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Structure of ras Proteins

Science, 1989
In the Table of Contents of the 24 March 1989 issue, the title of the report "Histamine is an intracellular messenger mediating platelet aggregation" by S. P. Saxena et al. appearing on page 1596 was incorrectly printed.
L, Tong   +3 more
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Prenylation of ras and ras-Related Proteins

1991
In common with certain other cellular proteins, a CAAX motif (C=cysteine, A=Aliphatic, X=any amino acid) is found at the C-terminus of all ras proteins. This motif undergoes a triplet of closely coupled post-translational modifications. First, a prenoid derivative is linked as a thioether to the cysteine residue (Hancock et al,1989; Casey et al,1989 ...
J. F. Hancock   +8 more
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Ras proteins as therapeutic targets

Biochemical Society Transactions, 2018
Oncogenic mutations in RAS genes underlie the pathogenesis of many human tumours, and there has been intense effort for over 30 years to develop effective and tolerated targeted therapeutics for patients with Ras-driven cancers. This review summarises the progress made in Ras drug discovery, highlighting some of the recent developments in directly ...
Atanu, Chakraborty   +2 more
openaire   +2 more sources

Ras-GTPase Activating Protein (GAP): A Putative Effector for Ras

Cellular Signalling, 1997
One attractive candidate for a Ras effector protein, other than the Raf kinases, is Ras-GAP. Indeed, recent literature suggests that besides the Raf/MAP kinase cascade, additional pathways must be stimulated to elicit a full biological response to Ras. Ras binds the COOH terminal domain of Ras-GAP, while the NH2 terminal domain appears to be essential ...
B, Tocque   +5 more
openaire   +2 more sources

Peptide inhibitors targeting Ras and Ras-associated protein–protein interactions

European Journal of Medicinal Chemistry
Peptides represent attractive molecules for targeting protein-protein interactions, and peptide drug development has made great progress during the last decades. Ras protein, the most promising target in cancer therapy, is one of the major growth drivers in various cancers.
Dan Han   +5 more
openaire   +2 more sources

The Ras Superfamily G-Proteins

2013
The Ras superfamily G-proteins are monomeric proteins of approximately 21kDa that act as a molecular switch to regulate a variety of cellular processes. The structure of the Ras superfamily G-proteins, their regulators as well as posttranslational modification of these proteins leading to their membrane association have been elucidated.
Ashley L, Tetlow, Fuyuhiko, Tamanoi
openaire   +2 more sources

The very druggable RAS proteins

Trends in Cancer
RAS genes encode molecular switches that control cell growth and survival, and their oncogenic mutations drive many cancers. Once deemed 'undruggable', RAS is now being challenged by innovative inhibitors. Recent advances, reported by Stanland and Huggins et al.
Marie C. Hasselluhn, Kenneth P. Olive
openaire   +2 more sources

Activation of Ras Proteins by Ras Guanine Nucleotide Releasing Protein Family Members

2006
Ras guanine nucleotide releasing proteins (RasGRPs) function as guanine nucleotide exchange factors for Ras proteins. Thus, RasGRPs are direct activators of Ras proteins and contribute an important role in various cell-signaling pathways that are regulated by the activation state of Ras proteins.
Que T, Lambert, Gary W, Reuther
openaire   +2 more sources

Dissection of the GTPase mechanism of Ras protein by MD analysis of Ras mutants

Proteins: Structure, Function, and Bioinformatics, 2005
AbstractControlling the hydrolysis rate of GTP bound to the p21ras protein is crucial for the delicate timing of many biological processes. A few mechanisms were suggested for the hydrolysis of GTP. To gain more insight into the individual elementary events of GTP hydrolysis, we carried out molecular dynamic analysis of wild‐type p21ras and some of its
Zeev Y, Friedman, Yoram, Devary
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Three-dimensional structure of Ras and Ras-related proteins

1995
Abstract The structures of several different wild-type and mutantp21 complexes have been determined by two groups. A listof the published structures is shown in Table 1 togetherwith the resolutions obtained in the crystallographic analyses.For wild-type and one oncogenic mutant both thetriphosphate and diphosphate structures have been
Alfred Wittinghofer, Alfonso Valencia
openaire   +1 more source

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