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Craig M. Jackson
Craig M. Jackson
Retired, former Professor, Washington University, St.Louis
Brak zweryfikowanego adresu e-mail
Tytuł
Cytowane przez
Cytowane przez
Rok
Blood coagulation
CM Jackson, Y Nemerson
Annual review of biochemistry 49 (1), 765-811, 1980
9721980
Properties of the factor Xa binding site on human platelets.
JP Miletich, CM Jackson, PW Majerus
Journal of Biological Chemistry 253 (19), 6908-6916, 1978
5711978
Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III: implications for heparin efficacy.
PJ Hogg, CM Jackson
Proceedings of the National Academy of Sciences 86 (10), 3619-3623, 1989
4821989
Prothrombin structure, activation, and biosynthesis
JW Suttie, CM Jackson
Physiological Reviews 57 (1), 1-70, 1977
4781977
The conversion of prothrombin to thrombin: I. Characterization of the reaction products formed during the activation of bovine prothrombin
WG Owen, CT Esmon, CM Jackson
Journal of Biological Chemistry 249 (2), 594-605, 1974
4341974
[28] Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates
R Lottenberg, U Christensen, CM Jackson, PL Coleman
Methods in enzymology 80, 341-361, 1981
4171981
Interaction of coagulation factor Xa with human platelets.
JP Miletich, CM Jackson, PW Majerus
Proceedings of the National Academy of Sciences 74 (9), 4033-4036, 1977
2611977
The functional significance of vitamin K action. Difference in phospholipid binding between normal and abnormal prothrombin
CT Esmon, JW Suttie, CM Jackson
Journal of Biological Chemistry 250 (11), 4095-4099, 1975
2371975
Studies on the Structure of Glyceryl Ethers and the Glyceryl Ether Phospholipids of Bovine Erythrocytes*
DJ Hanahan, J Ekholm, CM Jackson
Biochemistry 2 (4), 630-641, 1963
2181963
A polypeptide region of bovine prothrombin specific for binding to phospholipids
SN Gitel, WG Owen, CT Esmon, CM Jackson
Proceedings of the National Academy of Sciences 70 (5), 1344-1348, 1973
2031973
Factor Va-dependent binding of factor Xa to human platelets.
WH Kane, MJ Lindhout, CM Jackson, PW Majerus
Journal of Biological Chemistry 255 (3), 1170-1174, 1980
1921980
The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin.
I Björk, CM Jackson, H Jörnvall, KK Lavine, K Nordling, WJ Salsgiver
Journal of Biological Chemistry 257 (5), 2406-2411, 1982
1851982
The conversion of prothrombin to thrombin: IV. The function of the fragment 2 region during activation in the presence of factor V
CT Esmon, CM Jackson
Journal of Biological Chemistry 249 (24), 7791-7797, 1974
1721974
A plausible mechanism for prothrombin activation by factor Xa, factor Va, phospholipid, and calcium ions
CT Esmon, WG Owen, CM Jackson
Journal of Biological Chemistry 249 (24), 8045-8047, 1974
1711974
The action of thrombin on peptide p-Nitroanilide substrates: Substrate selectivity and examination of hydrolysis under different reaction condtions
R Lottenberg, JA Hall, M Blinder, EP Binder, CM Jackson
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 1983
1691983
Solution composition dependent variation in extinction coefficients for p-nitroaniline
R Lottenberg, CM Jackson
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 1983
1681983
Bovine Factor XI Large-scale purification of the bovine plasma protein possessing Factor X activity
CM Jackson, TF Johnson, DJ Hanahan
Biochemistry 7 (12), 4492-4505, 1968
1511968
Interpretation of the temperature dependence of equilibrium and rate constants
DJ Winzor, CM Jackson
Journal of Molecular Recognition: An Interdisciplinary Journal 19 (5), 389-407, 2006
1452006
Relationship between factor V and activated factor X in the generation of prothrombinase
PG Barton, CM Jackson, DJ Hanahan
Nature 214 (5091), 923-924, 1967
1381967
The association of bovine prothrombin fragment 1 with phospholipid. Quantitative characterization of the Ca2+ ion-mediated binding of prothrombin fragment 1 to phospholipid …
FA Dombrose, SN Gitel, K Zawalich, CM Jackson
The Journal of biological chemistry 254 (12), 5027-5040, 1979
1331979
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