| Year |
Citation |
Score |
| 2023 |
Jin DY, Chen X, Liu Y, Williams CM, Pedersen LC, Stafford DW, Tie JK. A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase. Nature Communications. 14: 828. PMID 36788244 DOI: 10.1038/s41467-023-36446-8 |
0.323 |
|
| 2021 |
Hao Z, Jin DY, Chen X, Schurgers LJ, Stafford DW, Tie JK. γ-Glutamyl carboxylase mutations differentially affect the biological function of vitamin K-dependent proteins. Blood. 137: 533-543. PMID 33507293 DOI: 10.1182/blood.2020006329 |
0.33 |
|
| 2020 |
Hao Z, Jin D, Chen X, Schurgers LJ, Stafford DW, Tie JK. Gamma-glutamyl carboxylase mutations differentially affect the biological function of vitamin K-dependent proteins. Blood. PMID 32785662 DOI: 10.1182/Blood.2020006329 |
0.437 |
|
| 2020 |
Chen X, Li C, Jin D, Ingram B, Hao Z, Bai X, Stafford DW, Hu K, Tie JK. A cell-based high-throughput screen identifies drugs that cause bleeding disorders by off-targeting the vitamin K cycle. Blood. PMID 32374827 DOI: 10.1182/Blood.2019004234 |
0.354 |
|
| 2019 |
Hao Z, Jin DY, Stafford DW, Tie JK. Vitamin K-dependent carboxylation of coagulation factors: insights from a cell-based functional study. Haematologica. PMID 31624106 DOI: 10.3324/Haematol.2019.229047 |
0.46 |
|
| 2019 |
Cooley B, Broze G, Mann DM, Lin FC, Pedersen LG, Stafford DW. Dysfunctional Endogenous FIX Impairs Prophylaxis in a Mouse Hemophilia B Model. Blood. PMID 30992271 DOI: 10.1182/Blood.2018884015 |
0.516 |
|
| 2018 |
Chen X, Jin DY, Stafford DW, Tie JK. Evaluation of oral anticoagulants with vitamin K epoxide reductase in its native milieu. Blood. PMID 30089628 DOI: 10.1182/Blood-2018-05-846592 |
0.413 |
|
| 2018 |
Wu S, Chen X, Jin DY, Stafford DW, Pedersen LG, Tie JK. Warfarin and vitamin K epoxide reductase: a molecular accounting for observed inhibition. Blood. PMID 29743176 DOI: 10.1182/Blood-2018-01-830901 |
0.637 |
|
| 2017 |
Sinhadri BCS, Jin DY, Stafford DW, Tie JK. Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions. Scientific Reports. 7: 17632. PMID 29247216 DOI: 10.1038/S41598-017-18008-3 |
0.478 |
|
| 2017 |
Jin DY, Ingram BO, Stafford DW, Tie JK. Molecular basis of the first reported clinical case of congenital combined deficiency of coagulation factors. Blood. PMID 28679738 DOI: 10.1182/Blood-2017-05-782367 |
0.344 |
|
| 2016 |
Tie JK, Stafford DW. Functional Study of the Vitamin K Cycle Enzymes in Live Cells. Methods in Enzymology. 584: 349-394. PMID 28065270 DOI: 10.1016/Bs.Mie.2016.10.015 |
0.451 |
|
| 2016 |
Jin DY, Vermeer C, Stafford DW, Tie JK. Splice-site mutation of exon 3 deletion in the gamma-glutamyl carboxylase gene causes inactivation of the enzyme. The Journal of Investigative Dermatology. PMID 27394683 DOI: 10.1016/J.Jid.2016.05.128 |
0.317 |
|
| 2016 |
Tie JK, Carneiro JD, Jin DY, Martinhago CD, Vermeer C, Stafford DW. Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and non-bleeding disorders. Blood. PMID 26758921 DOI: 10.1182/Blood-2015-10-677633 |
0.401 |
|
| 2016 |
Tie JK, Stafford DW. Structural and functional insights into enzymes of the vitamin K cycle. Journal of Thrombosis and Haemostasis : Jth. 14: 236-47. PMID 26663892 DOI: 10.1111/Jth.13217 |
