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Crystal structure of an inactive Akt2 kinase domain
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title
Crystal structure of an inactive Akt2 kinase domain
(English)
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main subject
crystal structure
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author name string
Xin Huang
series ordinal
1
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Michael Begley
series ordinal
2
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Kurt A Morgenstern
series ordinal
3
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Yan Gu
series ordinal
4
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Paul Rose
series ordinal
5
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Huilin Zhao
series ordinal
6
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Xiaotian Zhu
series ordinal
7
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publication date
January 2003
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published in
Structure
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volume
11
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page(s)
21-30
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issue
1
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cites work
A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
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Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
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Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily
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Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma
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Akt is a direct target of the phosphatidylinositol 3-kinase. Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells
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Myogenic signaling of phosphatidylinositol 3-kinase requires the serine-threonine kinase Akt/protein kinase B.
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Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation.
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Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site.
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Mechanism of activation and function of protein kinase B.
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Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice
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Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene
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Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta)
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Role of AKT1 in 17beta-estradiol- and insulin-like growth factor I (IGF-I)-dependent proliferation and prevention of apoptosis in MCF-7 breast carcinoma cells
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A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain.
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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
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Regulation of protein kinase B.
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Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
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PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2.
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Identifiers
DOI
10.1016/S0969-2126(02)00937-1
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3834254
OpenCitations bibliographic resource ID
3834254
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3834254
PubMed ID
12517337
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3834254
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