Reference health
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
34/34 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
6 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 34 checked references that resolve
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[70] Determination of glutathione and glutathione disulfide in biological samples
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Regulation of rat liver microsomal glutathione S-transferase activity by thiol/disulfide exchange
resolves10.1002/jcp.1041040211
Formation of sulfhydryl groups in the culture medium by human diploid fibroblasts
resolves10.1016/S0021-9258(20)82001-8
Evidence for an alpha-mannosidase in endoplasmic reticulum of rat liver.
resolves10.1038/335649a0
Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
resolves10.1016/0076-6879(87)43016-4
Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography
resolves10.1042/bj2750341
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase
resolves10.1111/j.1432-1033.1968.tb00470.x
Thioredoxin. 6. The Amino Acid Sequence of the Protein from <i>Escherichia coli</i> B
resolves10.1016/0304-4165(77)90152-0
Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
resolves10.1016/0003-9861(87)90344-4
Sulfhydryl oxidase-catalyzed formation of disulfide bonds in reduced ribonuclease
resolves10.1042/bj2170145
Dog pancreatic microsomal-membrane polypeptides analysed by two-dimensional gel electrophoresis
resolves10.1111/j.1432-1033.1985.tb09283.x
Studies on the formation of intrachain disulphide bonds in newly biosynthesised bovine prolactin
resolves10.1016/S0021-9258(18)45552-4
Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation.
resolves10.1038/227680a0
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
resolves10.1042/bj2130235
Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction
resolves10.1021/bi00217a004
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer
resolves10.1016/S0021-9258(20)79774-7
An in Vitro System for Studying the Kinetics of Interchain Disulfide Bond Formation in Immunoglobulin G
resolves10.1021/bi00827a028
Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
resolves10.1016/S0021-9258(18)33711-6
Conformational changes associated with proteolytic processing of presecretory proteins allow glutathione-catalyzed formation of native disulfide bonds.
resolves10.1016/S0021-9258(18)33088-6
Proteolytic processing of presecretory proteins is required for development of biological activities in pancreatic exocrine proteins.
resolves10.1016/S0076-6879(83)96011-1
[7] Methods for the study of protein translocation across the RER membrane using the reticulocyte lysate translation system and canine pancreatic microsomal membranes
resolves10.1042/bj2660625
<i>γ</i>-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase
resolves10.1016/S0076-6879(83)96010-X
[6] Preparation of microsomal membranes for cotranslational protein translocation
resolves10.1016/0092-8674(87)90224-8
The rate of bulk flow from the endoplasmic reticulum to the cell surface
resolves10.1016/S0021-9258(17)44311-0
Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides.
resolves10.1093/protein/1.2.141
The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential
resolves10.1083/jcb.113.5.997
Nonlysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor subunits: a TLCK- and TPCK-sensitive cleavage within the ER.
resolves10.1146/annurev.bi.54.070185.001513
ROLE OF REVERSIBLE OXIDATION-REDUCTION OF ENZYME THIOLS-DISULFIDES IN METABOLIC REGULATION
resolves10.1016/0968-0004(77)90042-1
Protein disulfide bond synthesis: a possible intracellular mechanism
The 6 references without a DOI — listed, not checked
no DOI — not checkedCotgreave, I. A., Sulfur- Containing Drugs and Related Organic Compounds. Chemistry, Biochemistry, and Toxicology. Analytical, Biochemical, and Toxicological Aspects of Sulphur Xenobiochemistry 2: 101 (1989).
no DOI — not checkedDolphin D. Gtutathione: Chemical Biochemical and Medical Aspects (1989).
no DOI — not checkedGILBERT, H.F., MOLECULAR AND CELLULAR ASPECTS OF THIOL DISULFIDE EXCHANGE, ADVANCES IN ENZYMOLOGY AND RELATED AREAS OF MOLECULAR BIOLOGY 63: 69 (1990).
no DOI — not checkedHWANG C unpublished data.
no DOI — not checkedMARTENSSON, J, HIGH-AFFINITY TRANSPORT OF GLUTATHIONE IS PART OF A MULTICOMPONENT SYSTEM ESSENTIAL FOR MITOCHONDRIAL-FUNCTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 87: 7185 (1990).
no DOI — not checkedTorchinskii Y. M. Sulphur in Proteins (1981).
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