(Q36313197)

13 August 2017

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title

AKT crystal structure and AKT-specific inhibitors (English)

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13 August 2017

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Chandra C Kumar

1

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13 August 2017

Vincent Madison

series ordinal

2

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13 August 2017

language of work or name

English

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publication date

1 November 2005

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13 August 2017

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13 August 2017

24

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13 August 2017

50

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13 August 2017

7493-7501

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https://scigraph.springernature.com/pub.10.1038/sj.onc.1209087

13 August 2017

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Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase

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Perturbations of the AKT signaling pathway in human cancer

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Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates

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AKT2 is frequently upregulated in HER-2/neu-positive breast cancers and may contribute to tumor aggressiveness by enhancing cell survival

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The Akt/PKB family of protein kinases: a review of small molecule inhibitors and progress towards target validation

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Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants

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Structure-based optimization of novel azepane derivatives as PKB inhibitors

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Preferential inhibition of Akt and killing of Akt-dependent cancer cells by rationally designed phosphatidylinositol ether lipid analogues

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Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA

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The multiple roles of PTEN in tumor suppression

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Regulation of neuronal survival by the serine-threonine protein kinase Akt

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PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth

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The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/threonine kinase, Akt.

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Inhibition of Akt kinase activity by a peptide spanning the betaA strand of the proto-oncogene TCL1.

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Crystal structure of an inactive Akt2 kinase domain

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Involvement of Akt kinase in the action of STI571 on chronic myelogenous leukemia cells

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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Akt-dependent and -independent survival signaling pathways utilized by insulin-like growth factor I.

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Expression, purification, characterization and homology modeling of active Akt/PKB, a key enzyme involved in cell survival signaling

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Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors

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Potent and selective inhibitors of Akt kinases slow the progress of tumors in vivo

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Pseudosubstrate peptides inhibit Akt and induce cell growth inhibition

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Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change

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Different inhibitory effect of imatinib on phosphorylation of mitogen-activated protein kinase and Akt and on proliferation in cells expressing different types of mutant platelet-derived growth factor receptor-alpha

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EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy

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Breast cancer--loss of PTEN predicts resistance to treatment

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Regulation of protein kinases in insulin, growth factor and Wnt signalling

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7 January 2021

Toward a PKB inhibitor: modification of a selective PKA inhibitor by rational design

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Adenovirus-mediated transfer of the PTEN gene inhibits human colorectal cancer growth in vitro and in vivo

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7 January 2021

Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies

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Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways

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High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate

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7 January 2021

Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1209087

7 January 2021

Catalytic domain crystal structure of protein kinase C-theta (PKCtheta).

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1209087

7 January 2021

Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1209087

7 January 2021

Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation

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7 January 2021

Discovery of 2,3,5-trisubstituted pyridine derivatives as potent Akt1 and Akt2 dual inhibitors

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7 January 2021

Identifiers

DOI

10.1038/SJ.ONC.1209087

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Dimensions Publication ID

13 August 2017

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