INT189030

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Context Info
Confidence 0.31
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 4
Disease Relevance 1.17
Pain Relevance 0.39

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

cytoskeletal protein binding (PTPN3) plasma membrane (PTPN3) cytoskeleton (PTPN3)
cytoplasm (PTPN3)
Anatomy Link Frequency
T cells 1
body 1
spermatozoa 1
PTPN3 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 60 98.20 Very High Very High Very High
sodium channel 2 95.88 Very High Very High Very High
cytokine 80 73.76 Quite High
Inflammatory response 10 60.56 Quite High
nMDA receptor 1 59.48 Quite High
IPN 6 56.64 Quite High
Sciatic nerve 1 53.64 Quite High
Eae 4 45.76 Quite Low
Spontaneous pain 10 42.24 Quite Low
rheumatoid arthritis 2 41.76 Quite Low
Disease Link Frequency Relevance Heat
INFLAMMATION 70 98.20 Very High Very High Very High
Body Weight 2 97.12 Very High Very High Very High
Targeted Disruption 47 95.68 Very High Very High Very High
Stress 19 86.32 High High
Male Infertility 1 74.96 Quite High
Inflammatory Pain 6 56.64 Quite High
Achondroplasia 8 51.84 Quite High
Disease 14 50.00 Quite Low
Anxiety Disorder 8 43.12 Quite Low
Rheumatoid Arthritis 2 41.76 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Recently, our group has demonstrated that PTPH1 dephosphorylates GHR in vitro and in cellular assays [21] and results in an increase of body weight in the functional PTPH1-knockout (KO) mice via modulation of IGF1 secretion [22] thus demonstrating its in vivo relevance.
Phosphorylation (dephosphorylates) of PTPH1 in body associated with targeted disruption and body weight
1) Confidence 0.31 Published 2008 Journal Behav Brain Funct Section Body Doc Link PMC2531118 Disease Relevance 0.35 Pain Relevance 0.10
Indeed, biochemical approaches and substrate trapping experiments identify PTPH1, together with SHP-1, as the phosphatases able to interact and to dephosphorylate TCR?
Phosphorylation (dephosphorylate) of PTPH1
2) Confidence 0.23 Published 2010 Journal J Inflamm (Lond) Section Body Doc Link PMC2873500 Disease Relevance 0 Pain Relevance 0
PTPH1 dephosphorylates TCRzeta in vitro, inhibiting the downstream inflammatory signaling pathway, however no immunological phenotype has been detected in primary T cells derived from PTPH1-KO mice.
Phosphorylation (dephosphorylates) of PTPH1 in T cells associated with inflammation
3) Confidence 0.18 Published 2010 Journal J Inflamm (Lond) Section Abstract Doc Link PMC2873500 Disease Relevance 0.46 Pain Relevance 0.29
The ability of ROS to enhance the tyrosine phosphorylation status of human spermatozoa depends partly on the ability of H2O2 to suppress tyrosine phosphatase activity, and partly on the ability of these molecules to stimulate cAMP generation by the soluble form of adenylyl cyclase (sAC) [16,17].
Phosphorylation (phosphorylation) of tyrosine phosphatase in spermatozoa
4) Confidence 0.09 Published 2005 Journal Reprod Biol Endocrinol Section Body Doc Link PMC1315356 Disease Relevance 0.36 Pain Relevance 0

General Comments

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