Search

Your search keyword '"W. Jeffries"' showing total 14 results
Start Over Author "W. Jeffries" Publisher american chemical society
14 results on '"W. Jeffries"'

10. Wood Deterioration and Preservation

Author

Barry Goodell, Darrel D. Nicholas, Tor P. Schultz, Barry Halliwell, N. Scott Reading, Kevin D. Welch, Steven D. Aust, Geoffrey Daniel, Kurt Messner, Karin Fackler, Pongsak Lamaipis, Wolfgang Gindl, Ewald Srebotnik, Takashi Watanabe, Timothy R. Filley, Akio Enoki, Hiromi Tanaka, Shuji Itakura, Jaime Rodriguez, André Ferraz, Maricilda P. de Mello, William P. Henry, Kaichang Li, William R. Kenealy, Thomas W. Jeffries, Thomas G. Shelton, J. Kenneth Grace, Daniel L. Distel, Simon M. Cragg, Douglas Crawford, Susan V. Diehl, M. Lynn Prewitt, Fatima Moore Shmulsky, C. A. Clausen, Barbara L. Illman, Jody Jellison, Claudia Jasalavich, Andrea Ostrofsky, C. Husseneder, E. L. Vargo, J. K. Grace, Alan F. Preston, Frederick Green, Liam E. Leightley, Douglas J. Gardner, Cihat Tascioglu, Magnus E. P. Wålinder, Barry Goodell, Darrel D. Nicholas, Tor P. Schultz, Barry Halliwell, N. Scott Reading, Kevin D. Welch, Steven D. Aust, Geoffrey Daniel, Kurt Messner, Karin Fackler, Pongsak Lamaipis, Wolfgang Gindl, Ewald Srebotnik, Takashi Watanabe, Timothy R. Filley, Akio Enoki, Hiromi Tanaka, Shuji Itakura, Jaime Rodriguez, André Ferraz, Maricilda P. de Mello, William P. Henry, Kaichang Li, William R. Kenealy, Thomas W. Jeffries, Thomas G. Shelton, J. Kenneth Grace, Daniel L. Distel, Simon M. Cragg, Douglas Crawford, Susan V. Diehl, M. Lynn Prewitt, Fatima Moore Shmulsky, C. A. Clausen, Barbara L. Illman, Jody Jellison, Claudia Jasalavich, Andrea Ostrofsky, C. Husseneder, E. L. Vargo, J. K. Grace, Alan F. Preston, Frederick Green, Liam E. Leightley, Douglas J. Gardner, Cihat Tascioglu, and Magnus E. P. Wålinder

Subjects
Wood--Deterioration--Congresses, Wood--Preservation--Congresses
Published
2003

