Results 151 to 160 of about 19,795 (176)

Uncontrolled hypertension contributes to vascular permeability after cardioplegic arrest and cardiopulmonary bypass. [PDF]

JTCVS Open
Kanuparthy M, Stone CR, Manthana R, Kaushik H, Muir KC, Hamze J, Ehsan A, Sodha N, Feng J, Sellke FW.   +9 more
europepmc   +1 more source

Turning the knobs: The impact of glutathionylation on starch metabolism. [PDF]

Plant Physiol
Moseler A.
europepmc   +1 more source

Endoplasmic Reticulum Redoxome: Protein Folding and Beyond. [PDF]

Biochemistry
Oliveira PVS, De Bessa TC, Laurindo FRM.
europepmc   +1 more source

A monoclonal antibody to platelet αIIbβ3 that inhibits protein disulfide isomerase binding and platelet aggregation. [PDF]

Blood Adv
Wang L, Wang J, Li J, Coller BS.
europepmc   +1 more source

Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase

FEBS Letters, 1995
Protein disulfide-isomerase (PDI) is the best known representative of a growing family of enzymes with thioredoxin domains. Two such proteins with thioredoxin (Trx) domains, CaBP1 and CaBP2 (ERp72), have previously been isolated from rat liver microsomes.
Hans-Dieter Soling, Arne Holmgren
exaly   +2 more sources

Thioredoxin and thioredoxin reductase: Current research with special reference to human disease

Biochemical and Biophysical Research Communications, 2010
Thioredoxin (Trx) and thioredoxin reductase (TrxR) plus NADPH, comprising the thioredoxin system, has a large number of functions in DNA synthesis, defense against oxidative stress and apoptosis or redox signaling with reference to many diseases.
Arne Holmgren, Jun Lu
exaly   +2 more sources

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER [PDF]

EMBO Journal, 2017
Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called non ...
Greg J Poet, Zhenbo Cao, Philip J Robinson   +2 more
exaly   +2 more sources

Reductive activation of ricin and ricin A-chain immunotoxins by protein disulfide isomerase and thioredoxin reductase

Biochemical Pharmacology, 2004
Intracellular activation of ricin and of the ricin A-chain (RTA) immunotoxins requires reduction of their intersubunit disulfide(s). This crucial event is likely to be catalyzed by disulfide oxidoreductases and precedes dislocation of the toxic subunit ...
Giuseppe Bellisola, Giulio Fracasso, Rodolfo Ippoliti   +2 more
exaly   +3 more sources