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Search results 701 to 800 out of 895 for Hmgb1

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Type Details Score
Publication
31026770 | J:294809
 
First Author: Kwak MS
Year: 2019
Journal: Redox Biol
Title: Peroxiredoxin-mediated disulfide bond formation is required for nucleocytoplasmic translocation and secretion of HMGB1 in response to inflammatory stimuli.
Volume: 24
Pages: 101203
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Publication
34210972 | J:340204
First Author: Lou MM
Year: 2021
Journal: Nat Commun
Title: Long noncoding RNA BS-DRL1 modulates the DNA damage response and genome stability by interacting with HMGB1 in neurons.
Volume: 12
Issue: 1
Pages: 4075
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Publication
29421543 | J:257482
 
First Author: Wang X
Year: 2018
Journal: Neurosci Lett
Title: Sigma 1 receptor mediated HMGB1 expression in spinal cord is involved in the development of diabetic neuropathic pain.
Volume: 668
Pages: 164-168
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Publication
17513788 | J:147826
First Author: Tang D
Year: 2007
Journal: J Immunol
Title: Nuclear heat shock protein 72 as a negative regulator of oxidative stress (hydrogen peroxide)-induced HMGB1 cytoplasmic translocation and release.
Volume: 178
Issue: 11
Pages: 7376-84
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Publication
28844955 | J:255470
First Author: Jiang Y
Year: 2017
Journal: Biochim Biophys Acta
Title: BRD4 has dual effects on the HMGB1 and NF-κB signalling pathways and is a potential therapeutic target for osteoarthritis.
Volume: 1863
Issue: 12
Pages: 3001-3015
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Publication
20547845 | J:161368
First Author: Yang H
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: A critical cysteine is required for HMGB1 binding to Toll-like receptor 4 and activation of macrophage cytokine release.
Volume: 107
Issue: 26
Pages: 11942-7
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Publication
30971430 | J:280420
First Author: Yu S
Year: 2019
Journal: J Biol Chem
Title: The complement receptor C5aR2 promotes protein kinase R expression and contributes to NLRP3 inflammasome activation and HMGB1 release from macrophages.
Volume: 294
Issue: 21
Pages: 8384-8394
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Publication
37441587 | J:354338
First Author: Du S
Year: 2023
Journal: Theranostics
Title: Hepatocyte HSPA12A inhibits macrophage chemotaxis and activation to attenuate liver ischemia/reperfusion injury via suppressing glycolysis-mediated HMGB1 lactylation and secretion of hepatocytes.
Volume: 13
Issue: 11
Pages: 3856-3871
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Publication
21642542 | J:176186
First Author: Liu Z
Year: 2011
Journal: J Immunol
Title: Knockdown of HMGB1 in tumor cells attenuates their ability to induce regulatory T cells and uncovers naturally acquired CD8 T cell-dependent antitumor immunity.
Volume: 187
Issue: 1
Pages: 118-25
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Publication
19890065 | J:157164
First Author: Qin YH
Year: 2009
Journal: J Immunol
Title: HMGB1 enhances the proinflammatory activity of lipopolysaccharide by promoting the phosphorylation of MAPK p38 through receptor for advanced glycation end products.
Volume: 183
Issue: 10
Pages: 6244-50
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Publication
21763292 | J:176474
First Author: Ha YM
Year: 2011
Journal: Biochem Pharmacol
Title: β₁-adrenergic receptor-mediated HO-1 induction, via PI3K and p38 MAPK, by isoproterenol in RAW 264.7 cells leads to inhibition of HMGB1 release in LPS-activated RAW 264.7 cells and increases in survival rate of CLP-induced septic mice.
Volume: 82
Issue: 7
Pages: 769-77
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Publication
12110890 | -
First Author: Scaffidi P
Year: 2002
Journal: Nature
Title: Release of chromatin protein HMGB1 by necrotic cells triggers inflammation.
Volume: 418
Issue: 6894
Pages: 191-5
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Publication
26078984 | -
 
