Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin.
about
Biological functions of low-frequency vibrations (phonons). III. Helical structures and microenvironment.The active site of aspartic proteinasesA general model of the P2 protein of peripheral nervous system myelin based on secondary structure predictions, tertiary folding principles, and experimental observations.Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virusAmino acid sequence of porcine spleen cathepsin DAmino acid sequence of mouse submaxillary gland renin.Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized in two homologous clusters of four exonsThe Chou-Fasman secondary structure prediction method with an extended data base.Ty3, a yeast retrotransposon associated with tRNA genes, has homology to animal retroviruses.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesAnionic lipid headgroups as a proton-conducting pathway along the surface of membranes: a hypothesis.Correlations between three-dimensional structure and function of immunoglobulins.Comparative biochemistry of the proteinases of eucaryotic microorganisms.The first step in the activation of chicken pepsinogen is similar to that of prochymosinMechanism of pepsin catalysis: general base catalysis by the active-site carboxylate ion.alpha-Bromo-4-amino-3-nitroacetophenone, a new reagent for protein modification. Modification of the methionine-290 residue of porcine pepsinStructure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents.Inactivation of aspartyl proteinases by butane-2,3-dione. Modification of tryptophan and tyrosine residues and evidence against reaction of arginine residues.cDNA cloning of an aspartic proteinase secreted by Candida albicans.Roles of electrostatic interaction in proteins.Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin
P2860
Q24548202-E7378CD8-469F-4D76-B570-98EA34756420Q27729140-92568A5E-CF68-4E49-AFD8-B6E62C0D43C6Q30196332-1FEFF79E-F9BB-4C73-A036-DDAEB4E85CE5Q30878497-C1F95DA4-1B43-4E39-9790-3B102122A2F1Q33931299-2F6B2F2D-D6D1-469B-A6D4-002FB0C150ACQ36262613-D3087515-99B8-46C3-945A-85A4A7213CE1Q36307435-B9617EE3-B726-422F-BE2F-B333DA38F93DQ36315424-5C5DB796-54D7-4731-95F1-BA94462FA6B5Q36601488-F7DCC4A0-1994-47CB-9049-28FF41A6F363Q36641451-8871162D-F7C6-48CB-8CE4-9872AA395D08Q36850242-88C6C6F3-DF1D-452F-8E76-87D8B0BA0079Q37059742-0D84437A-3BFE-41A6-B531-C330FFC5FA49Q37600596-1CD1D01F-D7AF-4C63-B848-E706662E30CCQ39617902-34560799-2485-4498-8C2C-0FE2C339F7B1Q40266220-C403028E-4159-436C-BE42-7B624652E009Q40855754-D96D5D7D-E377-47CB-ACC6-882D22F29C3CQ40877840-3D56D420-00A9-48DC-9146-01A352D402C3Q41976955-61B9289E-ED95-4518-AF4E-B141F3D56E38Q42845253-60EEC9F9-3EFF-4749-B363-BA822097F383Q42882616-DEDD2867-BF97-41A9-8F45-4E582BFD0D7EQ43580856-7BC06A48-E25B-4D3F-B9E3-E12E488CDBBBQ51649868-B185E6AA-C26D-452D-820F-25E39E5F35F9Q59074664-78B0A070-FCB2-452F-9EB8-4B054AD4F96B
P2860
Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin.
description
1977 nî lūn-bûn
@nan
1977 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի մարտին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年学术文章
@wuu
1977年学术文章
@zh-cn
1977年学术文章
@zh-hans
1977年学术文章
@zh-my
1977年学术文章
@zh-sg
1977年學術文章
@yue
name
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@ast
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@en
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@nl
type
label
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@ast
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@en
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@nl
prefLabel
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@ast
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@en
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@nl
P2093
P2860
P356
P1433
P1476
Penicillopepsin from Penicilli ...... homology with porcine pepsin.
@en
P2093
P2860
P2888
P304
P356
10.1038/266140A0
P407
P577
1977-03-01T00:00:00Z
P6179
1044663807