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INPP5D gene
Known as:
Inositol Polyphosphate-5-Phosphatase, 145kDa Gene
, SH2 domain-containing inositol 5'-phosphatase 1
, inositol polyphosphate-5-phosphatase D
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This gene is involved in the modulation of signaling.
National Institutes of Health
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Related topics
Related topics
8 relations
Dephosphorylation
Hydrolysis
INPP5A gene
INPP5B gene
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2014
2014
Impaired T cell survival promotes mucosal inflammatory disease in SHIP1-deficient mice
Mi Young Park
,
Neetu Srivastava
,
+5 authors
William G Kerr
Mucosal Immunology
2014
Corpus ID: 15115767
T cells have a critical role in immune surveillance at mucosal surfaces. SHIP1−/− mice succumb to mucosal inflammatory disease…
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2011
2011
An ENU-induced mouse mutant of SHIP1 reveals a critical role of the stem cell isoform for suppression of macrophage activation.
N. Nguyen
,
Mhairi J. Maxwell
,
+9 authors
D. Curtis
Blood
2011
Corpus ID: 18080335
In a recessive ENU mutagenesis screen for embryonic lethality, we identified a mouse pedigree with a missense mutation of SHIP1…
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Highly Cited
2004
Highly Cited
2004
The adaptor protein SH2D1A regulates signaling through CD150 (SLAM) in B cells.
S. Mikhalap
,
L. Shlapatska
,
+5 authors
S. P. Sidorenko
Blood
2004
Corpus ID: 28135695
The CD150 receptor is expressed on activated T and B lymphocytes, dendritic cells, and monocytes. A TxYxxV/I motif in the CD150…
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2002
2002
Association of SH 2-Containing Inositol Phosphatase 2 With the Insulin Resistance of Diabetic db / db Mice
H. Hori
,
T. Sasaoka
,
+4 authors
Masashi Kobayashi
2002
Corpus ID: 26784100
SH-2 containing inositol 5 -phosphatase 2 (SHIP-2) is a physiologically important lipid phosphatase that functions to hydrolyze…
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Highly Cited
2000
Highly Cited
2000
Effects of Src Homology Domain 2 (SH2)-Containing Inositol Phosphatase (SHIP), SH2-Containing Phosphotyrosine Phosphatase (SHP)-1, and SHP-2 SH2 Decoy Proteins on FcγRIIB1-Effector Interactions and…
K. Nakamura
,
A. Brauweiler
,
J. Cambier
Journal of Immunology
2000
Corpus ID: 23129892
Coaggregation of FcγRIIB1 with B cell Ag receptors (BCR) leads to inhibition of BCR-mediated signaling via recruitment of Src…
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Highly Cited
1999
Highly Cited
1999
An SH2 Domain-Containing 5′ Inositolphosphatase Inhibits Insulin-Induced GLUT4 Translocation and Growth Factor-Induced Actin Filament Rearrangement
P. Vollenweider
,
M. Clodi
,
Stuart S. Martin
,
T. Imamura
,
W. Kavanaugh
,
J. Olefsky
Molecular and Cellular Biology
1999
Corpus ID: 21931928
ABSTRACT Tyrosine kinase receptors lead to rapid activation of phosphatidylinositol 3-kinase (PI3 kinase) and the subsequent…
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1999
1999
The SH2-containing inositol-5'-phosphatase enhances LFA-1-mediated cell adhesion and defines two signaling pathways for LFA-1 activation.
J. Rey-Ladino
,
Michael Huber
,
Ling Liu
,
J. Damen
,
Gerald Krystal
,
Fumio Takei
Journal of Immunology
1999
Corpus ID: 44964983
The inside-out signaling involved in the activation of LFA-1-mediated cell adhesion is still poorly understood. Here we examined…
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1999
1999
Role of the Src Homology 2 (SH2) Domain and C-Terminus Tyrosine Phosphorylation Sites of SH2-Containing Inositol Phosphatase (SHIP) in the Regulation of Insulin-Induced Mitogenesis1.
T. Wada
,
T. Sasaoka
,
+4 authors
Masashi Kobayashi
Endocrinology
1999
Corpus ID: 39035535
To examine the role of SHIP in insulin-induced mitogenic signaling, we used a truncated SHIP lacking the SH2 domain (ΔSH2-SHIP…
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1999
1999
Role of the Src homology 2 (SH2) domain and C-terminus tyrosine phosphorylation sites of SH2-containing inositol phosphatase (SHIP) in the regulation of insulin-induced mitogenesis.
T. Wada
,
T. Sasaoka
,
+4 authors
M. Kobayashi
Endocrinology
1999
Corpus ID: 26764287
To examine the role of SHIP in insulin-induced mitogenic signaling, we used a truncated SHIP lacking the SH2 domain (deltaSH2…
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Highly Cited
1998
Highly Cited
1998
Regulation of apoptosis by tyrosine-containing domains of IL-4R alpha: Y497 and Y713, but not the STAT6-docking tyrosines, signal protection from apoptosis.
J. Zamorano
,
A. Keegan
Journal of Immunology
1998
Corpus ID: 333909
IL-4 is a cytokine with important antiapoptotic activity. We have analyzed the role that tyrosine-containing domains within the…
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