Search

Your search keyword '"Gabriella T. Heller"' showing total 8 results
Start Over Author "Gabriella T. Heller" Topic molecular biology
8 results on '"Gabriella T. Heller"'

1. Promoting transparency and reproducibility in enhanced molecular simulations

Author

B. Pavel, L. Vittorio, C. Michele, F. Marta, W. Andrew, G. Federico, V. Michele, Š. Jiří, Davide Provasi, M. Layla, K. Evgeny, S. Matteo, V. Omar, Riccardo Capelli, M. Carla, David W.H. Swenson, Kim E. Jelfs, G. Piero, D. Davide, M. Angelos, P. Jim, Gareth A. Tribello, M. Fabrizio, C. Francesco, P. Michele, E. Bernd, Cristina Paissoni, M. Matteo, F. Haohao, L. Kresten, P. Pablo, T. Pratyush, L. Alessandro, Marco De La Pierre, B. Mattia, J. Alexander, M. Tetsuya, B. Sandro, Andrew L. Ferguson, Gabriella T. Heller, Francesco Luigi Gervasio, B. Davide, R. Paolo, D. Viktor, Massimiliano Bonomi, I. Michele, Peter G. Bolhuis, P. GiovanniMaria, Carlo Camilloni, C. Andrea, P. Elena, S. Vojtěch, James S. Fraser, L. Thomas, C. Haochuan, C. Paolo, N. Marco, B. Alessandro, P. Fabio, B. Giovanni, I. Marcella, G. Alejandro, C. Wei, Glen M. Hocky, G. Toni, P. Adriana, Gabriele C. Sosso, Q. David, P. Silvio, Gregory A. Voth, M. Ralf, R. Stefano, D. Sandip, R. Jakub, The Royal Society, Département de Biologie structurale et Chimie - Department of Structural Biology and Chemistry, Institut Pasteur [Paris] (IP), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Scuola Internazionale Superiore di Studi Avanzati / International School for Advanced Studies (SISSA / ISAS), Università degli Studi di Milano = University of Milan (UNIMI), Queen's University [Belfast] (QUB), Centre de Biochimie Structurale [Montpellier] (CBS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Institut de recherche pour le développement [IRD] : UR206-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Unité de Catalyse et Chimie du Solide - UMR 8181 (UCCS), Université d'Artois (UA)-Centrale Lille-Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre Blaise Pascal (CBP), École normale supérieure de Lyon (ENS de Lyon), University of Rochester [USA], Bonomi, M., Bussi, G., Camilloni, C., Tribello, G. A., Banas, P., Barducci, A., Bernetti, M., Bolhuis, P. G., Bottaro, S., Branduardi, D., Capelli, R., Carloni, P., Ceriotti, M., Cesari, A., Chen, H., Chen, W., Colizzi, F., De, S., De La