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Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin

Author

Pierre De Meyts

1944 -

Published in: Nature

Date of publication: June 1, 1978

Language: English

Main subject: preproinsulin

Bibliographic databases:

Cites articles 24

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April 1, 1962

Studies on insulin. III. On the structure of the alanyl chain of bonito insulin
May 1, 1966

Species variation in the amino acid sequence of insulin
May 1, 1966

Relationship of structure to biological activity of insulin as revealed by degradative studies
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Preparation and characterization of diphenylthiocarbamyl-insulin and des-GlyA1-des-PheB1-insulin (bovine)
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The acetylation of insulin
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Insulin receptors in the liver: specific binding of ( 125 I)insulin to the plasma membrane and its relation to insulin bioactivity
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Physical and biological properties of guinea pig insulin
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Insulin interactions with its receptors: experimental evidence for negative cooperativity
February 1, 1974

Receptor-binding assay of chemically modified insulins. Comparison with in vitro and in vivo bioassays.
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Zinc binding, circular dichroism, and equilibrium sedimentation studies on insulin (bovine) and several of its derivatives
April 1, 1974

The biological activity and the binding affinity of modified insulins determined on isolated rat fat cells
February 1, 1974

Molecular basis of negative co-operativity in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
September 1, 1974

Structural and crystallographic observations on hagfish insulin
July 1, 1974

Low resolution crystal structure of hagfish insulin
July 1, 1975

The relation of conformation and association of insulin to receptor binding; x-ray and circular-dichroism studies on bovine and hystricomorph insulins

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Is the evolution of insulin Darwinian or due to selectively neutral mutation?

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Binding of insuling and other hormones to non-receptor materials: Saturability, specificity and apparent “negative cooperativity”,Binding of insulin and other hormones to non-receptor materials: saturability, specificity and apparent "negative cooperativity"
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Radioreceptor Assay of Insulin: Comparison of Plasma and Pancreatic Insulins and Proinsulins
February 1, 1976

Receptor-binding region of insulin

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Synthesis and properties of carbonylbis(methionyl)insulin, a proinsulin analog which is convertible to insulin by cyanogen bromide cleavage,Synthesis and properties of carbonylbis(methionyl)insulin, a proinsulin analogue which is convertible to insulin by cyanogen bromide cleavage
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Cooperative properties of hormone receptors in cell membranes
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Amino-terminal sequences of two polypeptides from human serum with nonsuppressible insulin-like and cell-growth-promoting activities: evidence for structural homology with insulin B chain

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