Spin-labeled sulfonyl fluorides as active-site probes of protease structure. Part 3. Active-site topography of human coagulant (.alpha.) and noncoagulant (.gamma.)thrombins
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00510a018
Reference23 articles.
1. Stability differences between high coagulant (alpha) and noncoagulant (gamma) human thrombins. Denaturation.
2. Binding of competitive inhibitors to the different pH-dependent forms of trypsin
3. Spin-labeled Sulfonyl Fluorides as Active Site Probes of Protease Structure
4. Physical evidence for an apolar binding site near the catalytic center of human α-thrombin
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1. Atomic structures of two nitroxide spin labels complexed with human thrombin: Comparison with solution studies;Journal of Protein Chemistry;2000
2. Unexpected crucial role of residue 225 in serine proteases;Proceedings of the National Academy of Sciences;1999-03-02
3. Comparison of the active-site conformations of bovine α-thrombin and meizothrombin(desF1) by electron spin resonance;Journal of Protein Chemistry;1996-02
4. Binding of Fluorescent and Spin-Labeled C-Terminal Hirudin Analogs to Thrombin;Journal of Medicinal Chemistry;1994-10
5. Biophysical Studies of Interactions of Hirudin Analogs with Bovine and Human Thrombin by ESR and Fluorescence Labelling Studies;Advances in Experimental Medicine and Biology;1993
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