Back to search

Molten globule intermediates and protein folding

Data up to Jan 2025

Published1991
Citations281
References47

Total Citations Per Year

Abstract

References (47)

Dominant forces in protein folding

1990 • 3,682 citations

Are there pathways for protein folding?

1968 • 1,496 citations

The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

1989 • 1,446 citations

INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS

1990 • 1,133 citations

Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding

1982 • 1,041 citations

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR

1988 • 823 citations

‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains

1983 • 723 citations

Evidence for a molten globule state as a general intermediate in protein folding

1990 • 677 citations

α‐lactalbumin: compact state with fluctuating tertiary structure?

1981 • 611 citations

NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

1988 • 583 citations

Mechanism of acid-induced folding of proteins

1990 • 560 citations

Acid-induced folding of proteins.

1990 • 555 citations

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

1989 • 473 citations

Transient folding intermediates characterized by protein engineering

1990 • 446 citations

Conformational states in .beta.-lactamase: molten-globule states at acidic and alkaline pH with high salt

1989 • 404 citations

Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR

1990 • 306 citations

Comparison of the transient folding intermediates in lysozyme and .alpha.-lactalbumin

1985 • 281 citations

Compact state of a protein molecule with pronounced small-scale mobility: bovine ?-lactalbumin

1985 • 257 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

Demonstration by NMR of folding domains in lysozyme

1991 • 246 citations

Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism

1987 • 244 citations

Detection and characterization of a folding intermediate in barnase by NMR

1990 • 212 citations

Sequential mechanism of refolding of carbonic anhydrase B

1987 • 199 citations

‘Molten‐globule“ state accumulates in carbonic anhydrase folding

1984 • 174 citations

A folding model of α-lactalbumin deduced from the three-state denaturation mechanism

1977 • 173 citations

Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution

1989 • 157 citations

Analysis of the code relating sequence to conformation in proteins: Possible implications for the mechanism of formation of helical regions

1971 • 154 citations

Kinetics of unfolding and refolding of proteins

1973 • 145 citations

An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’

1990 • 109 citations

The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation

1976 • 108 citations

Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme

1981 • 87 citations

Kinetics of the helix—coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements

1979 • 77 citations

Effects of sulphate and urea on the stability and reversible unfolding of β-lactamase from Staphylococcus aureus

1985 • 76 citations

Physical nature of the phase transition in globular proteins

1986 • 71 citations

Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and ‘molten globule’ states

1986 • 71 citations

Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinase

1978 • 62 citations

Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresis

1980 • 61 citations

A hydrophobic cluster forms early in the folding of dihydrofolate reductase

1989 • 56 citations

Conformation, stability, and folding of interleukin 1.beta.

1987 • 56 citations

An early intermediate of refolding α‐lactalbumin forms within 20 ms

1987 • 54 citations

Kinetic characterization of early immunoreactive intermediates during the refolding of guanidine-unfolded Escherichia coli tryptophan synthase .beta.2 subunits

1990 • 46 citations

Intermediates on the folding pathway of octopine dehydrogenase from Pecten jacobaeus

1987 • 45 citations

Comparison of intramolecular packing of a protein in native and ‘molten globule’ states

1986 • 43 citations

Kinetics of appearance of an early immunoreactive species during the refolding of acid-denatured Escherichia coli tryptophan synthase .beta.2 subunit

1988 • 29 citations

Is thermally denatured protein unfolded? The example of α-lactalbumin

1987 • 26 citations

[Self-organization of the myoglobin molecule].

1973 • 26 citations

Identification by n.m.r. spectroscopy of a stable intermediate structure in the unfolding of staphylococcal β-lactamase

1983 • 10 citations

Cited By (0)

No citing papers found in database

Molten globule intermediates and protein folding (1991) – European Biophysics Journal | Metascience Observatory Explorer