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HMGB1 — HMGB2
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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IRef Biogrid Interaction:
HMGB1
—
HMGB2
(physical association, affinity chromatography technology)
Krynetski et al., Cancer Res 2003*
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MIPS CORUM HMGB1-HMGB2-HSC70-ERP60-GAPDH complex:
HMGB1-HMGB2-HSC70-ERP60-GAPDH complex complex (GAPDH-HMGB1-HMGB2-HSPA8-PDIA3)
Krynetski et al., Cancer Res 2003*
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IRef Corum Interaction:
Complex of GAPDH-HMGB1-HSPA8-HMGB2-PDIA3
(association, electrophoretic mobility shift assay)
Krynetski et al., Cancer Res 2003*
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IRef Intact Interaction:
Complex of 168 proteins
(association, cross-linking study)
Byron et al., Proteomics 2012
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IRef Intact Interaction:
Complex of 400 proteins
(association, cross-linking study)
Humphries et al., Science signaling 2009
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IRef Intact Interaction:
Complex of 30 proteins
(association, filter binding)
Sgarra et al., Proteomics 2008
Text-mined interactions from Literome
Rabadi et al., American journal of physiology. Renal physiology 2012
(MAP Kinase Signaling System) :
Once released,
HMGB1 in autocrine fashion
promoted further
HMGB1 release while also stimulating NF-?B activity and increased angiopoietin-2 expression and protein release
Javaherian et al., Nucleic Acids Res 1979
:
In a previous communication we have shown that both
HMG1 and HMG2 nonhistone proteins change the DNA helical structure and the binding of HMG1 and
HMG2 to DNA
induces a net unwinding equivalent of DNA double helix ( Javaherian, K., Liu, L. F. and Wang, J. C. ( 1978 ) Science, 199, 1345-1346 )
Luo et al., Eur J Cancer 2013
(Colonic Neoplasms...) :
HMGB1 induced tumour necrosis factor-a secretion via Toll-like receptor (TLR)4 in U937 monocytes ; however,
HMGB1 decreased the number of U937 cells, resulting in restriction of immune activation via receptor for advanced glycation endproducts ( RAGE )