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1 caused by mutation of the OCRL1 protein, an inositol polyphosphate 5-phosphatase.
2 Inpp5b is an ubiquitously expressed type II inositol polyphosphate 5-phosphatase.
3 ion; and INP53, encoding a synaptojanin-like inositol polyphosphate 5-phosphatase.
4 cerevisiae INP51 locus (YIL002c) encodes an inositol polyphosphate 5-phosphatase.
5 or oculocerebrorenal syndrome (OCRL), is an inositol polyphosphate 5-phosphatase.
6 DXNXR and PXWCDRXL, define a large family of inositol polyphosphate 5-phosphatases.
7 binding sites, and a domain with homology to inositol polyphosphate-5-phosphatases.
9 loning and characterization of a novel human inositol polyphosphate 5-phosphatase (5-phosphatase) tha
16 overlapped between MCF-7 and MCF-10A cells: inositol polyphosphate-5-phosphatase A, corticotropin ho
18 amino-terminal regions similar to mammalian inositol polyphosphate 5-phosphatases and to yeast SAC1.
19 tenin complexes), down-regulation of 51C (an inositol polyphosphate-5-phosphatase), and down-regulati
26 phate (PtdIns(4)P) 5-kinase (PIPKIgamma) and inositol polyphosphate-5-phosphatase E (INPP5E), a Joube
27 ibe a protein-protein interaction network of inositol polyphosphate-5-phosphatase E (INPP5E), a preny
28 ified mutations in the INPP5E gene, encoding inositol polyphosphate-5-phosphatase E, which hydrolyzes
30 th increased expression of the gene encoding inositol polyphosphate-5-phosphatase f (Inpp5f) resultin
34 pleckstrin in platelets is in a complex with inositol polyphosphate 5-phosphatase I (5-phosphatase I)
35 ited in cells microinjected with recombinant inositol polyphosphate 5-phosphatase I, which degrades i
36 ermed SIP-145 and SIP-130 (SIP for signaling inositol polyphosphate 5-phosphatase), identified them a
37 ating each to alanine in the platelet 75 kDa inositol polyphosphate 5-phosphatase II (5-phosphatase I
39 ms of two other 5-phosphatases designated as inositol polyphosphate-5- phosphatase II, and OCRL (the
41 tially suppressed by a mutation in IPP-5, an inositol polyphosphate 5-phosphatase, indicating that on
42 emically-induced dimerization to translocate inositol polyphosphate 5-phosphatase (Inp54p) to plasma
43 P(2) pool by plasma membrane targeting of an inositol polyphosphate-5-phosphatase (Inp54p) blocked PL
44 Ocrl1 deficiency is complemented in mice by inositol polyphosphate 5-phosphatase (Inpp5b), an autoso
46 cible proapoptotic targets of p53, including inositol polyphosphate-5-phosphatase (INPP5D), pleckstri
48 s constitutively expressing the human type I inositol polyphosphate 5-phosphatase (InsP 5-ptase), an
49 cells were transformed with the human type I inositol polyphosphate 5-phosphatase (InsP 5-ptase), an
50 liana plants expressing the mammalian type I inositol polyphosphate 5-phosphatase (InsP 5-ptase), whi
53 bisphosphate even though at least four other inositol polyphosphate 5-phosphatase isozymes are presen
55 drolase 1 (Nceh1), adenylate kinase 1 (Ak1), inositol polyphosphate 5-phosphatase J (Inpp5j), ATP syn
58 is also present at the amino termini of the inositol polyphosphate 5-phosphatases, mammalian synapto
59 tions and that substrates and/or products of inositol polyphosphate 5-phosphatases may have roles in
60 eans, by overexpression of the TGN-localized inositol polyphosphate 5-phosphatase Ocrl, or by blockad
61 Arabidopsis 5PTase13 gene, which encodes an inositol polyphosphate 5-phosphatase previously shown to
64 tor activation by inhibitory coreceptors: an inositol polyphosphate 5'-phosphatase, SHIP, and a tyros
65 the recruitment of the SH2-domain-containing inositol polyphosphate 5-phosphatase, SHIP, to the tyros
69 although it hydrolyzes all four of the known inositol polyphosphate 5-phosphatase substrates: inosito
70 utations in both CVP2 and CVL1, which encode inositol polyphosphate 5'-phosphatases that generate the
71 nsive homology to the SH2 domain of SHIP, an inositol polyphosphate 5-phosphatase that functions as a
73 The subcellular localization of Ocrl, the inositol polyphosphate 5-phosphatase that is mutated in
74 Previous studies revealed that INPP5E, the inositol polyphosphate-5-phosphatase that is mutated in
77 approximately 10-fold greater than the other inositol polyphosphate 5-phosphatases, which use this su
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