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Structural Basis of Sequential and Concerted Cooperativity.
Not available
S-EPMC9687781
|
biostudies-literature
Cite
Residues W215, E217 and E192 control the allosteric E*-E equilibrium of thrombin.
Not available
S-EPMC6707225
|
biostudies-literature
Cite
Thrombin.
Not available
S-EPMC2491495
|
biostudies-literature
Cite
Serine proteases.
Not available
S-EPMC2675663
|
biostudies-literature
Cite
Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.
Not available
S-EPMC4566218
|
biostudies-literature
Cite
Role of the I16-D194 ionic interaction in the trypsin fold.
Not available
S-EPMC6889508
|
biostudies-literature
Cite
Mutant N143P reveals how Na+ activates thrombin.
Not available
S-EPMC2794733
|
biostudies-literature
Cite
The active site region plays a critical role in Na
+
binding to thrombin.
Not available
S-EPMC8695361
|
biostudies-literature
Cite
Role of sequence and position of the cleavage sites in prothrombin activation.
Not available
S-EPMC8348271
|
biostudies-literature
Cite
Codon switching of conserved Ser residues in coagulation and fibrinolytic proteases.
Not available
S-EPMC11343676
|
biostudies-literature
Cite
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