0.467 |
|
| 2015 |
Cooley B, Mann DM, Monroe D, Lin F, Monahan PE, Stafford DW. At Equal Doses FIXFc (Alprolix) Is Not Significanly Better in a Saphenous Vein Bleeding Model Than Recombinant FIX (BeneFix) Seven Days Post-Infusion Blood. 126: 3490-3490. DOI: 10.1182/Blood.V126.23.3490.3490 |
0.312 |
|
| 2014 |
Tie JK, Jin DY, Stafford DW. Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration. The Journal of Biological Chemistry. 289: 9396-407. PMID 24532791 DOI: 10.1074/Jbc.M113.534446 |
0.471 |
|
| 2014 |
Parker CH, Morgan CR, Rand KD, Engen JR, Jorgenson JW, Stafford DW. A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry. Biochemistry. 53: 1511-20. PMID 24512177 DOI: 10.1021/Bi401536M |
0.424 |
|
| 2014 |
Feng D, Whinna H, Monroe D, Stafford DW. FVIIa as used pharmacologically is not TF dependent in hemophilia B mice. Blood. 123: 1764-6. PMID 24425804 DOI: 10.1182/Blood-2013-08-522987 |
0.334 |
|
| 2014 |
Wu S, Tie JK, Stafford DW, Pedersen LG. Membrane topology for human vitamin K epoxide reductase. Journal of Thrombosis and Haemostasis : Jth. 12: 112-4. PMID 24406068 DOI: 10.1111/Jth.12450 |
0.577 |
|
| 2014 |
Tie JK, Jin DY, Tie K, Stafford DW. Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cells. Journal of Thrombosis and Haemostasis : Jth. 11: 1556-64. PMID 23710884 DOI: 10.1111/Jth.12306 |
0.405 |
|
| 2014 |
Chu PH, Huang TY, Williams J, Stafford DW. Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH 2(Proceedings of the National Academy of Sciences of the United States of America (2006) 103, 51, (19308-19313) DOI:10.1073/pnas.0609401103) Proceedings of the National Academy of Sciences of the United States of America. 111: 3194. DOI: 10.1073/Pnas.1401722111 |
0.414 |
|
| 2013 |
Feng D, Stafford KA, Broze GJ, Stafford DW. Evidence of clinically significant extravascular stores of factor IX. Journal of Thrombosis and Haemostasis. 11: 2176-2178. PMID 24112220 DOI: 10.1111/Jth.12421 |
0.34 |
|
| 2013 |
Ingram BO, Turbyfill JL, Bledsoe PJ, Jaiswal AK, Stafford DW. Assessment of the contribution of NAD(P)H-dependent quinone oxidoreductase 1 (NQO1) to the reduction of vitamin K in wild-type and NQO1-deficient mice. The Biochemical Journal. 456: 47-54. PMID 24015818 DOI: 10.1042/Bj20130639 |
0.437 |
|
| 2013 |
Stafford DW. Extended action of FIX for improving the lifestyle of Hemophiliacs Journal of Blood Disorders and Transfusion. DOI: 10.4172/2155-9864.S1.004 |
0.313 |
|
| 2012 |
Tie JK, Jin DY, Stafford DW. Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms. The Journal of Biological Chemistry. 287: 33945-55. PMID 22923610 DOI: 10.1074/Jbc.M112.402941 |
0.435 |
|
| 2012 |
Tie JK, Jin DY, Stafford DW. Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells. Antioxidants & Redox Signaling. 16: 329-38. PMID 21939388 DOI: 10.1089/ars.2011.4043 |
0.341 |
|
| 2011 |
Wu S, Liu S, Davis CH, Stafford DW, Kulman JD, Pedersen LG. A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle. Journal of Theoretical Biology. 279: 143-9. PMID 21453708 DOI: 10.1016/J.Jtbi.2011.03.030 |
