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1 tify a functional role for enigmatic nuclear phosphatidylinositol phosphates.
2 o isolated granule membranes and do not bind phosphatidylinositol phosphates.
3 reviously been used in headgroup analysis of phosphatidylinositol phosphates.
4 phosphorus chemical shifts in NMR spectra of phosphatidylinositol phosphates.
5 gy (PX) domains selectively bind to specific phosphatidylinositol phosphates.
6 ma and internal Na+ via mechanisms requiring phosphatidylinositol phosphates.
7 a likely binding site for the head groups of phosphatidylinositol phosphates.
8 ctor, whereas the PH domain binds to various phosphatidylinositol-phosphates.
9 ly activating the beta isoform of the type I phosphatidylinositol phosphate 5-kinase (PIP5Kbeta) thro
12 us to infect CV1 cells with the mouse type I phosphatidylinositol phosphate 5-kinase alpha (PIP5KI),
15 wever, we demonstrate here that type I gamma phosphatidylinositol phosphate 5-kinase i5 (PIPKIgammai5
18 hat hydrolyze 5-phosphates from a variety of phosphatidylinositol phosphate and inositol phosphate su
20 acylglycerol and concomitant accumulation of phosphatidylinositol phosphate and phosphatidylinositol
21 n the PTEN N-terminus, we tested all natural phosphatidylinositol phosphates and found preferential b
23 ol, phosphatidic acid, phosphatidylinositol, phosphatidylinositol phosphate, and phosphatidylinositol
24 hosphatidylglycerols, phosphatidylinositols, phosphatidylinositol-phosphates, and sulfatides) were sc
25 include lipid kinases with the generation of phosphatidylinositol phosphates as second messengers, al
31 ility; however, the highest-ranking lipid is phosphatidylinositol phosphate, in line with its propose
32 tes but can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidyli
35 hreonine protein kinase (PK) and type IIbeta phosphatidylinositol phosphate kinase (PIPK) structures
39 vation of PIP2-producing enzyme, type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma), by a
40 we show that phosphorylation of type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma661) on
43 signalling, increasing both the activity of phosphatidylinositol phosphate kinase and its associatio
45 uded that the flattened face of type II beta phosphatidylinositol phosphate kinase binds to membranes
46 mma (PIPKIgamma90) is a member of the type I phosphatidylinositol phosphate kinase family that has be
47 This new protein, which we have designated phosphatidylinositol phosphate kinase homolog (PIPKH), i
48 Analytical ultracentrifugation shows that phosphatidylinositol phosphate kinase is a dimer in solu
51 nositol phosphate kinase is a representative phosphatidylinositol phosphate kinase that is active aga
54 tyrosine kinase Src phosphorylates Tyr644 on phosphatidylinositol phosphate kinase type I (PIPKI) gam
56 retion in chromaffin cells from mice lacking phosphatidylinositol phosphate kinase type I gamma, the
58 alin binds to a short C-terminal sequence in phosphatidylinositol phosphate kinase type Igamma (PIPKI
60 another non-integrin talin-binding protein, phosphatidylinositol phosphate kinase type Igamma-90, al
61 he structure of one such enzyme, type IIbeta phosphatidylinositol phosphate kinase, reveals a protein
63 ts of micromolar wortmannin and anti-type II phosphatidylinositol-phosphate kinase antibodies were ad
64 embers of one of these families, the type II phosphatidylinositol phosphate kinases (PIP kinases), ar
65 l G protein and upstream regulator of type I phosphatidylinositol phosphate kinases (PIP5Ks) and PM P
66 he 5 position of the inositol ring by type I phosphatidylinositol phosphate kinases (PIPK): PIPKIalph
73 te is synthesized by two distinct classes of phosphatidylinositol phosphate kinases (PIPKs), the type
75 yrosine-binding domain specifically binds to phosphatidylinositol phosphates known to be produced dur
76 suggest a model whereby local production of phosphatidylinositol phosphates may trigger the binding
77 icantly reduced binding to liposomes lacking phosphatidylinositol phosphates or cholesterol, liposome
78 mologue deleted on chromosome 10 (PTEN) is a phosphatidylinositol phosphate phosphatase and is freque
80 t is lost in many human tumors and encodes a phosphatidylinositol phosphate phosphatase specific for
84 tive method to detect, identify and quantify phosphatidylinositol phosphate (PIP) and phosphatidylino
85 ts of about 100 pmol, and the D3 isoforms of phosphatidylinositol phosphate (PIP) and PIP(2) are dete
87 to PI(4,5)P2 and its generating enzymes, the phosphatidylinositol phosphate (PIP) kinases (PIPKs).
88 also shows significant homology to mammalian phosphatidylinositol phosphate (PIP) kinases and we show
92 ruption of Ptpmt1, a mitochondrial Pten-like phosphatidylinositol phosphate (PIP) phosphatase, result
96 the most widespread, binding specifically to phosphatidylinositol phosphates (PIPs) in cell membranes
99 of Dok7 associates with membranes containing phosphatidylinositol phosphates (PIPs) via interactions
100 residues that are predicted to interact with phosphatidylinositol phosphate (PtdInsP) head groups.
102 its PH domain preferentially interacted with phosphatidylinositol phosphates showing strongest affini
105 tris- and bis-, but not mono-phosphorylated phosphatidylinositol phosphate substrates containing a 5
106 cy altered mitochondrial metabolism and that phosphatidylinositol phosphate substrates of PTPMT1 dire
107 port the structures of a related enzyme, the phosphatidylinositol-phosphate synthase from Renibacteri
108 PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protei
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