Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Requirements for the different cysteines in the chemotactic and desensitizing activity of human thioredoxin.

Antioxidants & redox signaling - 1 Jan 2000

Bizzarri Cinzia, Holmgren Arne, Pekkari Klas, Chang Geng, Colotta Francesco, Ghezzi Pietro, Bertini Riccardo

Abstract excerpt

Thioredoxin (Trx) is a protein disulfide oxidoreductase that can be secreted and act as a chemoattractant for leukocytes. Like chemokines, it causes desensitization of monocytes against its chemotactic activity and that of monocyte chemoattractant protein-1 (MCP-1). To investigate the role of the redox properties of Trx, and particularly of some of its five cysteines, in its chemotactic and desensitizing action,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chemokine CCL2
Share to Chemokines

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chemotaxis

Share to Cysteine

Share to Leukocytes, Mononuclear

Share to Monocytes

Share to Neutrophils

Share to Thioredoxins

Source

Identifiers

PMID: 16115022
DOI: 10.1089/ars.2005.7.1189

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Requirements for the different cysteines in the chemotactic and desensitizing activity of human thioredoxin.PMID 16115022Read ↗

Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69.Semantic proximity Read ↗

Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release.Semantic proximity Read ↗

Guanylyl cyclase sensitivity to nitric oxide is protected by a thiol oxidation-driven interaction with thioredoxin-1.Semantic proximity Read ↗

c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation.Semantic proximity Read ↗

Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif.Semantic proximity Read ↗

Cysteine-3 and cysteine-4 are essential for the thioredoxin-like oxidoreductase and antioxidant activities of Plasmodium falciparum macrophage migration inhibitory factor.Semantic proximity Read ↗

Oxidation regulates the inflammatory properties of the murine S100 protein S100A8.Semantic proximity Read ↗

Interleukin 8 dimerization as a mechanism for regulation of neutrophil adherence-dependent oxidant production.Semantic proximity Read ↗

Demonstration of the interaction of thioredoxin with p40phox, a phagocyte oxidase component, using a yeast two-hybrid system.Semantic proximity Read ↗

Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding.Semantic proximity Read ↗

Redox regulation of RhoA.Semantic proximity Read ↗

Redox control of caspase-3 activity by thioredoxin and other reduced proteins.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.