INT186064

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.59
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 19
Total Number 19
Disease Relevance 7.14
Pain Relevance 1.48

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

cytosol (STAT1) nucleoplasm (STAT1) nucleolus (STAT1)
nucleus (STAT1) enzyme binding (STAT1) cytoplasm (STAT1)
Anatomy Link Frequency
nucleus 4
epithelial cell 2
internal 1
STAT1 (Homo sapiens)
Pain Link Frequency Relevance Heat
methotrexate 18 99.28 Very High Very High Very High
cytokine 621 97.96 Very High Very High Very High
rheumatoid arthritis 85 80.56 Quite High
Inflammation 449 80.00 Quite High
Arthritis 36 72.24 Quite High
metalloproteinase 15 66.28 Quite High
antagonist 49 57.20 Quite High
Leflunomide 15 56.68 Quite High
Potency 10 28.00 Quite Low
imagery 3 23.28 Low Low
Disease Link Frequency Relevance Heat
Asthma 318 95.72 Very High Very High Very High
Disease 166 95.48 Very High Very High Very High
Cancer 250 91.08 High High
Leiomyosarcoma 177 90.48 High High
Stress 27 89.92 High High
Hypoxia 2 89.44 High High
Pancreatic Cancer 8 88.44 High High
Atherosclerosis 132 88.00 High High
Hepatitis C Virus Infection 11 87.28 High High
Necrosis 25 87.04 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
did not appreciably activate ERK and STAT3, but yielded highest level of STAT1 phosphorylation (2441 ± 2073% of OSM level (Fig. 4E &4F).
Phosphorylation (phosphorylation) of STAT1
1) Confidence 0.59 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0 Pain Relevance 0.07
STAT3 phosphorylation by OSM and IL-6, and STAT1 phosphorylation by OSM, IL-6 and IFN?
Phosphorylation (phosphorylation) of STAT1
2) Confidence 0.59 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0.23 Pain Relevance 0.03
to the type II IFN receptor, JAK1 and JAK2 are activated and phosphorylate the signal transducer and activator of transcription 1(STAT1) on the tyrosine residue at position 701 (Tyr701) and the serine residue at position 727 (Ser727) (Parmar and Platanias, 2005; Platanias, 2005) (Fig. 2).
Phosphorylation (phosphorylate) of STAT1
3) Confidence 0.54 Published 2008 Journal Gene Regulation and Systems Biology Section Body Doc Link PMC2733082 Disease Relevance 0.56 Pain Relevance 0
The phosphorylated STAT1 forms homodimers that translocate to the nucleus and bind GAS (IFN-?
Phosphorylation (phosphorylated) of STAT1 in nucleus
4) Confidence 0.54 Published 2008 Journal Gene Regulation and Systems Biology Section Body Doc Link PMC2733082 Disease Relevance 0.57 Pain Relevance 0
to the type II IFN receptor, JAK1 and JAK2 are activated and phosphorylate the signal transducer and activator of transcription 1(STAT1) on the tyrosine residue at position 701 (Tyr701) and the serine residue at position 727 (Ser727) (Parmar and Platanias, 2005; Platanias, 2005) (Fig. 2).
Phosphorylation (phosphorylate) of activator of transcription 1
5) Confidence 0.47 Published 2008 Journal Gene Regulation and Systems Biology Section Body Doc Link PMC2733082 Disease Relevance 0.56 Pain Relevance 0
Separate blots were used to probe for phosphorylated and total STAT1.
Phosphorylation (phosphorylated) of STAT1
6) Confidence 0.45 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0 Pain Relevance 0
Data from 63 separate preparations of normal bronchial epithelial cell cultures indicated that basal level of phosphorylated ERK was consistently low (7.5 ± 5.6 % of OSM level; mean ± SD) and the basal levels of phosphorylated STAT3 and STAT1 were generally low to non-detectable.
Phosphorylation (phosphorylated) of STAT1 in epithelial cell
7) Confidence 0.45 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0.11 Pain Relevance 0.14
To compare the responses between normal and abnormal epithelial cell cultures from individual donors, as well the responses among different donors, the OSM-induced phosphorylation of STAT1, STAT3 and ERK1/2 in the normal cell cultures of each paired set was used as an internal reference (defined as 100).
Phosphorylation (phosphorylation) of STAT1 in internal
8) Confidence 0.45 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0 Pain Relevance 0.03