First Author: Lu M
Year: 2015
Journal: J Immunol Res
Title: HMGB1 Promotes Systemic Lupus Erythematosus by Enhancing Macrophage Inflammatory Response.
Volume: 2015
Pages: 946748
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Publication
12818428 | -
First Author: Dasgupta A
Year: 2003
Journal: Biochim Biophys Acta
Title: TFIIA abrogates the effects of inhibition by HMGB1 but not E1A during the early stages of assembly of the transcriptional preinitiation complex.
Volume: 1627
Issue: 2-3
Pages: 101-10
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Publication
22544226 | -
First Author: Polanská E
Year: 2012
Journal: Chromosoma
Title: HMGB1 gene knockout in mouse embryonic fibroblasts results in reduced telomerase activity and telomere dysfunction.
Volume: 121
Issue: 4
Pages: 419-31
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Publication
3743550 | -
First Author: Chatterjee PK
Year: 1986
Journal: EMBO J
Title: Adenoviral protein VII packages intracellular viral DNA throughout the early phase of infection.
Volume: 5
Issue: 7
Pages: 1633-44
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Publication
27362237 | -
First Author: Avgousti DC
Year: 2016
Journal: Nature
Title: A core viral protein binds host nucleosomes to sequester immune danger signals.
Volume: 535
Issue: 7610
Pages: 173-7
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Protein Domain
IPR004912 | Adeno_VII
Type: Family
Description: Adenoviruses encode a highly basic protein called protein VII that resembles cellular histones. Protein VII forms complexes with nucleosomes, limiting DNA accessibility, and sequesters protein HMGB1 in the chromatin. HMGB1 is normally released in response to inflammatory stimuli and mediates activation of immune responses. This is thought to be part of a viral strategy to control extracellular immune signaling []. Protein VII also plays a role in packaging the viral DNA [].
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Publication
16600991 | J:109515
First Author: Paracchini S
Year: 2006
Journal: Hum Mol Genet
Title: The chromosome 6p22 haplotype associated with dyslexia reduces the expression of KIAA0319, a novel gene involved in neuronal migration.
Volume: 15
Issue: 10
Pages: 1659-66
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Protein
A2A786
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
A2A787
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: true
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Publication
20697954 | -
First Author: Poon MW
Year: 2011
Journal: Cell Mol Neurobiol
Title: Dyslexia-associated kiaa0319-like protein interacts with axon guidance receptor nogo receptor 1.
Volume: 31
Issue: 1
Pages: 27-35
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Publication
16781891 | -
First Author: McGrath LM
Year: 2006
Journal: Trends Mol Med
Title: Breakthroughs in the search for dyslexia candidate genes.
Volume: 12
Issue: 7
Pages: 333-41
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Publication
20956978 | -
First Author: Poelmans G
Year: 2011
Journal: Mol Psychiatry
Title: A theoretical molecular network for dyslexia: integrating available genetic findings.
Volume: 16
Issue: 4
Pages: 365-82
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Protein Domain
IPR029865 | KIAA0319-like
Type: Family
Description: Several dyslexia-associated proteins have been identified: ROBO1, KIAA0319, KIAA0319L, S100B, DOCK4, FMR1, DIP2A, GTF2I, DYX1C, DCDC2, SLIT2, HMGB1 and VAPA [, ]. This entry includes KIAA0319 and KIAA0319-like (KIAA0319L) proteins. KIAA0319 is required for neuronal migration during the formation of the cerebral neocortex []. KIAA0319L has a possible role in axon guidance through interaction with nogo receptor 1 [].
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Protein
D6RIQ7
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
D3Z7C2
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Protein
Q3UT44
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q05C74
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: false
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Publication
8610010 | -
First Author: Tan S
Year: 1996
Journal: Nature
Title: Crystal structure of a yeast TFIIA/TBP/DNA complex.
Volume: 381
Issue: 6578
Pages: 127-51
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Protein
E0CYD4
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: true
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Protein
Q3USX2
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: true
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Publication
11089979 | -
First Author: Yudkovsky N
Year: 2000
Journal: Nature
Title: A transcription reinitiation intermediate that is stabilized by activator.
Volume: 408
Issue: 6809
Pages: 225-9
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Protein Domain
IPR004855 | TFIIA_asu/bsu
Type: Family
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the precursor that yields both the alpha and beta subunits of TFIIA. The TFIIA heterotrimer is an essential general transcription initiation factor for the expression of genes transcribed by RNA polymerase II [].
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Protein Domain
IPR009083 | TFIIA_a-hlx
Type: Homologous_superfamily
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcriptionpre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This superfamily represents the α-helical domain found at the N-terminal of the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR009088 | TFIIA_b-brl
Type: Homologous_superfamily
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This superfamily represents the β-barrel domain found at the C-terminal of both TOA1 (or alpha/beta) and TOA2 (or gamma) subunits of TFIIA, and their homologues.
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Protein Domain
IPR003194 | TFIIA_gsu
Type: Family
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR015871 | TFIIA_gsu_C
Type: Domain
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the β-barrel domain found at the C-terminal of the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR015872 | TFIIA_gsu_N
Type: Domain
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the α-helical domain found at the N-terminal of the gamma subunit of transcription factor TFIIA.
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Protein
Q80ZM7
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
D3Z7S8
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
Q3TN86
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Protein
D3Z793
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
Q3TE88
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
Q99PM3
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein
Q8R4I4
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: false
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Protein
Q149E9
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
A2A788
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Protein
Q0VGZ0
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Publication
22469986 | J:193364
First Author: Heijmans J
Year: 2013
Journal: Oncogene
Title: Rage signalling promotes intestinal tumourigenesis.
Volume: 32
Issue: 9
Pages: 1202-6
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Publication
14581561 | -
First Author: Zhang G
Year: 2003
Journal: J Virol
Title: Borna disease virus phosphoprotein represses p53-mediated transcriptional activity by interference with HMGB1.
Volume: 77
Issue: 22
Pages: 12243-51
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Publication
8523585 | -
First Author: Kishi M
Year: 1996
Journal: J Virol
Title: Sequence variability of Borna disease virus open reading frame II found in human peripheral blood mononuclear cells.
Volume: 70
Issue: 1
Pages: 635-40
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Publication
9811743 | -
First Author: Iwata Y
Year: 1998
Journal: J Virol
Title: Detection and sequence analysis of borna disease virus p24 RNA from peripheral blood mononuclear cells of patients with mood disorders or schizophrenia and of blood donors.
Volume: 72
Issue: 12
Pages: 10044-9
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Publication
18623121 | -
First Author: Nunes SO
Year: 2008
Journal: J Clin Lab Anal
Title: RNA from Borna disease virus in patients with schizophrenia, schizoaffective patients, and in their biological relatives.
Volume: 22
Issue: 4
Pages: 314-20
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Publication
16324750 | -
First Author: Miranda HC
Year: 2006
Journal: J Affect Disord
Title: Detection of Borna disease virus p24 RNA in peripheral blood cells from Brazilian mood and psychotic disorder patients.
Volume: 90
Issue: 1
Pages: 43-7
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Protein Domain
IPR009517 | BDV_P24
Type: Family
Description: Borna disease virus (BDV) is a non-cytolytic, neurotropic RNA virus that has a broad host range in warm-blooded animals. BDV is an enveloped virus, non-segmented, negative-stranded RNA genome and has an organisation characteristic of a member of Bornaviridae in the order of Mononegavirale. This family consists of several BDV P24 (phosphoprotein 24) proteins. They are essential components of the RNA polymerase transcription and replication complex. P24 is encoded by open reading frame II (ORF-II) and undergoes high rates of mutation in humans. They bind amphoterin-HMGB1, a multifunctional protein, directly may cause deleterious effects in cellular functions by its interference with HMGB1 []. Horse and human P24 have no species-specific amino acid residues, suggesting that the two viruses related [, ].Numerous interactions of the immune system with the central nervous system have been described. Mood and psychotic disorders, such as severe depression and schizophrenia, are both heterogeneous disorders regarding clinical symptomatology, the acuity of symptoms, the clinical course and the treatment response []. BDV p24 RNA has been detected in the peripheral blood mononuclear cells (PBMCs) of psychiatric patients with such conditions []. Some studies find a significant difference in the prevalence of BDV p24 RNA in patients with mood disorders and schizophrenia [], whilst others find no difference between patients and control groups []. Consequently, debate about the role of BDV in psychiatric diseases remains alive.
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Publication
24492532 | J:244194
 
