INT210193

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Context Info
Confidence 0.44
First Reported 2007
Last Reported 2010
Negated 2
Speculated 1
Reported most in Body
Documents 31
Total Number 33
Disease Relevance 6.88
Pain Relevance 0.78

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

nucleoplasm (TXN) transport (TXN) mitochondrion (TXN)
small molecule metabolic process (TXN) cell-cell signaling (TXN) cytoplasm (TXN)
Anatomy Link Frequency
lymphocytes 3
plasma 2
HeLa 2
HDLM-2 1
upper 1
TXN (Homo sapiens)
Pain Link Frequency Relevance Heat
member 8 62 98.12 Very High Very High Very High
Inflammation 250 91.28 High High
cytokine 93 82.68 Quite High
Inflammatory response 67 70.84 Quite High
agonist 31 66.32 Quite High
rheumatoid arthritis 31 64.92 Quite High
palliative 4 5.00 Very Low Very Low Very Low
dexamethasone 2 5.00 Very Low Very Low Very Low
peripheral neuropathy 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Diarrhoea 2 99.44 Very High Very High Very High
Lymphatic System Cancer 217 99.42 Very High Very High Very High
Vomiting 18 98.88 Very High Very High Very High
Alopecia 6 98.16 Very High Very High Very High
Neutropenia 2 97.76 Very High Very High Very High
Stress 93 97.52 Very High Very High Very High
Leukopenia 8 97.24 Very High Very High Very High
Anaemia 22 96.76 Very High Very High Very High
Necrosis 64 96.64 Very High Very High Very High
Cancer 92 96.28 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In brief, we allowed mutant Trx1 to interact with the surface of live cells, removed unreacted oxidoreductase by washing and collected disulfide-linked Trx1 complexes from cellular lysates by streptavidin (SAv) affinity purification.
Trx1 Binding (interact) of
1) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
Kinetic trapping can be applied to detect Trx1 interactions on the cell surface
Trx1 Binding (interactions) of
2) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
The Trx1–Prx1 association was further confirmed by immunoblotting (data not shown).
Trx1 Binding (association) of
3) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
We demonstrate that Trx1 interacts with intra- and extracellular target proteins in a highly selective manner, guided by specific protein–protein recognition rather than random encounters with disulfide bonds.
Trx1 Binding (interacts) of
4) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.22 Pain Relevance 0.10
Interestingly, we found that Trx1 predominantly engages a single protein on the lymphoblastoid surface, suggesting a highly selective interaction (Figure 2A, lane 3).
Trx1 Binding (engages) of
5) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.29 Pain Relevance 0
Trx1 is recognized as one of the most important regulators of cellular and organismal redox homeostasis (Gromer et al, 2004).
Trx1 Binding (recognized) of
6) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.33 Pain Relevance 0.04
In contrast, expression of CD95 (Figure 4D), TNFR1 or NGFR (data not shown) did not promote Trx1 interactions with the cell surface, further strengthening the notion that Trx1 reactivity is a specific property of CD30.
Trx1 Neg (not) Binding (interactions) of
7) Confidence 0.44 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.11 Pain Relevance 0
In this study, we address the question as to which cell surface receptors expressed on lymphocytes specifically interact with extracellular Trx1 by way of disulfide bond exchange.
Trx1 Binding (interact) of in lymphocytes
8) Confidence 0.38 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.22 Pain Relevance 0.03
While mock-transfected HeLa cells did not capture Trx1(CSAAA) on their surface (Figure 4C, lower row), expression of CD30 led to a strong Trx1 surface association and colocalization of both proteins (Figure 4C, upper row).
Trx1 Binding (association) of in HeLa
9) Confidence 0.38 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
To test whether Trx1(CSAAA) would also undergo authentic interactions under conditions more typical of an extracellular environment, we allowed Trx1(CSAAA) to react with human plasma proteins.
Trx1 Binding (interactions) of in plasma
10) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
To exclude the possibility that Trx1 interacts with CRDs uniformly, we tested whether Trx1 discriminates between distinct members of the TNFR superfamily.
Trx1 Binding (interacts) of
11) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0
A brief incubation of CD30+Hodgkin's lymphoma HDLM-2 cells with wild-type Trx1 led to a substantial loss in CD30L binding to the cell surface (Figure 6A).
Trx1 Binding (binding) of in HDLM-2 associated with lymphatic system cancer
12) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.19 Pain Relevance 0
The interaction between Trx1 and CD30 might represent a regulatory link between oxidative stress and lymphocyte function.
Trx1 Spec (might) Binding (interaction) of in lymphocyte associated with stress
13) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.93 Pain Relevance 0.18
Conversely, ectopic overexpression of several related TNFR superfamily members in HeLa cells did not lead to their interaction with Trx1, yet CD30 strongly interacted on the same cells under the same conditions.
Trx1 Binding (interaction) of in HeLa
14) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.09 Pain Relevance 0
To validate the direct covalent interaction between Trx1(CSAAA) and CD30, an aliquot of trapped complexes from the same experiment was separated under non-reducing and reducing conditions and subjected to immunoblotting analysis with anti-Trx1 (Figure 3A, middle panel) and anti-CD30 antibodies (Figure 3A, right panel), respectively.
Trx1 Binding (interaction) of
15) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.11 Pain Relevance 0
To test whether Trx1-mediated reduction of CD30 influences binding of CD30 to its ligand (CD30L), we analyzed the interaction between CD30 and recombinant soluble CD30L (sCD30L) on the cell surface by flow cytometry.
Trx1 Binding (influences) of
16) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.15 Pain Relevance 0
Kinetic trapping on the surface of lymphoid cell lines identifies a prominent Trx1 interaction partner
Trx1 Binding (interaction) of
17) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.09 Pain Relevance 0
Trx1-mediated disulfide exchange interferes with CD30 receptor–ligand interactions
Trx1 Binding (exchange) of
18) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.11 Pain Relevance 0
Kinetic trapping on the surface of lymphoid cell lines identifies a prominent Trx1 interaction partner
Trx1 Binding (partner) of
19) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0.09 Pain Relevance 0
Additional immunoblotting experiments demonstrated that low nanomolar concentrations of Trx1(CSAAA) are sufficient to detect the interaction with CD30 (Figure 3B) and also confirmed that trapping of CD30 depends on the N-terminal cysteine of the CXXC motif (Figure 3C, lanes 1–8).
Trx1 Binding (interaction) of
20) Confidence 0.34 Published 2007 Journal EMBO J Section Body Doc Link PMC1914094 Disease Relevance 0 Pain Relevance 0

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