0.609 |
|
| 2011 |
Tie JK, Jin DY, Straight DL, Stafford DW. Functional study of the vitamin K cycle in mammalian cells. Blood. 117: 2967-74. PMID 21239697 DOI: 10.1182/Blood-2010-08-304303 |
0.445 |
|
| 2010 |
Wu S, Liu S, Davis CH, Stafford DW, Pedersen LG. Quantum Chemical Study of the Mechanism of Action of Vitamin K Carboxylase in Solvent. International Journal of Quantum Chemistry. 110: 2744-2751. PMID 21892230 DOI: 10.1002/Qua.22740 |
0.6 |
|
| 2010 |
Higgins-Gruber SL, Mutucumarana VP, Lin PJ, Jorgenson JW, Stafford DW, Straight DL. Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of {gamma}-glutamyl carboxylase. The Journal of Biological Chemistry. 285: 31502-8. PMID 20716530 DOI: 10.1074/Jbc.M110.143297 |
0.799 |
|
| 2009 |
Gui T, Reheman A, Ni H, Gross PL, Yin F, Monroe D, Monahan PE, Stafford DW. Abnormal hemostasis in a knock-in mouse carrying a variant of factor IX with impaired binding to collagen type IV. Journal of Thrombosis and Haemostasis : Jth. 7: 1843-51. PMID 19583826 DOI: 10.1111/J.1538-7836.2009.03545.X |
0.32 |
|
| 2008 |
Tie JK, Zheng MY, Hsiao KL, Perera L, Stafford DW, Straight DL. Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase. Biochemistry. 47: 6301-10. PMID 18498174 DOI: 10.1021/Bi800235R |
0.341 |
|
| 2008 |
Tie JK, Stafford DW. Structure and function of vitamin K epoxide reductase. Vitamins and Hormones. 78: 103-30. PMID 18374192 DOI: 10.1016/S0083-6729(07)00006-4 |
0.481 |
|
| 2007 |
Jin DY, Tie JK, Stafford DW. The conversion of vitamin K epoxide to vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines. Biochemistry. 46: 7279-83. PMID 17523679 DOI: 10.1021/Bi700527J |
0.446 |
|
| 2007 |
Davis CH, Ii DD, Stafford DW, Pedersen LG. Quantum chemical study of the mechanism of action of vitamin K carboxylase (VKC). IV. Intermediates and transition states. The Journal of Physical Chemistry. A. 111: 7257-61. PMID 17503787 DOI: 10.1021/Jp068564Y |
0.589 |
|
| 2007 |
Stafford DW, Roberts HR, Vermeer C. Vitamin K supplementation during oral anticoagulation: concerns. Blood. 109: 3607; author reply 3. PMID 17409344 DOI: 10.1182/Blood-2006-12-061200 |
0.403 |
|
| 2007 |
Davis CH, Deerfield D, Wymore T, Stafford DW, Pedersen LG. A quantum chemical study of the mechanism of action of Vitamin K epoxide reductase (VKOR) II. Transition states. Journal of Molecular Graphics & Modelling. 26: 401-8. PMID 17182266 DOI: 10.1016/J.Jmgm.2006.10.005 |
0.604 |
|
| 2007 |
Davis CH, Deerfield D, Wymore T, Stafford DW, Pedersen LG. A quantum chemical study of the mechanism of action of Vitamin K carboxylase (VKC) III. Intermediates and transition states. Journal of Molecular Graphics & Modelling. 26: 409-14. PMID 17182265 DOI: 10.1016/J.Jmgm.2006.10.006 |
0.584 |
|
| 2007 |
Zhang TP, Jin DY, Wardrop RM, Gui T, Maile R, Frelinger JA, Stafford DW, Monahan PE. Transgene expression levels and kinetics determine risk of humoral immune response modeled in factor IX knockout and missense mutant mice. Gene Therapy. 14: 429-40. PMID 17066096 DOI: 10.1038/Sj.Gt.3302881 |
0.304 |
|
| 2007 |
