Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains (Q27626998)

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English	Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains	scientific article

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10 November 2019

Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains (English)

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10 November 2019

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10 November 2019

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K M Ferguson

1

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10 November 2019

J M Kavran

2

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10 November 2019

V G Sankaran

3

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10 November 2019

E Fournier

4

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10 November 2019

S J Isakoff

5

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10 November 2019

E Y Skolnik

6

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10 November 2019

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1 August 2000

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10 November 2019

1 reference

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10 November 2019

6

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10 November 2019

2

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10 November 2019

373-384

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10 November 2019

Methods used in the structure determination of bovine mitochondrial F1 ATPase

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A novel integrin-activated pathway forms PKB/Akt-stimulatory phosphatidylinositol 3,4-bisphosphate via phosphatidylinositol 3-phosphate in platelets

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Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate

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Specificity of the purified inositol (1,3,4,5) tetrakisphosphate-binding protein from porcine platelets

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Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin

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Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain

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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate

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High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity

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The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphos

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Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast

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Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain

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Pleckstrin homology domains: a common fold with diverse functions

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Identifiers

10.1016/S1097-2765(00)00037-X

2 references

Consolidated OpenCitations Corpus – April 2017

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Europe PubMed Central

PubMed publication ID

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10 November 2019

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10983984%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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