistry, Fluorescent Dyes
- Abstract
We present a simple and rapid method to label specific structures of neural tissue in paraffin sections. After incubation of deparaffinized sections in the cyanine dye 5,5'-diphenyl-9-ethyl-oxacarbocyanine (DEOC), three different washing and mounting procedures were performed. Incubation in DEOC followed by washes in ethanol and water and mounting in glycerol-gelatin resulted in selective labeling of myelin in the central and peripheral nervous systems. Weak labeling of myelin and axons and staining of nuclei of neurons was seen after incubation in DEOC followed by washes in ethanol and xylene, and mounting in Eukitt. Nuclear proteins, the endoplasmic reticulum and the Golgi apparatus were stained strongly and exclusively after incubation in DEOC, washes in water, ethanol and xylene, and mounting in Eukitt. Thus the absorption pattern of DEOC is changed significantly by solvents applied after the fluorochrome. In any case, fluorescence did not fade even after repeated and intense fluorescence microscopy over a period of 6 months.
- Published
- 1999
- Full Text
- View/download PDF
35. Examination of polypeptide beta-sheet structure in solutions and thin layers: determination of the concentration and the 'critical aggregation concentration' using a cyanine dye as sensor.
- Author
-
Hermel H and De Rossi U
- Subjects
- Circular Dichroism, Light, Membranes, Artificial, Molecular Probes, Polylysine chemistry, Scattering, Radiation, Solutions, Spectrophotometry, Biopolymers chemistry, Carbocyanines chemistry, Fluorescent Dyes chemistry, Peptides chemistry, Protein Structure, Secondary
- Abstract
In the visible spectra of some cyanine dyes a bathochromic shift of the dye monomer band was observed on the preconditions that: (1) beta-sheet containing polypeptides (denotes also proteins) were presented; and (2) these polypeptides were embedded in a layer or aggregated in solution. The band with the polypeptides which contained only the alpha-helix did not shift. In several cases the absorbance lifetime of the shifted band was limited. This was caused by dye self-association at the polypeptide surface, but there were enough quantities for this lifetime to obtain exact analytical measurements. These were executed quantitatively (100-20% beta-sheet), qualitatively (to about 10% beta-sheet) and moreover for the determination of the 'critical aggregation concentration' (cac). The applications of the dye sensor in biophysics, medicine and pharmacy were discussed.
- Published
- 1997
- Full Text
- View/download PDF
36. Band-shifting through polypeptide beta-sheet structures in the cyanine UV-Vis spectrum.
- Author
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Hermel H, Höltje HD, Bergemann S, De Rossi U, and Kriwanek J
- Subjects
- Circular Dichroism, Models, Molecular, Polylysine chemistry, Spectrophotometry, Carbocyanines chemistry, Peptides chemistry, Protein Structure, Secondary
- Abstract
If oxa- or thiacarbocyanine is introduced into an aqueous poly-L-lysine (PL) solution in a concentration higher than that of aggregation, then a shift of the absorption band of the cyanine monomer (M) can be observed in the UV-Vis spectrum, provided that the PL has a beta-sheet conformation. Other polypeptide aggregates with a high beta-sheet content exhibit this effect as well, whereas for PL with an alpha-helix conformation no spectral shift is observed. The force-field optimized molecular models and the calculated interaction energies prove that the beta-sheet interacts significantly more intensively with the cyanine than the alpha-helix does. The quantum chemically calculated highest occupied and lowest unoccupied molecular orbital (HOMO-LUMO) energies of the cyanines and cyanine beta-sheet polypeptide complexes predict a M-shift to bathochromic frequencies in agreement with experimental findings. In the case of the measured M-shift to hypsochromic frequencies, the shift appears to be influenced by the presence of cyanine J-aggregates. The results open the way for a fast and simple method to identify polypeptide beta-sheet structures in biological and other systems containing polypeptides by using cyanine as a sensor.
- Published
- 1995
- Full Text
- View/download PDF
37. [On the mechanism of the catalase-hydrogen peroxide reaction. I. The disulfide and sulfhydryl content of beef-liver catalase].
- Author
-
Hermel H and Havemann R
- Subjects
- Animals, Cattle, Electrochemistry, Enzymes metabolism, Hydrogen Peroxide analysis, Hydrogen-Ion Concentration, Mercury pharmacology, Catalase analysis, Liver enzymology, Sulfhydryl Compounds analysis, Sulfides analysis
- Published
- 1966
38. [On the mechanism of the catalase-hydrogen peroxide reaction. II. The active centers of catalase and their mode of action].
- Author
-
Hermel H and Havemann R
- Subjects
- Animals, Catalysis, Cattle, Electrochemistry, Hydrogen Peroxide metabolism, Hydrogen-Ion Concentration, Catalase metabolism, Heme metabolism, Iron metabolism, Liver enzymology, Sulfhydryl Compounds metabolism, Sulfides metabolism
- Published
- 1966
Catalog
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