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

Redox-dependent regulation of end-binding protein 1 activity by glutathionylation.

Science China. Life sciences - 1 Apr 2021

Chen Miao, Wang Jian, Yang Yang, Zhong Tao, Zhou Peng, Ma Huixian, Li Jingrui, Li Dengwen, Zhou Jun, Xie Songbo, Liu Min

Abstract excerpt

Cytoskeletal proteins are susceptible to glutathionylation under oxidizing conditions, and oxidative damage has been implicated in several neurodegenerative diseases. End-binding protein 1 (EB1) is a master regulator of microtubule plus-end tracking proteins (+TIPs) and is critically involved in the control of microtubule dynamics and cellular processes. However, the impact of glutathionylation on EB1 functions...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Glutaredoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione

Share to Microscopy, Confocal

Share to Microtubule-Associated Proteins

Share to Microtubules

Share to Oxidation-Reduction

Share to Time-Lapse Imaging

Source

Identifiers

PMID: 32737853
DOI: 10.1007/s11427-020-1765-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Redox-dependent regulation of end-binding protein 1 activity by glutathionylation.PMID 32737853Read ↗

Expression of recombinant human glutamylating TTLLs in human cells leads to differential tubulin glutamylation patterns, with only TTLL6 disrupting microtubule dynamicsSemantic proximity Read ↗

The ER Thioredoxin-Related Transmembrane Protein TMX2 Controls Redox-Mediated Tethering of ER-Mitochondria Contacts (ERMCS)Semantic proximity Read ↗

Characterization of a novel EB1 acetylation site important for the regulation of microtubule dynamics and cargo recruitment.Semantic proximity Read ↗

Mutation in G6PD gene leads to loss of cellular control of protein glutathionylation: mechanism and implication.Semantic proximity Read ↗

A TIRF microscopy assay to decode how tau regulates EB's tracking at microtubule ends.Semantic proximity Read ↗

Mitochondrial translocation of APE1 relies on the MIA pathway.Semantic proximity Read ↗

Regulation of DJ-1 by Glutaredoxin 1 in Vivo: Implications for Parkinson’s DiseaseSemantic proximity Read ↗

Histone deacetylase 6 inhibition promotes microtubule acetylation and facilitates autophagosome–lysosome fusion in dystrophin‐deficient mdx miceSemantic proximity Read ↗

Phosphorylation of EB1 regulates the recruitment of CLIP-170 and p150glued to the plus ends of astral microtubules.Semantic proximity Read ↗

Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis.Semantic proximity Read ↗

Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymerase.Semantic proximity Read ↗

S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid.Semantic proximity Read ↗

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