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FEBS Letters|March 12, 1990
Evidence for a molten globule state as a general intermediate in protein foldingO B Ptitsyn, R H Pain, G V Semisotnov, et al.Biofizika|March 10, 2001
[Y97V substitution in the horse cytochrome c causes accumulation of the equilibrium intermediate]R F Latypov, D A Dolgikh, M P Kirpichnikov, et al.Folding & Design|August 26, 1998
Release of retinol and denaturation of its plasma carrier, retinol-binding proteinV E Bychkova, A E Dujsekina, A Fantuzzi, et al.Biochemistry|August 25, 1992
Retinol-binding protein is in the molten globule state at low pHV E Bychkova, R Berni, G L Rossi, et al.Molekuliarnaia Biologiia|July 1, 1980
[Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures]I A Bolotina, V O Chekhov, V Iu Lugauskas, et al.Molekuliarnaia Biologiia|March 1, 1980
[Compact structure of random copolymers of hydrophobic and hydrophilic amino acid residues]V E Bychkova, G V Semisotnov, O B Ptitsyn, et al.Biofizika|November 1, 1982
[Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model]R I Gil'manshin, D A Dolgikh, O B Ptitsyn, et al.FEBS Letters|April 9, 1990
An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'M E Goldberg, G V Semisotnov, B Friguet, et al.Molekuliarnaia Biologiia|May 1, 1983
[Fluctuating state of the protein globule]O B Ptitsyn, D A Dolgikh, R I Gil'manshin, et al.FEBS Letters|November 16, 1987
Sequential mechanism of refolding of carbonic anhydrase BG V Semisotnov, N A Rodionova, V P Kutyshenko, et al.Pageof 7