Results 341 to 350 of about 13,339,631 (403)

Protein myristoylation in protein–lipid and protein–protein interactions

Biophysical Chemistry, 1999
Various proteins in signal transduction pathways are myristoylated. Although this modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification exerts its effects is still largely unknown. Here we discuss the roles played by protein myristoylation, in both protein-lipid and protein-protein ...
openaire   +3 more sources

Acute-phase proteins and other systemic responses to inflammation.

New England Journal of Medicine, 1999
A large number of changes, distant from the site or sites of inflammation and involving many organ systems, may accompany inflammation. In 1930 interest was focused on these changes by the discovery of C-reactive protein (so named because it reacted with
C. Gabay, I. Kushner
semanticscholar   +1 more source

G proteins: transducers of receptor-generated signals.

Annual Review of Biochemistry, 1987
PERSPECTIVES AND SUMMARy ......... .. ........ . ...... 615 HISTORy ....... ...... . . . . . ...... . . .. .... . . . .. . 616 INDIVIDUAL G PROTEINS: FUNCTIONS AND MOLECULAR ENTITIES 617 Criter ia for In volvemen t o f a G Pr otein ..... .........
A. Gilman
semanticscholar   +1 more source

The impact of protein flexibility on protein–protein docking

Proteins: Structure, Function, and Bioinformatics, 2004
AbstractAccounting for protein flexibility in protein–protein docking algorithms is challenging, and most algorithms therefore treat proteins as rigid bodies or permit side‐chain motion only. While the consequences are obvious when there are large conformational changes upon binding, the situation is less clear for the modest conformational changes ...
Rebecca C. Wade, Lutz P. Ehrlich, Michael Nilges   +2 more
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Protein–protein association kinetics and protein docking

Current Opinion in Structural Biology, 2002
Rigid body protein docking methods frequently yield false positive structures that have good surface complementarity, but are far from the native complex. The main reason for this is the uncertainty of the protein structures to be docked, including the positions of solvent-exposed sidechains. Substantial efforts have been devoted to finding near-native
Sandor Vajda, Carlos J. Camacho
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Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology.

Annual Review of Physiology, 1999
Molecular chaperones, including the heat-shock proteins (Hsps), are a ubiquitous feature of cells in which these proteins cope with stress-induced denaturation of other proteins.
M. Feder, G. Hofmann
semanticscholar   +1 more source

THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

, 1996
▪ Abstract The transcription factor NF-κB has attracted widespread attention among researchers in many fields based on the following: its unusual and rapid regulation, the wide range of genes that it controls, its central role in immunological processes,
A. Baldwin
semanticscholar   +1 more source

Protein-Protein Interactions in Membranes

Protein & Peptide Letters, 2011
In this article we review the current status of our understanding of membrane mediated interactions from theory and experiment. Phenomenological mean field and molecular models will be discussed and compared to recent experimental results from dynamical neutron scattering and atomic force microscopy.
Armstrong, C.L., Sandqvist, E., Rheinstädter, M.C.   +2 more
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Protein Phosphorylation and Protein-Protein Interactions

2002
Intracellular signaling is the series of events which translates the specific message of circulating ligands into a particular biological response in target cells. The first step in hormone signaling involves the interaction between a ligand and its cognate receptor (membrane or nuclear), which in turn induces stoichiometric and conformational changes ...
Paul A. Kelly, Vincent Goffin
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DISCOVERING PROTEIN–PROTEIN INTERACTIONS

Journal of Bioinformatics and Computational Biology, 2004
The ongoing genomics and proteomics efforts have helped identify many new genes and proteins in living organisms. However, simply knowing the existence of genes and proteins does not tell us much about the biological processes in which they participate. Many major biological processes are controlled by protein interaction networks.
See-Kiong Ng, Soon-Heng Tan
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