ON THE RATIONAL DESIGN OF RENIN INHIBITORS - X-RAY STUDIES OF ASPARTIC PROTEINASES COMPLEXED WITH TRANSITION-STATE ANALOGS

被引：112

作者：

BLUNDELL, TL ^{[1
]}

COOPER, J ^{[1
]}

FOUNDLING, SI ^{[1
]}

JONES, DM ^{[1
]}

ATRASH, B ^{[1
]}

SZELKE, M ^{[1
]}

机构：

[1] ROYAL POSTGRAD MED SCH,DEPT CHEM PATHOL,LONDON W12 0HS,ENGLAND

来源：

BIOCHEMISTRY | 1987年 / 26卷 / 18期

关键词：

D O I：

10.1021/bi00392a001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：5585 / 5590

页数：6

共 52 条

[21] HARTSUCK JA, 1972, J BIOL CHEM, V247, P2575
[22] ENERGY CALCULATIONS ON ASPARTIC PROTEINASES - HUMAN RENIN, ENDOTHIAPEPSIN AND ITS COMPLEX WITH AN ANGIOTENSINOGEN FRAGMENT ANALOG, H-142
HEMMINGS, AM
FOUNDLING, SI
SIBANDA, BL
WOOD, SP
PEARL, LH
BLUNDELL, T
[J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 1985, 13 (06) : 1036 - 1041
[23] INHIBITION OF RENIN - RECENT IMMUNOLOGICAL AND PHARMACOLOGICAL ADVANCES
HOFBAUER, KG
WOOD, JM
[J]. TRENDS IN PHARMACOLOGICAL SCIENCES, 1985, 6 (04) : 173 - 177
[24] CRYOENZYMOLOGY OF PENICILLOPEPSIN - APPENDIX - MECHANISM OF ACTION OF ASPARTYL PROTEINASES
HOFMANN, T
DUNN, BM
FINK, AL
[J]. BIOCHEMISTRY, 1984, 23 (22) : 5247 - 5256
[25] MOLECULAR-STRUCTURE OF AN ASPARTIC PROTEINASE ZYMOGEN, PORCINE PEPSINOGEN, AT 1.8 A RESOLUTION
JAMES, MNG
SIELECKI, AR
[J]. NATURE, 1986, 319 (6048) : 33 - 38
[26] CONFORMATIONAL FLEXIBILITY IN THE ACTIVE-SITES OF ASPARTYL PROTEINASES REVEALED BY A PEPSTATIN FRAGMENT BINDING TO PENICILLOPEPSIN
JAMES, MNG
SIELECKI, A
SALITURO, F
RICH, DH
HOFMANN, T
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1982, 79 (20): : 6137 - 6141
[27] STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8-A RESOLUTION
JAMES, MNG
SIELECKI, AR
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1983, 163 (02) : 299 - 361
[28] STEREOCHEMICAL ANALYSIS OF PEPTIDE-BOND HYDROLYSIS CATALYZED BY THE ASPARTIC PROTEINASE PENICILLOPEPSIN
JAMES, MNG
SIELECKI, AR
[J]. BIOCHEMISTRY, 1985, 24 (14) : 3701 - 3713
[29] JONES M, 1985, 9TH P AM PEPT S, P759
[30] KOKUBU T, 1973, BIOCHEM PHARMACOL, V22, P3217

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