11. Enzymes in Biomass Conversion

Author

GARY F. LEATHAM, MICHAEL E. HIMMEL, K. Grohmann, L. Viikari, A. Kantelinen, M. Rättö, J. Sundquist, Christopher J. Rivard, William S. Adney, J. Gregory Zeikus, Chanyong Lee, Yong-Eok Lee, Badal C. Saha, Koki Horikoshi, J. W. Fox, J. D. Shannon, J. B. Bjarnason, W. Douglas Crabb, Ian T. Forrester, Chittra Mishra, D. S. Chahal, R. C. Lawson, K. W. Evans, D. J. Mitchell, J. O. Baker, K. K. Oh, Anthony C. Grabski, Mark N. Shahan, Kathleen Fletcher, Ronald M. Spears, Danying Cai, Ming Tien, M. H. Gold, J. A. Brown, B. J. Godfrey, M. B. Mayfield, H. Wariishi, K. Valli, Pascal Bonnarme, Juana Perez, Thomas W. Jeffries, Noriyuki Morohoshi, K. Polvinen, P. Lehtonen, M. Leisola, K. Visuri, Toshiaki Umezawa, Takayoshi Higuchi, Simo Sarkanen, R. P. Overend, K. G. Johnson, K. O. Elliston, M. D. Yablonsky, D. E. Eveleigh, H. Esterbauer, M. Hayn, P. M. Abuja, M. Claeyssens, James C. Linden, Ming Shiang, Neil R. Gilkes, Andreas Meinke, John B. Coutinho, Edgar Ong, Jeffrey M. Greenwood, Robert C. Miller, Douglas G. Kilburn, Antony J. Warren, Saroj P. Mathupala, Bernard, GARY F. LEATHAM, MICHAEL E. HIMMEL, K. Grohmann, L. Viikari, A. Kantelinen, M. Rättö, J. Sundquist, Christopher J. Rivard, William S. Adney, J. Gregory Zeikus, Chanyong Lee, Yong-Eok Lee, Badal C. Saha, Koki Horikoshi, J. W. Fox, J. D. Shannon, J. B. Bjarnason, W. Douglas Crabb, Ian T. Forrester, Chittra Mishra, D. S. Chahal, R. C. Lawson, K. W. Evans, D. J. Mitchell, J. O. Baker, K. K. Oh, Anthony C. Grabski, Mark N. Shahan, Kathleen Fletcher, Ronald M. Spears, Danying Cai, Ming Tien, M. H. Gold, J. A. Brown, B. J. Godfrey, M. B. Mayfield, H. Wariishi, K. Valli, Pascal Bonnarme, Juana Perez, Thomas W. Jeffries, Noriyuki Morohoshi, K. Polvinen, P. Lehtonen, M. Leisola, K. Visuri, Toshiaki Umezawa, Takayoshi Higuchi, Simo Sarkanen, R. P. Overend, K. G. Johnson, K. O. Elliston, M. D. Yablonsky, D. E. Eveleigh, H. Esterbauer, M. Hayn, P. M. Abuja, M. Claeyssens, James C. Linden, Ming Shiang, Neil R. Gilkes, Andreas Meinke, John B. Coutinho, Edgar Ong, Jeffrey M. Greenwood, Robert C. Miller, Douglas G. Kilburn, Antony J. Warren, Saroj P. Mathupala, and Bernard

Subjects
Hydrolases--Industrial applications--Congresse, Biomass conversion--Congresses, Microbial enzymes--Industrial applications--Co
Published
1991

12. Emerging Technologies for Materials and Chemicals From Biomass

Author

ROGER M. ROWELL, TOR P. SCHULTZ, RAMANI NARAYAN, Helena L. Chum, Arthur J. Power, John Youngquist, George E. Myers, Teresa M. Harten, R. G. Raj, B. V. Kokta, David V. Plackett, Hideaki Matsuda, Raymond A. Young, Nobuo Shiraishi, Robert A. Northey, David N.-S. Hon, William M. Doane, Charles L. Swanson, George F. Fanta, Stoil K. Dirlikov, Arjun C. Sau, Thomas G. Majewicz, S. F. Thames, P. W. Poole, Thomas L. Krinski, Thomas W. Jeffries, Irving S. Goldstein, K. Grohmann, C. E. Wyman, M. E. Himmel, David E. Knox, Philip L. Robinson, J. W. Barrier, M. M. Bulls, D. S. Scott, J. Piskorz, D. St. A. G. Radlein, James D. McChesney, Alice M. Clark, ROGER M. ROWELL, TOR P. SCHULTZ, RAMANI NARAYAN, Helena L. Chum, Arthur J. Power, John Youngquist, George E. Myers, Teresa M. Harten, R. G. Raj, B. V. Kokta, David V. Plackett, Hideaki Matsuda, Raymond A. Young, Nobuo Shiraishi, Robert A. Northey, David N.-S. Hon, William M. Doane, Charles L. Swanson, George F. Fanta, Stoil K. Dirlikov, Arjun C. Sau, Thomas G. Majewicz, S. F. Thames, P. W. Poole, Thomas L. Krinski, Thomas W. Jeffries, Irving S. Goldstein, K. Grohmann, C. E. Wyman, M. E. Himmel, David E. Knox, Philip L. Robinson, J. W. Barrier, M. M. Bulls, D. S. Scott, J. Piskorz, D. St. A. G. Radlein, James D. McChesney, and Alice M. Clark

Subjects
Biomass chemicals--Congresses, Biomass energy--Congresses
Published
1992

13. Binding of Inhibitors to Nuclear Localization Signal Peptide from Venezuelan Equine Encephalitis Virus Capsid Protein Explored with All-Atom Replica Exchange Molecular Dynamics.

