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PTPN6 wt Allele
Known as:
Protein Tyrosine Phosphatase, Non-Receptor Type 6 wt Allele
, SHP-1L
, HCPH
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Human PTPN6 wild-type allele is located within 12p13 and is approximately 29 kb in length. This allele, which encodes tyrosine-protein phosphatase…
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National Institutes of Health
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Related topics
Related topics
15 relations
12p13
Apoptosis
B Cell Receptor Signaling Pathway
Cell Differentiation process
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Broader (1)
PTPN6 gene
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1
H. An
,
J. Hou
,
+6 authors
Xuetao Cao
Nature Immunology
2008
Corpus ID: 3199745
Unbalanced production of proinflammatory cytokines and type I interferons in immune responses may lead to immunopathology; thus…
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Highly Cited
2007
Highly Cited
2007
Ursolic Acid Inhibits STAT3 Activation Pathway Leading to Suppression of Proliferation and Chemosensitization of Human Multiple Myeloma Cells
A. Pathak
,
M. Bhutani
,
+6 authors
B. Aggarwal
Molecular Cancer Research
2007
Corpus ID: 15908477
The activation of signal transducers and activators of transcription 3 (STAT3) has been linked with the proliferation of a…
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Highly Cited
2003
Highly Cited
2003
Vav1 Dephosphorylation by the Tyrosine Phosphatase SHP-1 as a Mechanism for Inhibition of Cellular Cytotoxicity
C. Stebbins
,
C. Watzl
,
D. Billadeau
,
P. Leibson
,
D. Burshtyn
,
Eric O Long
Molecular and Cellular Biology
2003
Corpus ID: 39828531
ABSTRACT Here, we present data suggesting a novel mechanism for regulation of natural killer (NK) cell cytotoxicity through…
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Highly Cited
2003
Highly Cited
2003
The Role of C-terminal Tyrosine Phosphorylation in the Regulation of SHP-1 Explored via Expressed Protein Ligation*
Zhongsen Zhang
,
Kui Shen
,
W. Lu
,
P. Cole
The Journal of Biological Chemistry
2003
Corpus ID: 39322148
The protein-tyrosine phosphatase SHP-1 plays a variety of roles in the “negative” regulation of cell signaling. The molecular…
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Highly Cited
2001
Highly Cited
2001
Loss of HNF-1alpha function in mice leads to abnormal expression of genes involved in pancreatic islet development and metabolism.
D. Shih
,
S. Screenan
,
+5 authors
M. Stoffel
Diabetes
2001
Corpus ID: 22893502
Mutations in hepatocyte nuclear factor 1alpha (HNF-1alpha) lead to maturity-onset diabetes of the young type 3 as a result of…
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Highly Cited
2001
Highly Cited
2001
Specific Dephosphorylation of the Lck Tyrosine Protein Kinase at Tyr-394 by the SHP-1 Protein-tyrosine Phosphatase*
G. Chiang
,
B. Sefton
The Journal of Biological Chemistry
2001
Corpus ID: 26152364
The protein-tyrosine phosphatase SHP-1 has been shown to be a negative regulator of multiple signaling pathways in hematopoietic…
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Highly Cited
2000
Highly Cited
2000
Myeloid specific human CD33 is an inhibitory receptor with differential ITIM function in recruiting the phosphatases SHP-1 and SHP-2.
S. Paul
,
L. Taylor
,
E. K. Stansbury
,
D. McVicar
Blood
2000
Corpus ID: 14429971
CD33 is a myeloid specific member of the sialic acid-binding receptor family and is expressed highly on myeloid progenitor cells…
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Highly Cited
1999
Highly Cited
1999
Leishmania‐induced increases in activation of macrophage SHP‐1 tyrosine phosphatase are associated with impaired IFN‐γ‐triggered JAK2 activation
J. Blanchette
,
Nathalie Racette
,
R. Faure
,
K. Siminovitch
,
M. Olivier
European journal of immunology
1999
Corpus ID: 5014768
Leishmania‐induced macrophage (Mϕ) dysfunctions have been correlated with altered signaling events. Recent findings from our…
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Highly Cited
1998
Highly Cited
1998
Identification of Major Binding Proteins and Substrates for the SH2-Containing Protein Tyrosine Phosphatase SHP-1 in Macrophages
J. Timms
,
K. Carlberg
,
+5 authors
B. Neel
Molecular and Cellular Biology
1998
Corpus ID: 22611041
ABSTRACT The protein tyrosine phosphatase SHP-1 is a critical regulator of macrophage biology, but its detailed mechanism of…
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Highly Cited
1998
Highly Cited
1998
Phosphotyrosine 1173 Mediates Binding of the Protein-tyrosine Phosphatase SHP-1 to the Epidermal Growth Factor Receptor and Attenuation of Receptor Signaling*
H. Keilhack
,
T. Tenev
,
+4 authors
F. Böhmer
The Journal of Biological Chemistry
1998
Corpus ID: 27122489
The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates the epidermal growth factor receptor (EGFR), and both SH2…
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