» Articles » PMID: 7788290

Thioredoxin--a Fold for All Reasons

Overview
Journal Structure
Publisher Cell Press
Date 1995 Mar 15
PMID 7788290
Citations 253
Authors
Affiliations
Soon will be listed here.
Abstract

The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common property of interacting with cysteine-containing substrates.

Citing Articles

Unveiling the versatility of the thioredoxin framework: Insights from the structural examination of DsbA1.

Penning S, Hong Y, Cunliffe T, Hor L, Totsika M, Paxman J Comput Struct Biotechnol J. 2024; 23:4324-4336.

PMID: 39697679 PMC: 11653150. DOI: 10.1016/j.csbj.2024.11.034.


The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.

Wayment-Steele H, Otten R, Pitsawong W, Ojoawo A, Glaser A, Calderone L Proc Natl Acad Sci U S A. 2024; 121(45):e2412293121.

PMID: 39475637 PMC: 11551320. DOI: 10.1073/pnas.2412293121.


Functional implication of the homotrimeric multidomain vacuolar sorting receptor 1 (VSR1) from Arabidopsis thaliana.

Park H, Youn B, Park D, Puthanveettil S, Kang C Sci Rep. 2024; 14(1):9622.

PMID: 38671060 PMC: 11052993. DOI: 10.1038/s41598-024-57975-2.


Solution structure and pressure response of thioredoxin-1 of Plasmodium falciparum.

Munte C, Kalbitzer H PLoS One. 2024; 19(4):e0301579.

PMID: 38635664 PMC: 11025842. DOI: 10.1371/journal.pone.0301579.


Distinct or Overlapping Areas of Mitochondrial Thioredoxin 2 May Be Used for Its Covalent and Strong Non-Covalent Interactions with Protein Ligands.

Ntallis C, Tzoupis H, Tselios T, Chasapis C, Vlamis-Gardikas A Antioxidants (Basel). 2024; 13(1).

PMID: 38275635 PMC: 10812433. DOI: 10.3390/antiox13010015.