Associated Papers
NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution.
Maszota-Zieleniak M et al.
The Febs Journal, 2020
Structural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic protein.
Orlikowska M et al.
Acta Crystallographica. Section D, Biological Crystallography, 2013
Influence of point mutations on the stability, dimerization, and oligomerization of human cystatin C and its L68Q variant.
Szymańska A et al.
Frontiers in Molecular Neuroscience, 2012
Crystallization and preliminary X-ray diffraction analysis of Val57 mutants of the amyloidogenic protein human cystatin C.
Orlikowska M et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 2011
The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants.
Rodziewicz-Motowidło S et al.
Biopolymers, 2009
Governing the monomer-dimer ratio of human cystatin c by single amino acid substitution in the hinge region.
Szymańska A et al.
Acta Biochimica Polonica, 2009
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