Schmidt-Krey I, Haase W, Mutucumarana V, Stafford DW, Kühlbrandt W. Two-dimensional crystallization of human vitamin K-dependent gamma-glutamyl carboxylase. Journal of Structural Biology. 157: 437-42. PMID 16979907 DOI: 10.1016/J.Jsb.2006.08.002 |
0.33 |
|
| 2006 |
Chu PH, Huang TY, Williams J, Stafford DW. Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2. Proceedings of the National Academy of Sciences of the United States of America. 103: 19308-13. PMID 17164330 DOI: 10.1073/Pnas.0609401103 |
0.454 |
|
| 2006 |
Tie JK, Zheng MY, Pope RM, Straight DL, Stafford DW. Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function. Biochemistry. 45: 14755-63. PMID 17144668 DOI: 10.1021/Bi0618518 |
0.341 |
|
| 2006 |
Chu P, Huang T, Williams J, Stafford DW. Purification of a Single Peptide with Vitamin K Epoxide to Vitamin K and Vitamin K to Vitamin KH2 Activity. Blood. 108: 331-331. DOI: 10.1182/Blood.V108.11.331.331 |
0.466 |
|
| 2006 |
Tie J, Zheng M, Stafford DW, Straight DL. Expression of a Two Chain Gamma-Glutamyl Carboxylase: Importance of Disulfide Bond Formation and Transmembrane Domain Interactions. Blood. 108: 1694-1694. DOI: 10.1182/Blood.V108.11.1694.1694 |
0.385 |
|
| 2006 |
Jin D, Tie J, Stafford DW. Mutational Analysis of VKOR. Blood. 108: 1628-1628. DOI: 10.1182/Blood.V108.11.1628.1628 |
0.346 |
|
| 2006 |
Deerfield D, Davis CH, Wymore T, Stafford DW, Pedersen LG. Quantum chemical study of the mechanism of action of Vitamin K Epoxide Reductase (VKOR) International Journal of Quantum Chemistry. 106: 2944-2952. DOI: 10.1002/Qua.21119 |
0.519 |
|
| 2005 |
Stafford DW. The vitamin K cycle. Journal of Thrombosis and Haemostasis : Jth. 3: 1873-8. PMID 16102054 DOI: 10.1111/J.1538-7836.2005.01419.X |
0.485 |
|
| 2005 |
Sun YM, Jin DY, Camire RM, Stafford DW. Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X. Blood. 106: 3811-5. PMID 16081695 DOI: 10.1182/Blood-2005-06-2495 |
0.46 |
|
| 2005 |
Tie JK, Nicchitta C, von Heijne G, Stafford DW. Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation. The Journal of Biological Chemistry. 280: 16410-6. PMID 15716279 DOI: 10.1074/Jbc.M500765200 |
0.44 |
|
| 2004 |
Tie JK, Jin DY, Loiselle DR, Pope RM, Straight DL, Stafford DW. Chemical modification of cysteine residues is a misleading indicator of their status as active site residues in the vitamin K-dependent gamma-glutamyl carboxylation reaction. The Journal of Biological Chemistry. 279: 54079-87. PMID 15492002 DOI: 10.1074/Jbc.M408945200 |
0.434 |
|
| 2004 |
Jin DY, Zhang TP, Gui T, Stafford DW, Monahan PE. Creation of a mouse expressing defective human factor IX. Blood. 104: 1733-9. PMID 15178576 DOI: 10.1182/Blood-2004-01-0138 |
0.305 |
|
| 2004 |
Soute BA, Jin DY, Spronk HM, Mutucumarana VP, Lin PJ, Hackeng TM, Stafford DW, Vermeer C. Characteristics of recombinant W501S mutated human gamma-glutamyl carboxylase. Journal of Thrombosis and Haemostasis : Jth. 2: 597-604. PMID 15102014 DOI: 10.1111/J.1538-7836.2004.00686.X |
0.797 |
|
| 2004 |
Li T, Chang CY, Jin DY, Lin PJ, Khvorova A, Stafford DW. Identification of the gene for vitamin K epoxide reductase. Nature. 427: 541-4. PMID 14765195 DOI: 10.1038/Nature02254 |
