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-Reference-Cited by-同舟云学术

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

Published:2009-05 Issue:5 Volume:91 Page:373-383
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Rodziewicz-Motowidło Sylwia,Iwaszkiewicz Justyna,Sosnowska Renata,Czaplewska Paulina,Sobolewski Emil,Szymańska Aneta,Stachowiak Krystyna,Liwo Adam

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference57 articles.

1. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids.

2. Cystatin C-Properties and use as diagnostic marker

3. Structural studies of cysteine proteases and their inhibitors.

4. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C).

5. Molecular basis for amyloidosis related to hereditary brain hemorrhage

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