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Protein Science : a Publication of the Protein Society|October 23, 1997
Structural heterogeneity of the various forms of apomyoglobin: implications for protein foldingR Gilmanshin, R B Dyer, R H CallenderNature Structural Biology|May 20, 1998
The core of apomyoglobin E-form folds at the diffusion limitR Gilmanshin, R H Callender, R B DyerBiochemistry|July 12, 1994
Annexin IV reduces the rate of lateral lipid diffusion and changes the fluid phase structure of the lipid bilayer when it binds to negatively charged membranes in the presence of calciumR Gilmanshin, C E Creutz, L K TammBiochemistry|April 25, 2001
Structures of apomyoglobin's various acid-destabilized formsR Gilmanshin, M Gulotta, R B Dyer, et al.Annual Review of Physical Chemistry|February 6, 1999
Fast events in protein folding: the time evolution of primary processesR H Callender, R B Dyer, R Gilmanshin, et al.Biochemistry|April 25, 2001
Core formation in apomyoglobin: probing the upper reaches of the folding energy landscapeM Gulotta, R Gilmanshin, T C Buscher, et al.Biochemistry|December 16, 1997
Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobinR Gilmanshin, S Williams, R H Callender, et al.Proceedings of the National Academy of Sciences of the United States of America|April 15, 1997
Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobinR Gilmanshin, S Williams, R H Callender, et al.Investigative Ophthalmology & Visual Science|March 21, 2024
Prevalence of Myopic Maculopathy Among the Very Old: The Ural Very Old StudyMukharram M Bikbov, Timur R Gilmanshin, Gyulli M Kazakbaeva, et al.Biochemistry|January 23, 1996
Fast events in protein folding: helix melting and formation in a small peptideS Williams, T P Causgrove, R Gilmanshin, et al.Pageof 5