The Protein Kinase Complement of the Human Genome

By Gerard Manning, D. Whyte, R. Martinez, T. Hunter, S. Sudarsanam. Science, 2002

8,029 citations recorded by the source corpus.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/3aa3723f9d851b9f845508e8e64fb6fda2158d24

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Citations in the corpus

A small molecule–kinase interaction map for clinical kinase inhibitors (2005, background): “The vast majority of these compounds target the kinase ATP site, and because all of the more than 500 protein kinases identified in the human genome have an ATP sit”
A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen. (2006, background): “The targeted genes included 476 protein kinases and 180 phosphatases that represent 88% and 80%, respectively, of known NCBI reference sequences assigned to these gene classes (Manning et al., 2002).”
Protein Kinases: Evolution of Dynamic Regulatory Proteins (2010, background): “About 10% of the human kinome contain most of the major sequence motifs that define the eukaryotic protein kinase structure, specifically the Activation Loop and the helical GHI subdomain, as discussed above, but harbor mutations in positions that were thought to be crucially important for catalysis”
Comparative Analysis of the Receptor-Like Kinase Family in Arabidopsis and Rice (2004, background): “…in meristem maintenance (Clark et al., 1997), BRI1 in the regulation of cell growth (Li and Chory, 1997), maize CRINKLY4 in controlling cell morphogenesis and differentiation (Becraft et al., 1996), and carrot (Daucus carota) PSKR in controlling cell proliferation (Matsubayashi et al., 2002).”
Mechanisms of specificity in protein phosphorylation (2007, background): “It affects every basic cellular process, including metabolism, growth, division, differentiation, motility, organelle trafficking, membrane transport, muscle contraction, immunity, learning and memor”
The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. (2013, background): “MLKL is classified as a ‘‘pseudokinase’’ because its kinaselike domain lacks two of the three conserved catalytic residues considered crucial for phosphoryl transfer activity (Manning et al., 2002).”
Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy (2010, background): “The ATP-binding pocket of kinases is a classical target for the design of inhibitors and has been validated by several successful strategies to inhibit members of the human kinom”
Using Sequence Similarity Networks for Visualization of Relationships Across Diverse Protein Superfamilies (2009, methodology): “The kinase sequences and annotations were drawn from the base set of 621 human kinase domains in Kinbase (available at http://kinase.com/kinbase)[18] on Mar. 5, 2008.”
Preclinical overview of sorafenib, a multikinase inhibitor that targets both Raf and VEGF and PDGF receptor tyrosine kinase signaling (2008, background): “5) and the ongoing clinical development of over 30 targeted protein kinase inhibitors designed to inhibit tumor growth and progression offer promise for the future (6, 7).”
Large-scale integration of small molecule-induced genome-wide transcriptional responses, Kinome-wide binding affinities and cell-growth inhibition profiles reveal global trends characterizing systems-level drug action (2014, methodology): “We organized all kinase domains by an extended phylogenetic classiﬁcation tree that we based largely on the Sugen kinase classiﬁcation (Manning et al., 2002) 10 .”
The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis (2007, background): “Subsequent cloning of two other related human genes and the post-genome characterization of the human kinome completed the description of this family of four members (Kraus et al., 1989; Plowman et al., 1993; Manning et al., 2002).”
S6K1−/−/S6K2−/− Mice Exhibit Perinatal Lethality and Rapamycin-Sensitive 5′-Terminal Oligopyrimidine mRNA Translation and Reveal a Mitogen-Activated Protein Kinase-Dependent S6 Kinase Pathway (2004, result): “That S6K1 and S6K2 are the only genes coding for rapamycin-sensitive S6Ks is consistent with two other S6K genes identified by the human genome project representing pseudogenes ( 34 ).”