Results 11 to 20 of about 41,752 (255)

Metabolic Syndrome and Autophagy: Focus on HMGB1 Protein. [PDF]

open access: yesFront Cell Dev Biol, 2021
Metabolic syndrome (MetS) affects the population worldwide and results from several factors such as genetic background, environment and lifestyle. In recent years, an interplay among autophagy, metabolism, and metabolic disorders has become apparent.
Frisardi V, Matrone C, Street ME.
europepmc   +7 more sources

HMGB1 protein as a novel target for cancer. [PDF]

open access: yesToxicol Rep, 2019
Highly conserved nuclear protein High Mobility Group Box1 (HMGB1) present in mammals has functionality as an immuno-modulator in the form of cytokine molecule, as a nuclear factor to regulate these molecules and DNA structural determination. It has proximal homologous DNA binding domains Box-A, Box-B and distal C-terminal domain. Reduced form exists in
Tripathi A, Shrinet K, Kumar A.
europepmc   +4 more sources

The redox-sensitive protein HMGB1: intracellular and extracellular roles

open access: yesExperimental and Molecular Medicine
HMGB1 is a non-histone nuclear protein that is primarily located in the nucleus. It can be translocated to the cytoplasm and secreted into the extracellular space upon stimulation.
Man Sup Kwak   +3 more
doaj   +3 more sources

Insights into telomeric G-quadruplex DNA recognition by HMGB1 protein. [PDF]

open access: yesNucleic Acids Res, 2019
Abstract HMGB1 is a ubiquitous non-histone protein, which biological effects depend on its expression and subcellular location. Inside the nucleus, HMGB1 is engaged in many DNA events such as DNA repair, transcription and telomere maintenance.
Amato J   +13 more
europepmc   +5 more sources

Redox properties of the A‐domain of the HMGB1 protein [PDF]

open access: yesFEBS Letters, 2008
MINT‐6795963: txn (uniprotkb:P10599) and HMGB1 (uniprotkb:P09429) bind
Sahu, Debashish   +3 more
openaire   +2 more sources

C-terminal domain of nonhistone protein HMGB1 as a modulator of HMGB1–DNA structural interactions [PDF]

open access: yesSpectroscopy, 2010
The HMGB1 protein (High Mobility Group protein 1) participates in the formation of functionally significant DNA-protein complexes. HMGB1 protein contains two DNA-binding domains and negatively charged C-terminal region. The latter consists of continuous sequence of dicarboxylic amino acids residues.
Chikhirzhina, E.   +4 more
openaire   +1 more source

Post-Translational Modification of HMGB1 Disulfide Bonds in Stimulating and Inhibiting Inflammation

open access: yesCells, 2021
High mobility group box 1 protein (HMGB1), a highly conserved nuclear DNA-binding protein, is a “damage-associated molecular pattern” molecule (DAMP) implicated in both stimulating and inhibiting innate immunity.
Ulf Andersson   +2 more
doaj   +1 more source

Magnesium sulfate reduces vascular endothelial cell apoptosis in rats with preeclampsia via the miR-218-5p/HMGB1 pathway

open access: yesClinical and Experimental Hypertension, 2022
Objective This study aims to investigate the mechanism by which magnesium sulfate regulates the miR-218-5p/HMGB-pathway-mediated apoptosis of vascular endothelial cells (VECs) in rats with preeclampsia (PE).
Jiacui Zheng   +5 more
doaj   +1 more source

NMR studies of DNA recognition mechanism of HMGB1 protein [PDF]

open access: yesNucleic Acids Symposium Series, 2009
A 2'-deoxyuridylate dimer cyclized via cross-linkage by an ethylene (U(et)(p)U) or a propylene (U(pr)(p)U) linker at the 5-position was incorporated into DNA oligomers. Fluorescence resonance energy transfer (FRET) experiments showed that they bent at approximately 90 degrees .
Kyoko, Furuita   +5 more
openaire   +2 more sources

Mini‐review: The nuclear protein HMGB1 as a proinflammatory mediator [PDF]

open access: yesEuropean Journal of Immunology, 2004
AbstractThe intranuclear architectural protein that is termed high mobility group box chromosomal protein 1 (HMGB1) was recently identified as a potent proinflammatory mediator when present extracellularly. HMGB1 has been demonstrated to be a long‐searched‐for nuclear danger signal passively released by necrotic, as opposed to apoptotic, cells that ...
Helena, Erlandsson Harris   +1 more
openaire   +2 more sources

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