MODEL OF A SPECIFIC INTERACTION - SALT-BRIDGES FORM BETWEEN PROTHROMBIN AND ITS ACTIVATING ENZYME BLOOD-CLOTTING FACTOR-XA

被引：43

作者：

GREER, J

机构：

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1981年 / 153卷 / 04期

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D O I：

10.1016/0022-2836(81)90466-6

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：

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页码：1043 / 1053

页数：11

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共 28 条

[1] STRUCTURE OF CRYSTALLINE ALPHA-CHYMOTRYPSIN .5. ATOMIC STRUCTURE OF TOSYL-ALPHA-CHYMOTRYPSIN AT 2 A RESOLUTION
BIRKTOFT, JJ
BLOW, DM
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1972, 68 (02) : 187 - &
[2] MODE OF ACTION OF SOYBEAN TRYPSIN-INHIBITOR (KUNITZ) AS A MODEL FOR SPECIFIC PROTEIN-PROTEIN INTERACTIONS
BLOW, DM
JANIN, J
SWEET, RM
[J]. NATURE, 1974, 249 (5452) : 55 - 57
[3] INDUCTION OF BOVINE TRYPSINOGEN-TRYPSIN TRANSITION BY PEPTIDES SEQUENTIALLY SIMILAR TO N-TERMINUS OF TRYPSIN
BODE, W
HUBER, R
[J]. FEBS LETTERS, 1976, 68 (02) : 231 - 236
[4] TRANSITION OF BOVINE TRYPSINOGEN TO A TRYPSIN-LIKE STATE UPON STRONG LIGAND-BINDING .2. BINDING OF THE PANCREATIC TRYPSIN-INHIBITOR AND OF ISOLEUCINE-VALINE AND OF SEQUENTIALLY RELATED PEPTIDES TO TRYPSINOGEN AND TO P-GUANIDINOBENZOATE-TRYPSINOGEN
BODE, W
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1979, 127 (04) : 357 - 374
[5] A POSSIBLE 3-DIMENSIONAL STRUCTURE OF BOVINE ALPHA-LACTALBUMIN BASED ON THAT OF HENS EGG-WHITE LYSOZYME
BROWNE, WJ
NORTH, ACT
PHILLIPS, DC
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1969, 42 (01) : 65 - &
[6] DAVIE EW, 1975, PROTEASES BIOL CONTR, P65
[7] Dayhoff H., 1978, ALTAS PROTEIN SEQUEN, V5, P363
[8] COMPARATIVE MODEL-BUILDING OF THE MAMMALIAN SERINE PROTEASES
GREER, J
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1981, 153 (04) : 1027 - 1042
[9] MODEL FOR HAPTOGLOBIN HEAVY-CHAIN BASED UPON STRUCTURAL HOMOLOGY
GREER, J
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1980, 77 (06): : 3393 - 3397
[10] HOMOLOGIES IN SERINE PROTEINASES
HARTLEY, BS
[J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1970, 257 (813) : 77 - &