Pierre, M., Donadio, D., Drobot, V., Ensing, B., Ferguson, A. L., Filizola, M., Fraser, J. S., Fu, H., Gasparotto, P., Gervasio, F. L., Giberti, F., Gil-Ley, A., Giorgino, T., Heller, G. T., Hocky, G. M., Iannuzzi, M., Invernizzi, M., Jelfs, K. E., Jussupow, A., Kirilin, E., Laio, A., Limongelli, V., Lindorff-Larsen, K., Lohr, T., Marinelli, F., Martin-Samos, L., Masetti, M., Meyer, R., Michaelides, A., Molteni, C., Morishita, T., Nava, M., Paissoni, C., Papaleo, E., Parrinello, M., Pfaendtner, J., Piaggi, P., Piccini, G. M., Pietropaolo, A., Pietrucci, F., Pipolo, S., Provasi, D., Quigley, D., Raiteri, P., Raniolo, S., Rydzewski, J., Salvalaglio, M., Sosso, G. C., Spiwok, V., Sponer, J., Swenson, D. W. H., Tiwary, P., Valsson, O., Vendruscolo, M., Voth, G. A., White, A., Institut Pasteur [Paris], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano [Milano] (UNIMI), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centrale Lille Institut (CLIL)-Université d'Artois (UA)-Centrale Lille-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Lille, École normale supérieure - Lyon (ENS Lyon), Simulation of Biomolecular Systems (HIMS, FNWI), Molecular Simulations (HIMS, FNWI), and Massimiliano Bonomi, Giovanni Bussi, Carlo Camilloni, Gareth A. Tribello, Pavel Banáš, Alessandro Barducci, Mattia Bernetti, Peter G. Bolhuis, Sandro Bottaro, Davide Branduardi, Riccardo Capelli, Paolo Carloni, Michele Ceriotti, Andrea Cesari, Haochuan Chen, Wei Chen, Francesco Colizzi, Sandip De, Marco De La Pierre, Davide Donadio, Viktor Drobot, Bernd Ensing, Andrew L. Ferguson, Marta Filizola, James S. Fraser, Haohao Fu, Piero Gasparotto, Francesco Luigi Gervasio, Federico Giberti, Alejandro Gil-Ley, Toni Giorgino, Gabriella T. Heller, Glen M. Hocky, Marcella Iannuzzi, Michele Invernizzi, Kim E. Jelfs, Alexander Jussupow, Evgeny Kirilin, Alessandro Laio, Vittorio Limongelli, Kresten Lindorff-Larsen, Thomas Löhr, Fabrizio Marinelli, Layla Martin-Samos, Matteo Masetti, Ralf Meyer, Angelos Michaelides, Carla Molteni, Tetsuya Morishita, Marco Nava, Cristina Paissoni, Elena Papaleo, Michele Parrinello, Jim Pfaendtner, Pablo Piaggi, GiovanniMaria Piccini, Adriana Pietropaolo, Fabio Pietrucci, Silvio Pipolo, Davide Provasi, David Quigley, Paolo Raiteri, Stefano Raniolo, Jakub Rydzewski, Matteo Salvalaglio, Gabriele Cesare Sosso, Vojtěch Spiwok, Jiří Šponer, David W. H. Swenson, Pratyush Tiwary, Omar Valsson, Michele Vendruscolo, Gregory A. Voth & Andrew White

