Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Julie E. Penzotti"'
Autor:
Jutta Glock, Peter D. J. Grootenhuis, Steven Bondy, Daniel D. Comer, Soan Cheng, Arthur Steiger, Martin Zeller, Grit Laue, Adrian Friedmann, Olivier Jacob, Mafalda Nina, Hans-Jürg Widmer, Klaus Kreuz, Julie E. Penzotti, Hans Brunner, James Allen, Thierry Niderman, Hans Ulrich Haas, Renold Chollet, Martin Eberle, Peter Renold, William Lutz, Jürg Ehrler, Marian Valentini, Markus Walti, Evelyne Sieger, Thomas Vettiger, G. Wayne Craig
Publikováno v:
CHIMIA, Vol 62, Iss 1-2 (2008)
The search for new active molecules with novel modes of action and desirable physical properties is an ongoing endeavour. This publication describes the follow-up chemistry of a biological hit discovered in the screening system of Novartis Crop Prote
Externí odkaz:
https://doaj.org/article/5c120d9f6ae7458abd6d1d641fce6442
Publikováno v:
Journal of Computer-Aided Molecular Design. 20:751-762
In order to develop robust machine-learning or statistical models for predicting biological activity, descriptors that capture the essence of the protein-ligand interaction are required. In the absence of structural information from X-ray or NMR expe
Publikováno v:
Measurement Science and Technology. 16:270-277
A variety of machine learning algorithms, including hierarchical clustering, decision trees, k-nearest neighbours, support vector machines and bagging, were applied to construct models to predict the molecular weight of the polymers produced by a set
Autor:
David C. Spellmeyer, Peter D. J. Grootenhuis, Paul Beroza, Erin K. Bradley, Julie E. Penzotti, Jennifer L. Miller
Publikováno v:
Journal of Medicinal Chemistry. 43:2770-2774
The high failure rate of drugs in the development phase requires a strategy to reduce risks by generating lead candidates from different chemical classes. We describe a new three-dimensional computational approach for lead evolution, based on multipl
Autor:
Ronald E. Stenkamp, V. Chu, Patrick S. Stayton, David E. Hyre, Isolde Le Trong, Julie E. Penzotti, S. Freitag, Ashutosh Chilkoti, L.A. Klumb, Richard To, Terry P. Lybrand
Publikováno v:
Biomolecular Engineering. 16:39-44
The high affinity energetics in the streptavidin-biotin system provide an excellent model system for studying how proteins balance enthalpic and entropic components to generate an impressive overall free energy for ligand binding. We review here conc
Autor:
Richard To, Terry P. Lybrand, Patrick S. Stayton, V. Chu, David E. Hyre, Isolde Le Trong, S. Freitag, L.A. Klumb, Ronald E. Stenkamp, Julie E. Penzotti
Publikováno v:
Proceedings of the National Academy of Sciences. 96:8384-8389
It is currently unclear whether small molecules dissociate from a protein binding site along a defined pathway or through a collection of dissociation pathways. We report herein a joint crystallographic, computational, and biophysical study that sugg
Autor:
Derek G. Doherty, Julie E. Penzotti, David M. Koelle, William W. Kwok, Terry P. Lybrand, Susan Masewicz, Gerald T. Nepom
Publikováno v:
The Journal of Immunology. 161:3527-3535
TCR engagement of peptide-MHC class II ligands involves specific contacts between the TCR and residues on both the MHC and peptide molecules. We have used molecular modeling and assays of peptide binding and T cell function to characterize these inte
Publikováno v:
Journal of Neuroimmunology. 85:102-105
Myasthenia gravis (MG) is characterized by muscle weakness due to autoimmunity against the nicotinic acetylcholine receptor (nAChR). MG is associated with polymorphisms in HLA-DQ genes and the aim of the present study was to characterize structural d
Publikováno v:
Arthritis & Rheumatism. 40:1316-1326
Objective. To use molecular modeling tools to analyze the potential structural basis for the genetic association of rheumatoid arthritis (RA) with the major histocompatibility complex (MHC) “shared epitope,” a set of conserved amino acid residues
Publikováno v:
Journal of Autoimmunity. 9:287-293
HLA molecules associated with rheumatoid arthritis (RA) contain a discrete structural element known as the shared epitope, a set of conserved amino acid residues located on the alpha helical portion of the class II beta chain. Each of the different H