First Author: Van Opdenbosch N
Year: 2014
Journal: Nat Commun
Title: Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation.
Volume: 5
Pages: 3209
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Publication
32522835 | J:294822
First Author: Geng Y
Year: 2020
Journal: J Immunol
Title: HMGB1-Neutralizing IgM Antibody Is a Normal Component of Blood Plasma.
Volume: 205
Issue: 2
Pages: 407-413
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Publication
37733587 | J:342099
First Author: Focken J
Year: 2023
Journal: Cell Rep
Title: Neutrophil extracellular traps enhance S. aureus skin colonization by oxidative stress induction and downregulation of epidermal barrier genes.
Volume: 42
Issue: 10
Pages: 113148
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Publication
23630347 | J:204779
First Author: Shimizu K
Year: 2013
Journal: J Immunol
Title: Invariant NKT cells induce plasmacytoid dendritic cell (DC) cross-talk with conventional DCs for efficient memory CD8+ T cell induction.
Volume: 190
Issue: 11
Pages: 5609-19
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Publication
20348922 | J:159308
First Author: Maroso M
Year: 2010
Journal: Nat Med
Title: Toll-like receptor 4 and high-mobility group box-1 are involved in ictogenesis and can be targeted to reduce seizures.
Volume: 16
Issue: 4
Pages: 413-9
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Publication
25348021 | J:278392
 
