Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain. - Test2 - elhamkhani - TriplyDB

Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain.

Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain.

http://www.wikidata.org/entity/Q37657049

about

The emerging roles of inositol pyrophosphates in eukaryotic cell physiology The enzymes of human diphosphoinositol polyphosphate metabolism Biosynthesis and possible functions of inositol pyrophosphates in plants Structural insight into inositol pyrophosphate turnover The Vip1 inositol polyphosphate kinase family regulates polarized growth and modulates the microtubule cytoskeleton in fungi Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding Inositol pyrophosphates: why so many phosphates?Inositol Pyrophosphate Kinase Asp1 Modulates Chromosome Segregation Fidelity and Spindle Function in Schizosaccharomyces pombe.The kinetic properties of a human PPIP5K reveal that its kinase activities are protected against the consequences of a deteriorating cellular bioenergetic environment.Identification of a functional nuclear translocation sequence in hPPIP5K2.Genome wide in silico analysis of Plasmodium falciparum phosphatome.Asp1 from Schizosaccharomyces pombe binds a [2Fe-2S](2+) cluster which inhibits inositol pyrophosphate 1-phosphatase activity Inositol pyrophosphates as mammalian cell signals PPIP5K1 modulates ligand competition between diphosphoinositol polyphosphates and PtdIns(3,4,5)P3 for polyphosphoinositide-binding domains.Conditional peripheral membrane proteins: facing up to limited specificity.Inositol pyrophosphates: between signalling and metabolism.Intimate connections: Inositol pyrophosphates at the interface of metabolic regulation and cell signaling.Two inositol hexakisphosphate kinases drive inositol pyrophosphate synthesis in plants.When worlds collide: inositol pyrophosphates and phosphoinositides intersect at the plasma membrane.The inositol pyrophosphate pathway in health and diseases.Inositol Polyphosphate Kinases, Fungal Virulence and Drug Discovery.Inositol Pyrophosphate Synthesis by Diphosphoinositol Pentakisphosphate Kinase-1 is Regulated by Phosphatidylinositol(4,5)bisphosphate.Mutations in Diphosphoinositol-Pentakisphosphate Kinase PPIP5K2 are associated with hearing loss in human and mouse.

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P2860

Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain.

http://www.wikidata.org/entity/Q37657049

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

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bilimsel makale

@tr

scientific article published on March 2011

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Receptor-dependent compartment ...... osphoinositide binding domain.

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Receptor-dependent compartment ...... osphoinositide binding domain.

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type

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Receptor-dependent compartment ...... osphoinositide binding domain.

@en

Receptor-dependent compartment ...... osphoinositide binding domain.

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prefLabel

Receptor-dependent compartment ...... osphoinositide binding domain.

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Receptor-dependent compartment ...... osphoinositide binding domain.

@nl

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Biochemical Journal

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Receptor-dependent compartment ...... osphoinositide binding domain.

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P2093

Angelika Zaremba

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Nikhil A Gokhale

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Stephen B Shears

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P2860

The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification

Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family

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Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains

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Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt

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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis

Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells

Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains

P304

415-426

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scholarly article

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10.1042/BJ20101437

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3

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434

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2011-03-01T00:00:00Z

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21222653

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3962999

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