DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS. - Wikidata - wikimedia - TriplyDB

DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

http://www.wikidata.org/entity/Q36015937

about

The biosynthesis of insulin and a probable precursor of insulin by a human islet cell adenoma Functional differences in yeast protein disulfide isomerases.Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity Dual function of the propeptide of prouroguanylin in the folding of the mature peptide: disulfide-coupled folding and dimerization.Avian riboflavinuria IX. Qualitative action of a mutant gene in chicken on riboflavin-binding protein synthesis.Adventures with insulin in the islets of Langerhans Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum The spontaneous reoxidation of reduced beef and rat proinsulins.Multiple chemical forms of hepatitis B surface antigen produced in yeast.Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase.How many distinct enzymes are responsible for the several cellular processes involving thiol:protein-disulphide interchange?Properties of proinsulin and related polypeptides.C-peptide measurement: methods and clinical utility.Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies.Protein folding/refolding analysis by mass spectrometry. Scrambling of disulphide bridges in insulin Biosynthesis of an insulin precursor by islet tissue of cod (Gadus callarias).The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum.Collision induced dissociation products of disulfide-bonded peptides: ions result from the cleavage of more than one bond.The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase.Catalytically competent human and bovine zeta-thrombin and chimeras generated from unfolded polypeptide chains.The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase Approaching the thermodynamic view of protein folding through the reproduction of Anfinsen's experiment by undergraduate physical biochemistry students.The identity of the insulin degrading thiol-protein disulfide oxidoreductase (glutathione-insulin transhydrogenase) with the sulfhydryl-disulfide interchange enzyme.The effects of ribosomes on the activity of a membrane bound enzyme catalysing thiol-disulphide interchange.

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DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

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1965 nî lūn-bûn

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1965年の論文

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1965年学术文章

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1965年学术文章

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1965年学术文章

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1965年学术文章

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1965年学术文章

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1965年學術文章

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1965年學術文章

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1965年學術文章

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DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

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DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

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DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

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Proceedings of the National Academy of Sciences of the United States of America

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DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

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ANFINSEN CB

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DELORENZO F

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P2860

Protein measurement with the Folin phenol reagent

Tissue sulfhydryl groups

Studies on the reduction and re-formation of protein disulfide bonds

Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease

Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease

Insulin-I131 metabolism in human subjects: demonstration of insulin binding globulin in the circulation of insulin treated subjects

Disulphide interchange reactions.

Reconstitution of tobacco mosaic virus. III. Improved methods and the use of mixed nucleic acids.

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protein structure

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