Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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A.Berndt,
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(2010).
The p110 delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors.
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Nat Chem Biol, 6,
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PDB codes:
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B.G.Hale,
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Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein.
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Proc Natl Acad Sci U S A, 107,
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Nat Chem Biol, 6,
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Purinergic Signal, 5,
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S9, a novel anticancer agent, exerts its anti-proliferative activity by interfering with both PI3K-Akt-mTOR signaling and microtubule cytoskeleton.
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PLoS ONE, 4,
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A frequent kinase domain mutation that changes the interaction between PI3Kalpha and the membrane.
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Proc Natl Acad Sci U S A, 106,
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PDB codes:
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H.Lempiäinen,
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Emerging common themes in regulation of PIKKs and PI3Ks.
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EMBO J, 28,
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H.Wu,
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Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants.
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Proc Natl Acad Sci U S A, 106,
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K.M.Shokat,
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Isoform-selective phosphoinositide 3'-kinase inhibitors inhibit CXCR4 signaling and overcome stromal cell-mediated drug resistance in chronic lymphocytic leukemia: a novel therapeutic approach.
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Blood, 113,
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Proteins, 75,
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Proc Natl Acad Sci U S A, 105,
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Oncogene, 27,
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R.Beroukhim,
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(2008).
Comprehensive genomic characterization defines human glioblastoma genes and core pathways.
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Nature, 455,
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T.L.Yuan,
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J.V.Frangioni,
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(2008).
Class 1A PI3K regulates vessel integrity during development and tumorigenesis.
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Proc Natl Acad Sci U S A, 105,
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T.L.Yuan,
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PI3K pathway alterations in cancer: variations on a theme.
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Oncogene, 27,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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997 a.a.
139 a.a.
. Residues mutated in cancers are shown as CPK models. The start of the cancer-associated truncation (residue 571 of p85) is shown by the red arrowhead. (B) Electron density map of Arg^38 and Arg^88 cancer mutations shown at the interface between the ABD and the kinase domains. (C) Close-up view of the interface of the C2 domain of p110 with iSH2 of p85. The stick representation of the Asn^345 mutation of C2 and the residues within iSH2 (Asp^560 and Asn^564) with which it may interact are shown. (D) Mutations in the helical domain (Glu^542, Glu^545, and Gln^546), located at the interface with nSH2 (orange surface). (E) Mutations of the kinase domain (Met^1043 and His^1047), located near the C-terminal end of the activation loop, are shown in light green. The part of the activation loop between residues 941 and 950 could not be traced (see text).