Author

Delfing BM, Laracuente XE, Luo X, Olson A, Jeffries W, Foreman KW, Paige M, Kehn-Hall K, Lockhart C, and Klimov DK

Abstract

Several small molecule inhibitors have been designed to block binding of the Venezuelan equine encephalitis virus (VEEV) nuclear localization signal (NLS) sequence to the importin-α nuclear transport protein. To probe the inhibition mechanism on a molecular level, we used all-atom explicit water replica exchange molecular dynamics to study the binding of two inhibitors, I1 and I2, to the coreNLS peptide, representing the core fragment of the VEEV NLS sequence. Our objective was to evaluate the possibility of masking wherein binding of these inhibitors to the coreNLS occurs prior to its binding to importin-α. We found that the free energy of I1 and I2 binding to the coreNLS is less favorable than that to importin-α. This outcome argues against preemptive inhibitor binding to the coreNLS prior to importin-α. Instead, both inhibitors are expected to compete with the coreNLS peptide for binding to importin-α. The two factors responsible for the low affinities of the inhibitors to the coreNLS peptide are (i) the low cooperativity of binding to the peptide and (ii) the strong hydrophobic effect associated with binding to importin-α. Our results further show that upon binding to the coreNLS peptide, the inhibitors form multiple diverse binding poses. The coreNLS peptide coincubated with I1 and I2 adopts several conformational states, including open and collapsed, which underscores the fluidity of the coreNLS conformational ensemble as a target for inhibitors. Taken together with our prior investigations, this study sheds light on the molecular mechanism by which I1 and I2 ligands inhibit binding of the VEEV capsid protein to importin-α., Competing Interests: The authors declare no competing financial interest., (© 2024 The Authors. Published by American Chemical Society.)

Published
2024
Full Text
View/download PDF

14. Competitive Binding of Viral Nuclear Localization Signal Peptide and Inhibitor Ligands to Importin-α Nuclear Transport Protein.

Author

Delfing BM, Laracuente XE, Jeffries W, Luo X, Olson A, Foreman KW, Petruncio G, Lee KH, Paige M, Kehn-Hall K, Lockhart C, and Klimov DK

Subjects
Ligands, Encephalitis Virus, Venezuelan Equine metabolism, Encephalitis Virus, Venezuelan Equine chemistry, Protein Binding, Peptides chemistry, Peptides metabolism, Peptides pharmacology, Amino Acid Sequence, alpha Karyopherins metabolism, alpha Karyopherins chemistry, alpha Karyopherins antagonists & inhibitors, Molecular Dynamics Simulation, Nuclear Localization Signals chemistry, Binding, Competitive
Abstract

Venezuelan equine encephalitis virus (VEEV) is a highly virulent pathogen whose nuclear localization signal (NLS) sequence from capsid protein binds to the host importin-α transport protein and blocks nuclear import. We studied the molecular mechanisms by which two small ligands, termed I1 and I2, interfere with the binding of VEEV's NLS peptide to importin-α protein. To this end, we performed all-atom replica exchange molecular dynamics simulations probing the competitive binding of the VEEV coreNLS peptide and I1 or I2 ligand to the importin-α major NLS binding site. As a reference, we used our previous simulations, which examined noncompetitive binding of the coreNLS peptide or the inhibitors to importin-α. We found that both inhibitors completely abrogate the native binding of the coreNLS peptide, forcing it to adopt a manifold of nonnative loosely bound poses within the importin-α major NLS binding site. Both inhibitors primarily destabilize the native coreNLS binding by masking its amino acids rather than competing with it for binding to importin-α. Because I2, in contrast to I1, binds off-site localizing on the edge of the major NLS binding site, it inhibits fewer coreNLS native binding interactions than I1. Structural analysis is supported by computations of the free energies of the coreNLS peptide binding to importin-α with or without competition from the inhibitors. Specifically, both inhibitors reduce the free energy gain from coreNLS binding, with I1 causing significantly larger loss than I2. To test our simulations, we performed AlphaScreen experiments measuring IC50 values for both inhibitors. Consistent with in silico results, the IC50 value for I1 was found to be lower than that for I2. We hypothesize that the inhibitory action of I1 and I2 ligands might be specific to the NLS from VEEV's capsid protein.

Published
2024
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results