Subjects
Models, Molecular, DYNAMICS, enhanced-sampling, free-energy calculations, molecular dynamics simulations, transparency, reproducibility, dissemination, Biochemistry & Molecular Biology, Computer science, Molecular Conformation, Molecular Dynamics Simulation, Biochemistry, Biochemical Research Methods, Settore FIS/03 - Fisica della Materia, 03 medical and health sciences, 10 Technology, Humans, ddc:610, reproducibility, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 11 Medical and Health Sciences, 030304 developmental biology, 0303 health sciences, Reproducibility, Science & Technology, PLUMED consortium, Reproducibility of Results, Cell Biology, 06 Biological Sciences, simulation, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Transparency (graphic), Systems engineering, Life Sciences & Biomedicine, Software, Biotechnology, Developmental Biology
Abstract

The PLUMED consortium unifies developers and contributors to PLUMED, an open-source library for enhanced-sampling, free-energy calculations and the analysis of molecular dynamics simulations. Here, we outline our efforts to promote transparency and reproducibility by disseminating protocols for enhanced-sampling molecular simulations.

Published
2019
Full Text
View/download PDF

2. Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

Author

Benedetta Mannini, Roberta Pierattelli, Thomas Löhr, Massimiliano Bonomi, Carlo Camilloni, Thomas C. T. Michaels, Francesco Simone Ruggeri, Gabriella T. Heller, Alfonso De Simone, Michele Vendruscolo, Francesco A. Aprile, Christopher M. Dobson, Ryan Limbocker, Michele Perni, Isabella C. Felli, Tuomas P. J. Knowles, Heller, Gabriella T [0000-0002-5672-0467], Aprile, Francesco A [0000-0002-5040-4420], Perni, Michele [0000-0001-7593-8376], Ruggeri, Francesco Simone [0000-0002-1232-1907], Mannini, Benedetta [0000-0001-6812-7348], Löhr, Thomas [0000-0003-2969-810X], Bonomi, Massimiliano [0000-0002-7321-0004], Camilloni, Carlo [0000-0002-9923-8590], De Simone, Alfonso [0000-0001-8789-9546], Felli, Isabella C [0000-0002-6018-9090], Pierattelli, Roberta [0000-0001-7755-0885], Knowles, Tuomas PJ [0000-0002-7879-0140], Dobson, Christopher M [0000-0002-5445-680X], Vendruscolo, Michele [0000-0002-3616-1610], Apollo - University of Cambridge Repository, Heller, G. T., Aprile, F. A., Michaels, T. C. T., Limbocker, R., Perni, M., Ruggeri, F. S., Mannini, B., Lohr, T., Bonomi, M., Camilloni, C., de Simone, A., Felli, I. C., Pierattelli, R., Knowles, T. P. J., Dobson, C. M., Vendruscolo, M., University of Cambridge [UK] (CAM), Imperial College London, Harvard University, Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano = University of Milan (UNIMI), University of Naples Federico II = Università degli studi di Napoli Federico II, Università degli Studi di Firenze = University of Florence (UniFI), Funding: G.T.H. is supported by the Gates Cambridge Trust and the Rosalind Franklin Research Fellowship at Newnham College, Cambridge, F.A.A. is supported by UK Research and Innovation (Future Leaders Fellowship MR/S033947/1) and the Alzheimer’s Society, UK (317, 511), R.L. is supported by the Gates Cambridge Trust, TCTM by Peterhouse, Cambridge and the Swiss National Science Foundation, and F.S.R. is supported by Darwin College and the Swiss National Foundation (grant numbers P300P2_171219 and P2ELP2_162116, respectively). We acknowledge ARCHER UK National Supercomputing Service under ARCHER Leadership project (grant number e510) and PRACE for awarding us access to MareNostrum at Barcelona Supercomputing Center (BSC), Spain for metadynamic metainference simulations. Parameterization of 10074-G5 was performed using resources provided by the Cambridge Service for Data Driven Discovery (CSD3) operated by the University of Cambridge Research Computing Service (www.csd3.cam.ac.uk), provided by Dell EMC and Intel using Tier-2 funding from the Engineering and Physical Sciences Research Council (capital grant EP/P020259/1), and DiRAC funding from the Science and Technology Facilities Council (www.dirac.ac.uk). MALDI mass spectrometry measurements were performed by L. Packman at the Protein and Nucleic Acid Chemistry Facility (PNAC) at the Department of Biochemistry, University of Cambridge. The NMR measurements were supported by the iNEXT H2020 Programme (EC contract no. 653706). OW450 C. elegans were donated by E. Nollen. BLI measurements were performed in the Biophysics facility at the Department of Biochemistry, University of Cambridge. The work was also supported by the Centre for Misfolding Diseases and the INCEPTION project ANR-16-CONV-0005., ANR-16-CONV-0005,INCEPTION,Institut Convergences pour l'étude de l'Emergence des Pathologies au Travers des Individus et des populatiONs(2016), Harvard University [Cambridge], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano [Milano] (UNIMI), University of Naples Federico II, and Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI)

Subjects
Amyloid beta, In silico, Biophysics, Intrinsically disordered proteins, 03 medical and health sciences, 0302 clinical medicine, Alzheimer Disease, Drug Discovery, medicine, Humans, Life Science, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Research Articles, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Amyloid beta-Peptides, biology, Drug discovery, Chemistry, SciAdv r-articles, Conformational entropy, Small molecule, Peptide Fragments, 3. Good health, Mechanism of action, biology.protein, Small molecule binding, medicine.symptom, Hydrophobic and Hydrophilic Interactions, 030217 neurology & neurosurgery, Research Article
Abstract

