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Open AccessJournal ArticleDOI

Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases.

Peter J. Kennelly, +1 more
- 25 Aug 1991 - 
- Vol. 266, Iss: 24, pp 15555-15558
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This article is published in Journal of Biological Chemistry.The article was published on 1991-08-25 and is currently open access. It has received 1311 citations till now. The article focuses on the topics: Kinase & Phosphatase.

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Journal ArticleDOI

Cloned Glutamate Receptors

TL;DR: The application of molecular cloning technology to the study of the glutamate receptor system has led to an explosion of knowledge about the structure, expression, and function of this most important fast excitatory transmitter system in the mammalian brain.
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Interleukin-8 and related chemotactic cytokines--CXC and CC chemokines.

TL;DR: In this paper, the authors focused on interleukin-8 (IL-8) and related chemotactic cytokines, namely, CXC and CC chemokines.
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Protein Kinase C: Structure, Function, and Regulation

TL;DR: Multiple receptor pathways feeding into multiple lipid pathways have the common end result of activating protein kinase C by production of its second messenger, diacylglycerol.
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Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

TL;DR: Primary structure predictions indicate that the NAC peptide sequence has a strong tendency to form beta-structures consistent with its association with amyloid, and the availability of the cDNA encoding full-length NACP should help to elucidate the mechanisms of amyloidsosis in AD.
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Metastasis suppressor gene KiSS-1 encodes peptide ligand of a G-protein-coupled receptor.

TL;DR: It is shown that KiSS-1 encodes a carboxy-terminally amidated peptide with 54 amino-acid residues, which is isolated from human placenta as the endogenous ligand of an orphan G-protein-coupled receptor (hOT7T175) and named ‘metastin’.
References
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Journal ArticleDOI

Protein kinase recognition sequence motifs

TL;DR: Identification of phosphorylation site sequences and studies with corresponding model peptides have provided clues to how these important enzymes recognize their substrate proteins, making it possible to identify potential sites ofosphorylation in newly sequenced proteins.
Journal ArticleDOI

Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.

TL;DR: Findings support the idea that multiple basic residues, in particular arginine, on the NH,-terminal side of the phosphorylated serine act as important substrate specificity determinants for the protein kinase.
Journal ArticleDOI

Substrate specificity of protein kinase C: use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements

TL;DR: Comparative studies have demonstrated that, in vivo, the enzyme exhibits a preference for one basic residue C-terminal to the phosphorylatable residue, as in the sequence: Ser/Thr-Xaa-Lys/Arg, where Xaa is usually an uncharged residue.
Journal ArticleDOI

Substrates for p34cdc2: In vivo veritas?

TL;DR: Moreno and Nurse as discussed by the authors identified the in vivo substrates of the p34* protein kinase in eukaryotic cells and demonstrated that in vitro sites in vitro should be identical with the phosphoryla- tion sites in vivo.
Journal ArticleDOI

Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides.

TL;DR: A relatively short sequence of amino acids surrounding the phosphate acceptor site appears to serve as the basis for the specificity of casein kinase II.
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