Zobrazeno 1 - 8 of 8 pro vyhledávání: '"Jon S. REYNOLDS"'
1
Molecular modelling and site-directed mutagenesis of the inositol 1,3,4,5-tetrakisphosphate-binding pleckstrin homology domain from the Ras GTPase-activating protein GAP1IP4BP
Autor: Gyles COZIER, Richard SESSIONS, Joanna R. BOTTOMLEY, Jon S. REYNOLDS, Peter J. CULLEN
Publikováno v: Biochemical Journal. 349:333-342
GAP1IP4BP is a Ras GTPase-activating protein (GAP) that in vitro is regulated by the cytosolic second messenger inositol 1,3,4,5-tetrakisphosphate [Ins(1,3,4,5)P4]. We have studied Ins(1,3,4,5)P4 binding to GAP1IP4BP, and shown that the inositol phos
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::db04128b8f6abd84d3b6413587cc72f6
https://doi.org/10.1042/bj3490333
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2
Tissue-Specific Expression and Endogenous Subcellular Distribution of the Inositol 1,3,4,5-Tetrakisphosphate-Binding Proteins GAP1IP4BPand GAP1m
Autor: Sara Vanlingen, Robin F. Irvine, Jan B. Parys, Peter J. Lockyer, Jon S. Reynolds, Tracy J. McNulty, Peter J. Cullen
Publikováno v: Biochemical and Biophysical Research Communications. 255:421-426
GAP1 IP4BP and GAP1 m belong to the GAP1 family of Ras GTPase-activating proteins that are candidate InsP 4 receptors. Here we show they are ubiquitously expressed in human tissues and are likely to have tissue-specific splice variants. Analysis by s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed8c847ff16859a6a5e457dd475d33c0
https://doi.org/10.1006/bbrc.1999.0217
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3
Structural and Functional Analysis of the Putative Inositol 1,3,4,5-Tetrakisphosphate Receptors GAP1IP4BPand GAP1m
Autor: Peter J. Cullen, Joanna R. Bottomley, Peter J. Lockyer, Jon S. Reynolds
Publikováno v: Biochemical and Biophysical Research Communications. 250:143-149
Previously we have purified and cloned a high affinity isomerically specific inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P 4 )-binding protein which, because it is clearly a member of the GAP1 family of Ras GTPase-activating proteins (GAP), we ha
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62424d7fb68da784119cc16261b99df9
https://doi.org/10.1006/bbrc.1998.9179
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4
Distinct subcellular localisations of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m result from the GAP1IP4BP PH domain directing plasma membrane targeting
Autor: Barry V. L. Potter, Jon S. Reynolds, Kanamarlapudi Venkateswarlu, Joanna R. Bottomley, Christopher E. Dempsey, Tracy J. McNulty, Peter J. Cullen, Peter J. Lockyer
Publikováno v: Scopus-Elsevier
Inositol 1,3,4,5-tetrakisphosphate (IP4), is a ubiquitous inositol phosphate that has been suggested to function as a second messenger. Recently, we purified and cloned a putative IP4 receptor, termed GAP1(IP4BP)[1], which is also a member of the GAP
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5aedcb980a5eea63e9db08cc09ec41a
https://pubmed.ncbi.nlm.nih.gov/9382842
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8
GAP1IP4BP contains a novel group I pleckstrin homology domain that directs constitutive plasma membrane association
Autor: Sabine Kupzig, Peter J. Cullen, Thomas H. Millard, Joanna R. Bottomley, Peter J. Lockyer, George Banting, Gyles E. Cozier, Jon S. Reynolds
Publikováno v: Europe PubMed Central
The group I family of pleckstrin homology (PH) domains are characterized by their inherent ability to specifically bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) and its corresponding inositol head-group inositol 1,3,4,5-tetrakisph
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1144df352c994155ef7a94ec5d7baeea
http://europepmc.org/abstract/med/10869341
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