A small molecule binds to a disordered protein in its monomeric form, preventing its aggregation linked to Alzheimer’s disease., Disordered proteins are challenging therapeutic targets, and no drug is currently in clinical use that modifies the properties of their monomeric states. Here, we identify a small molecule (10074-G5) capable of binding and sequestering the intrinsically disordered amyloid-β (Aβ) peptide in its monomeric, soluble state. Our analysis reveals that this compound interacts with Aβ and inhibits both the primary and secondary nucleation pathways in its aggregation process. We characterize this interaction using biophysical experiments and integrative structural ensemble determination methods. We observe that this molecule increases the conformational entropy of monomeric Aβ while decreasing its hydrophobic surface area. We also show that it rescues a Caenorhabditis elegans model of Aβ-associated toxicity, consistent with the mechanism of action identified from the in silico and in vitro studies. These results illustrate the strategy of stabilizing the monomeric states of disordered proteins with small molecules to alter their behavior for therapeutic purposes.

Published
2020
Full Text
View/download PDF

3. Structural Ensemble Modulation upon Small-Molecule Binding to Disordered Proteins

Author

Gabriella T. Heller, Massimiliano Bonomi, Michele Vendruscolo, University of Cambridge [UK] (CAM), Heller, Gabrielle [0000-0002-5672-0467], Bonomi, Massimilano [0000-0002-7321-0004], Vendruscolo, Michele [0000-0002-3616-1610], and Apollo - University of Cambridge Repository

Subjects
0301 basic medicine, Models, Molecular, Protein Conformation, Entropy, structural ensembles, Computational biology, 010402 general chemistry, 01 natural sciences, drug discovery, 03 medical and health sciences, Structural Biology, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Physics, food and beverages, Proteins, Small molecule, 0104 chemical sciences, Intrinsically Disordered Proteins, Molecular Weight, small molecules, 030104 developmental biology, Small molecule binding, disordered proteins, Protein Binding
Abstract

Over the past decade, there has been a growing interest in investigating whether disordered proteins can be targeted for clinical purposes using small molecules [1] , [2] , [3] , [4] , [5] , [6] , [7] , [8] . While small-molecule binding to disordered proteins can be seen as unorthodox, examples of this phenomenon have been reported. In order to rationalize these observations, a variety of models are emerging, sometimes in apparent contradiction. Here, we offer a “structural ensemble modulation” view as an attempt to clarify the language, organize concepts, and facilitate the comparison of different studies. In doing so, we hope to promote the understanding of the general principles underlying this phenomenon toward the development of novel therapeutic compounds targeting disordered proteins, which are prevalent in a wide range of human diseases [1] , [2] , [3] , [4] , [5] , [6] , [7] , [8] .

Published
2017
Full Text
View/download PDF

4. Methods of probing the interactions between small molecules and disordered proteins

Author

Michele Vendruscolo, Francesco A. Aprile, Gabriella T. Heller, Heller, Gabrielle [0000-0002-5672-0467], Aprile, Francesco [0000-0002-5040-4420], Vendruscolo, Michele [0000-0002-3616-1610], and Apollo - University of Cambridge Repository

Subjects
0301 basic medicine, binding, Fluorescence Polarization, 010402 general chemistry, 01 natural sciences, drugs, Small Molecule Libraries, 03 medical and health sciences, Cellular and Molecular Neuroscience, Multi-author Review, Two-Hybrid System Techniques, Scattering, Small Angle, Human proteome project, Fluorescence Resonance Energy Transfer, Humans, Molecular Biology, Pharmacology, Molecular interactions, Drug discovery, Chemistry, Circular Dichroism, Cell Biology, Surface Plasmon Resonance, Small molecule, 0104 chemical sciences, Intrinsically Disordered Proteins, small molecules, 030104 developmental biology, Order (biology), Biophysics, Molecular Medicine, disordered proteins, Protein Binding, molecular interactions
Abstract

