Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA. - Wikidata - awgldk - TriplyDB

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

http://www.wikidata.org/entity/Q34744542

about

High Mobility Group B Proteins, Their Partners, and Other Redox Sensors in Ovarian and Prostate Cancer Oxidative stress-mediated HMGB1 biology The Next Generation of Platinum Drugs: Targeted Pt(II) Agents, Nanoparticle Delivery, and Pt(IV) Prodrugs Yeast HMO1: Linker Histone Reinvented The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract.HMGB1 in health and disease.Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1 Diepoxybutane interstrand cross-links induce DNA bending.Paraformaldehyde Fixation May Lead to Misinterpretation of the Subcellular Localization of Plant High Mobility Group Box Proteins Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein.Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1)Binding interaction of HMGB4 with cisplatin-modified DNA.Life after death: targeting high mobility group box 1 in emergent cancer therapies.Cisplatin protects against acute liver failure by inhibiting nuclear HMGB1 release Monofunctional and higher-valent platinum anticancer agents.The high mobility group box: the ultimate utility player of a cell.The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors.Reactive oxygen homeostasis - the balance for preventing autoimmunity.Repair shielding of platinum-DNA lesions in testicular germ cell tumors by high-mobility group box protein 4 imparts cisplatin hypersensitivity A novel expression system for production of soluble prion proteins in E. coli.Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release.Expression of cFLIPL Determines the Basal Interaction of Bcl-2 With Beclin-1 and Regulates p53 Dependent Ubiquitination of Beclin-1 During Autophagic Stress.The impact of pharmacokinetic gene profiles across human cancers.Oxidation Prevents HMGB1 Inhibition on PDGF-Induced Differentiation of Multipotent Vascular Stem Cells to Smooth Muscle Cells: A Possible Mechanism Linking Oxidative Stress to Atherosclerosis.

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P2860

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

http://www.wikidata.org/entity/Q34744542

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@ast

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@en

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@nl

type

label

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@ast

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@en

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@nl

prefLabel

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@ast

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@en

Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

@nl

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Redox state-dependent interaction of HMGB1 and cisplatin-modified DNA.

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Semi Park

http://www.w3.org/2001/XMLSchema#string

Stephen J Lippard

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P2860

HMG1 and 2: architectural DNA-binding proteins

The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases

Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins

Identification of the cysteine residue exposed by the conformational change in pig heart succinyl-CoA:3-ketoacid coenzyme A transferase on binding coenzyme A

Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human ABO(H) Blood Group B Glycosyltransferase without Affecting Activity: Structural Insights into Cooperative Substrate Binding

Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy

Release of chromatin protein HMGB1 by necrotic cells triggers inflammation

HMG1 and 2, and related 'architectural' DNA-binding proteins

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

Cisplatin: mode of cytotoxic action and molecular basis of resistance

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2567-2574

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scholarly article

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10.1021/BI2000214

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13

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50

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