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Calcium regulates folding and disulfide-bond formation in α-lactalbumin

Data up to Jan 2025

Published1989
Citations56
References15

Total Citations Per Year

Abstract

References (15)

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin

1989 • 473 citations

Mechanism of milk secretion

1971 • 401 citations

Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme

1970 • 394 citations

α-Lactalbumin: A calcium metalloprotein

1980 • 288 citations

Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozyme

1986 • 254 citations

Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase

1984 • 216 citations

α-Lactalbumin possesses a novel calcium binding loop

1986 • 216 citations

Some Kinetic Properties of Human-Milk Galactosyl Transferase

1974 • 186 citations

Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin.

1981 • 146 citations

Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.

1984 • 95 citations

Secretion of α-Lactalbumin into Milk and its Relevance to the Organization and Control of Lactose Synthetase

1969 • 95 citations

Physiological roles of zinc and calcium binding to .alpha.-lactalbumin in lactose biosynthesis

1985 • 57 citations

Refolding of reduced, denatured trypsinogen and trypsin immobilized on Agarose beads.

1975 • 49 citations

Role of the environment in the refolding of reduced pancreatic trypsin inhibitor

1980 • 46 citations

Crystallographic analysis of the three-dimensional structure of baboon α-lactalbumin at low resolution. Homology with lysozyme

1987 • 35 citations

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Calcium regulates folding and disulfide-bond formation in α-lactalbumin (1989) – Biochemical and Biophysical Research Communications | Metascience Observatory Explorer