The level of phosphorylated STAT1, STAT3 and ERK1/2 were quantified and expressed relative to the level of these proteins in OSM-treated normal cultures in each pair (Fig. 4A–F).
Phosphorylation (phosphorylated) of STAT1
9) Confidence 0.45 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1289280 Disease Relevance 0.22 Pain Relevance 0.17
Epigenetic level control, such as methylation, may represent an additional mechanism since a strict correlation exists between demethylation and enhancements in STAT-1 phosphorylation followed by an increase in ISG expression [39].
Phosphorylation (phosphorylation) of STAT-1
10) Confidence 0.44 Published 2010 Journal J Transl Med Section Body Doc Link PMC2845551 Disease Relevance 0.85 Pain Relevance 0
Notably, MTX treatment did reduce the levels of phosphorylation of AKT and STAT1.
Phosphorylation (phosphorylation) of STAT1 associated with methotrexate
11) Confidence 0.39 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2724743 Disease Relevance 0.80 Pain Relevance 0.62
In vitro this SNPs enhances the transcription of SOCS1 in human lung epithelial cells, but reduces phosphorylation of STAT1 stimulated with IFN-?
Phosphorylation (phosphorylation) of STAT1 in epithelial cells
12) Confidence 0.36 Published 2008 Journal J Occup Med Toxicol Section Body Doc Link PMC2259400 Disease Relevance 0.48 Pain Relevance 0.10
[33,37] and dependent upon the induction of the signal transducer and activator of transcription (STAT) STAT1 phosphorylation [38].
Phosphorylation (phosphorylation) of STAT1
13) Confidence 0.30 Published 2005 Journal BMC Infect Dis Section Body Doc Link PMC1208887 Disease Relevance 0.61 Pain Relevance 0
B p65, signal transducers and activators of transcription (STAT1), and STAT3 [38-41], but can also phosphorylate the nucleosomal proteins histone H3 and high-mobility-group 14 (HMG-14).
Phosphorylation (phosphorylate) of STAT1
14) Confidence 0.25 Published 2006 Journal Arthritis Res Ther Section Body Doc Link PMC1526596 Disease Relevance 0.27 Pain Relevance 0
In the indirect mechanism, STAT1 is tyrosine-phosphorylated and dimerized after antocrine/paracrine interactions within IFN-?
Phosphorylation (phosphorylated) of STAT1
15) Confidence 0.25 Published 2010 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2984459 Disease Relevance 0.12 Pain Relevance 0.11
Oxidized LDL (OxLDL) also initiates STAT1 and STAT3 Tyr-phosphorylation and translocation to the nucleus, with a more marked effect for the extensively modified CuLDL.
Phosphorylation (phosphorylation) of STAT1 in nucleus
16) Confidence 0.18 Published 2007 Journal Immun Ageing Section Body Doc Link PMC1845171 Disease Relevance 0.62 Pain Relevance 0.05
Oxidized LDL (OxLDL) also initiates STAT1 and STAT3 Tyr-phosphorylation and translocation to the nucleus, with a more marked effect for the extensively modified CuLDL.
Phosphorylation (-) of STAT1 in nucleus
17) Confidence 0.18 Published 2007 Journal Immun Ageing Section Body Doc Link PMC1845171 Disease Relevance 0.62 Pain Relevance 0.05
Subsequently, the activated JAK2 phosphorylates the receptor and STATs (signal transducer and activator of transcription), and dimers of the latter are translocated to the nucleus to promote gene transcription (Carter-Su and Smit 1998).
Phosphorylation (phosphorylates) of signal transducer and activator of transcription in nucleus
18) Confidence 0.13 Published 2006 Journal International Journal of Nanomedicine Section Body Doc Link PMC2676637 Disease Relevance 0 Pain Relevance 0.07
In one study, Genistein, a nonspecific Tyr-kinase inhibitor, and AG490, a specific inhibitor of JAKs, markedly prevented the CuLDL-induced enhancement of STAT1 and STAT3 Tyr-phosphorylation and DNA-binding activity, suggesting that JAKs are the main kinases involved in STATs' activation by oxidized LDL [125].
Phosphorylation (phosphorylation) of STAT1
19) Confidence 0.08 Published 2007 Journal Immun Ageing Section Body Doc Link PMC1845171 Disease Relevance 0.52 Pain Relevance 0.04

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox