Structure of the complex formed between the bacterial-produced inhibitor chymostatin and the serine enzyme Streptomyces griseus protease A
- 1 May 1980
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 139 (1) , 45-51
- https://doi.org/10.1016/0022-2836(80)90114-x
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Molecular structure of crystalline Streptomyces griseus protease A at 2.8 å resolutionJournal of Molecular Biology, 1978
- Molecular structure of crystalline Streptomyces griseus protease A at 2.8 Å resolutionJournal of Molecular Biology, 1978
- The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatinBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- The active centers of Streptomyces griseus protease 3 and α-chymotrypsin: enzyme-substrate interactions remote from the scissile bondBiochemistry, 1976
- The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: enzyme-substrate interactions close to the scissile bondBiochemistry, 1976
- AT LEAST THREE HUMAN NEUTROPHIL LYSOSOMAL PROTEASES ARE CAPABLE OF DEGRADING JOINT CONNECTIVE TISSUES*Annals of the New York Academy of Sciences, 1975
- Studies of the Heterogeneity of Streptomyces griseus Protease. Isolation and Characterization of an Alkaline Serine Protease from Commercial Pronase-P Derived from Streptomyces griseus Kl.Acta Chemica Scandinavica, 1973
- Neutrophil Proteases in InflammationAnnual Review of Medicine, 1972
- The difference Fourier technique in protein crystallography: errors and their treatmentActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1971
- A mathematical model-building procedure for proteinsActa Crystallographica, 1966