It is generally recognized that a large fraction of the human proteome is made up of proteins that remain disordered in their native states. Despite the fact that such proteins play key biological roles and are involved in many major human diseases, they still represent challenging targets for drug discovery. A major bottleneck for the identification of compounds capable of interacting with these proteins and modulating their disease-promoting behaviour is the development of effective techniques to probe such interactions. The difficulties in carrying out binding measurements have resulted in a poor understanding of the mechanisms underlying these interactions. In order to facilitate further methodological advances, here we review the most commonly used techniques to probe three types of interactions involving small molecules: (1) those that disrupt functional interactions between disordered proteins; (2) those that inhibit the aberrant aggregation of disordered proteins, and (3) those that lead to binding disordered proteins in their monomeric states. In discussing these techniques, we also point out directions for future developments.

Published
2017

5. Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide

Author

Gabriella T. Heller, Carlo Camilloni, Alfonso De Simone, Massimiliano Bonomi, Francesco A. Aprile, Michele Vendruscolo, University of Cambridge [UK] (CAM), Università degli Studi di Milano [Milano] (UNIMI), Imperial College London, Heller, Gabrielle [0000-0002-5672-0467], Aprile, Francesco [0000-0002-5040-4420], Bonomi, Massimilano [0000-0002-7321-0004], Vendruscolo, Michele [0000-0002-3616-1610], Apollo - University of Cambridge Repository, Heller, G. T., Aprile, F. A., Bonomi, M., Camilloni, C., De Simone, A., and Vendruscolo, M.

Subjects
0301 basic medicine, Magnetic Resonance Spectroscopy, Entropy, Statistics as Topic, small molecule, specificity, Peptide, Plasma protein binding, 010402 general chemistry, 01 natural sciences, Molecular Docking Simulation, Biophysical Phenomena, Proto-Oncogene Proteins c-myc, 03 medical and health sciences, drug binding, Structural Biology, disordered protein, Human proteome project, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, Intermolecular force, Nuclear magnetic resonance spectroscopy, Small molecule, 3. Good health, 0104 chemical sciences, small molecules, Thiazoles, 030104 developmental biology, Biochemistry, chemistry, Biophysics, Thiazole, disordered proteins, Human, Protein Binding
Abstract

Approximately one-third of the human proteome is made up of proteins that are entirely disordered or that contain extended disordered regions. Although these disordered proteins are closely linked with many major diseases, their binding mechanisms with small molecules remain poorly understood, and a major concern is whether their specificity can be sufficient for drug development. Here, by studying the interaction of a small molecule and a disordered peptide from the oncogene protein c-Myc, we describe a “specific-diffuse” binding mechanism that exhibits sequence specificity despite being of entropic nature. By combining NMR spectroscopy, biophysical measurements, statistical inference, and molecular simulations, we provide a quantitative measure of such sequence specificity and compare it to the case of the interaction of urea, which is diffuse but not specific. To investigate whether this type of binding can generally modify intermolecular interactions, we show that it leads to an inhibition of the aggregation of the peptide. These results suggest that the binding mechanism that we report may create novel opportunities to discover drugs that target disordered proteins in their monomeric states in a specific manner.

