about
sameAs
Crystal structure of a complement factor D mutant expressing enhanced catalytic activityA general model of the P2 protein of peripheral nervous system myelin based on secondary structure predictions, tertiary folding principles, and experimental observations.VASP: a volumetric analysis of surface properties yields insights into protein-ligand binding specificity.Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin.Overlapping Specificity of Duplicated Human Pancreatic Elastase 3 Isoforms and Archetypal Porcine Elastase 1 Provides Clues to Evolution of Digestive Enzymes.Could domain movements be involved in the mechanism of trypsin-like serine proteases?Getting intimate with trypsin, the leading protease in proteomics.Proposed knobs-into-holes packing for several membrane proteins.The active centers of serine proteinases.Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding?Comparison of the predicted model of alpha-lytic protease with the x-ray structure.Complete localization of the disulfide bridges and glycosylation sites in boar sperm acrosin.The alpha-helix dipole and the properties of proteins.Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen.Molecular cloning and expression of serum calcium-decreasing factor (caldecrin).The amino acid sequence and predicted structure of Streptomyces griseus protease A.
P2860
Q27729743-B82E93A7-7250-449F-B960-B896F8A6F9DEQ30196332-5F89CA99-EDF1-407D-AB9F-6D24A3ABD627Q33683387-CF74395E-B6A9-44E7-B46E-D4AE4F82F4C8Q34170771-0389D7A8-3487-48D0-B517-0958E359150EQ36243521-0697C638-D2A3-4D97-A3F0-C371DD80B130Q37977942-17038796-2990-4815-86E5-9D57E549B17BQ38115212-4201A018-55CE-4ADE-AF64-446C1B24C79CQ39311645-F96EA686-F4B3-44AE-9113-70F8C5F4A663Q39940544-E7B31085-5E20-46DE-A30C-326AD534D416Q40304071-EA82BD78-E26A-4DD2-AD79-C18C3D5CC6E8Q41582482-7E6F767E-DC80-4DCC-B3A3-75A6131C75C4Q44499423-59B4C47A-4470-486C-A092-5F073B4A82FDQ45281613-675ADC0F-AD10-4F45-859C-976C1F76E91AQ45975726-E9E5BDB3-4524-4D26-8E94-55B6B37FD739Q48068365-17C03EA3-ADDF-4A17-9D68-C56A02F16B57Q53901091-2818268D-D0C4-408D-9B93-2743691ED765
P2860
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в лютому 1970
@uk
name
Three-dimensional Structure of Tosyl-elastase
@en
Three-dimensional Structure of Tosyl-elastase
@nl
type
label
Three-dimensional Structure of Tosyl-elastase
@en
Three-dimensional Structure of Tosyl-elastase
@nl
prefLabel
Three-dimensional Structure of Tosyl-elastase
@en
Three-dimensional Structure of Tosyl-elastase
@nl
P2860
P356
P1433
P1476
Three-dimensional structure of tosyl-elastase
@en
P2093
H C Watson
P2860
P2888
P304
P356
10.1038/225811A0
P407
P577
1970-02-01T00:00:00Z