First Author: Yu LX
Year: 2014
Journal: Nat Commun
Title: Platelets promote tumour metastasis via interaction between TLR4 and tumour cell-released high-mobility group box1 protein.
Volume: 5
Pages: 5256
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Publication
29109024 | J:360232
 
First Author: Huang J
Year: 2018
Journal: Brain Behav Immun
Title: AMPK regulates immunometabolism in sepsis.
Volume: 72
Pages: 89-100
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Publication
27779186 | J:242646
 
First Author: Xie M
Year: 2016
Journal: Nat Commun
Title: PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation.
Volume: 7
Pages: 13280
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Publication
22521241 | J:188302
First Author: Kawakami M
Year: 2012
Journal: Cell Immunol
Title: The role of CCR7 in allergic airway inflammation induced by house dust mite exposure.
Volume: 275
Issue: 1-2
Pages: 24-32
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Publication
27294203 | J:236028
 
First Author: Yang H
Year: 2016
Journal: JCI Insight
Title: Identification of CD163 as an antiinflammatory receptor for HMGB1-haptoglobin complexes.
Volume: 1
Issue: 7
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Publication
36691613 | J:332859
First Author: Peng Z
Year: 2023
Journal: iScience
Title: PKR deficiency delays vascular aging via inhibiting GSDMD-mediated endothelial cell hyperactivation.
Volume: 26
Issue: 1
Pages: 105909
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Publication
30100261 | J:270527
First Author: Li C
Year: 2018
Journal: Dev Cell
Title: PINK1 and PARK2 Suppress Pancreatic Tumorigenesis through Control of Mitochondrial Iron-Mediated Immunometabolism.
Volume: 46
Issue: 4
Pages: 441-455.e8
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Publication
39423817 | J:358173
First Author: Fu M
Year: 2024
Journal: Cancer Cell
Title: Overcoming tyrosine kinase inhibitor resistance in lung cancer brain metastasis with CTLA4 blockade.
Volume: 42
Issue: 11
Pages: 1882-1897.e7
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Publication
23601685 | J:196961
First Author: Zou J
Year: 2013
Journal: Immunity
Title: Poly IC triggers a cathepsin D- and IPS-1-dependent pathway to enhance cytokine production and mediate dendritic cell necroptosis.
Volume: 38
Issue: 4
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