Published
2017
Full Text
View/download PDF

6. Principles of protein structural ensemble determination

Author

Carlo Camilloni, Gabriella T. Heller, Michele Vendruscolo, Massimiliano Bonomi, University of Cambridge [UK] (CAM), Università degli Studi di Milano [Milano] (UNIMI), Bonomi, Massimilano [0000-0002-7321-0004], Heller, Gabrielle [0000-0002-5672-0467], Vendruscolo, Michele [0000-0002-3616-1610], and Apollo - University of Cambridge Repository

Subjects
0301 basic medicine, Models, Molecular, 010304 chemical physics, Protein molecules, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Entropy, Proteins, Nanotechnology, Computational biology, 01 natural sciences, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Visualization, 03 medical and health sciences, 030104 developmental biology, Protein structure, Structural Biology, 0103 physical sciences, Human proteome project, Humans, Molecular Biology
Abstract

International audience; The biological functions of protein molecules are intimately contingent on their conformational dynamics. This aspect is particularly evident for disordered proteins, which constitute about one-third of the human proteome. Therefore, structural ensembles often offer more useful representations of proteins than individual conformations. Here, we describe how the well-established principles of protein structure determination should be extended to the case of protein structural ensembles determination. These principles concern primarily how to deal with conformationally heterogeneous states, and with experimental measurements that are averaged over such states and affected by a variety of errors. We first review the vast literature of recent methods that combine experimental and computational information to model structural ensembles, highlighting their similarities and differences. We then address some conceptual problems in the determination of structural ensembles and define future goals towards the establishment of objective criteria for the comparison, validation, visualization, and dissemination of such ensembles.

Published
2017
Full Text
View/download PDF

7. Targeting disordered proteins with small molecules using entropy

Author

Michele Vendruscolo, Gabriella T. Heller, Pietro Sormanni, Heller, Gabrielle [0000-0002-5672-0467], Sormanni, Pietro [0000-0002-6228-2221], Vendruscolo, Michele [0000-0002-3616-1610], and Apollo - University of Cambridge Repository

Subjects
binding, Protein Conformation, Entropy, Intermolecular force, small molecule, Proteins, Plasma protein binding, Biochemistry, Small molecule, chemistry.chemical_compound, Monomer, Protein structure, chemistry, Computational chemistry, entropic expansion, Biophysics, Human proteome project, Thermodynamics, Molecular Biology, disordered proteins, Entropy (order and disorder), Protein Binding
Abstract

The human proteome includes many disordered proteins. Although these proteins are closely linked with a range of human diseases, no clinically approved drug targets them in their monomeric forms. This situation arises, at least in part, from the current lack of understanding of the mechanisms by which small molecules bind proteins that do not fold into well-defined conformations. To explore possible solutions to this problem, we discuss quite generally how an overall decrease in the free energy associated with intermolecular binding can originate from different combinations of enthalpic and entropic contributions. We then consider more specifically a mechanism of binding by which small molecules can affect the conformational space of a disordered protein by creating an entropic expansion in which more conformations of the protein become populated.

Published
2015

8. Topological Complexity in Protein Structures

Author

Erica Flapan and Gabriella T. Heller

Subjects
Discrete mathematics, Topological complexity, links, topology, Applied Mathematics, lcsh:Mathematics, non-planarity, Biophysics, knots, food and beverages, lcsh:QA1-939, proteins, Knot theory, spatial graphs, Möbius ladders, Computational Mathematics, Protein structure, stomatognathic system, lcsh:Biology (General), Molecular Biology, lcsh:QH301-705.5, Mathematical Physics, Topology (chemistry), Mathematics
Abstract

For DNA molecules, topological complexity occurs exclusively as the result of knotting or linking of the polynucleotide backbone. By contrast, while a few knots and links have been found within the polypeptide backbones of some protein structures, non-planarity can also result from the connectivity between a polypeptide chain and inter- and intra-chain linking via cofactors and disulfide bonds. In this article, we survey the known types of knots, links, and non-planar graphs in protein structures with and without including such bonds and cofactors. Then we present new examples of protein structures containing Möbius ladders and other non-planar graphs as a result of these cofactors. Finally, we propose hypothetical structures illustrating specific disulfide connectivities that would result in the key ring link, the Whitehead link and the 51 knot, the latter two of which have thus far not been identified within protein structures.

Published
2015

Catalog

Books, media, physical & digital resources
See catalog results