0.776 |
|
| 2004 |
Lin PJ, Straight DL, Stafford DW. Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product. The Journal of Biological Chemistry. 279: 6560-6. PMID 14660587 DOI: 10.1074/Jbc.M312239200 |
0.786 |
|
| 2004 |
Monahan PE, Zhang T, Jin D, Gui T, Stafford DW. 31. Creation of a Hemophilia B Mouse Expressing Defective Human Factor IX Molecular Therapy. 9. DOI: 10.1016/J.Ymthe.2004.05.054 |
0.306 |
|
| 2003 |
Mutucumarana VP, Acher F, Straight DL, Jin DY, Stafford DW. A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate. The Journal of Biological Chemistry. 278: 46488-93. PMID 12968027 DOI: 10.1074/Jbc.M307707200 |
0.442 |
|
| 2003 |
Tie JK, Mutucumarana VP, Straight DL, Carrick KL, Pope RM, Stafford DW. Determination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The Journal of Biological Chemistry. 278: 45468-75. PMID 12963724 DOI: 10.1074/Jbc.M309164200 |
0.39 |
|
| 2003 |
Wang CP, Yagi K, Lin PJ, Jin DY, Makabe KW, Stafford DW. Identification of a gene encoding a typical gamma-carboxyglutamic acid domain in the tunicate Halocynthia roretzi. Journal of Thrombosis and Haemostasis : Jth. 1: 118-23. PMID 12871548 DOI: 10.1046/j.1538-7836.2003.00069.x |
0.752 |
|
| 2002 |
Presnell SR, Stafford DW. The vitamin K-dependent carboxylase. Thrombosis and Haemostasis. 87: 937-46. PMID 12083499 DOI: 10.1055/S-0037-1613115 |
0.467 |
|
| 2002 |
Gui T, Lin HF, Jin DY, Hoffman M, Straight DL, Roberts HR, Stafford DW. Circulating and binding characteristics of wild-type factor IX and certain Gla domain mutants in vivo. Blood. 100: 153-8. PMID 12070021 DOI: 10.1182/Blood.V100.1.153 |
0.364 |
|
| 2002 |
Lin PJ, Jin DY, Tie JK, Presnell SR, Straight DL, Stafford DW. The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site. The Journal of Biological Chemistry. 277: 28584-91. PMID 12034728 DOI: 10.1074/Jbc.M202292200 |
0.797 |
|
| 2001 |
Presnell SR, Tripathy A, Lentz BR, Jin DY, Stafford DW. A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase. Biochemistry. 40: 11723-33. PMID 11570873 DOI: 10.1021/Bi010332W |
0.442 |
|
| 2001 |
Jin J, Chang J, Stafford DW, Straight DL. Residues Y179 and H101 of a hydrophobic patch of factor VII are involved in activation by factor Xa. Biochemistry. 40: 11405-10. PMID 11560488 DOI: 10.1021/Bi010990G |
0.349 |
|
| 2001 |
Jin J, Perera L, Stafford D, Pedersen L. Four loops of the catalytic domain of factor VIIa mediate the effect of the first EGF-like domain substitution on factor VIIa catalytic activity Journal of Molecular Biology. 307: 1503-1517. PMID 11292356 DOI: 10.1006/Jmbi.2001.4556 |
0.555 |
|
| 2000 |
Perera L, Foley C, Darden TA, Stafford D, Mather T, Esmon CT, Pedersen LG. Modeling zymogen protein C. Biophysical Journal. 79: 2925-43. PMID 11106601 DOI: 10.1016/S0006-3495(00)76530-1 |
0.55 |
|
| 2000 |
Camire RM, Larson PJ, Stafford DW, High KA. Enhanced γ-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide Biochemistry. 39: 14322-14329. PMID 11087381 DOI: 10.1021/Bi001074Q |
0.371 |
|
| 2000 |
Mutucumarana VP, Stafford DW, Stanley TB, Jin DY, Solera J, Brenner B, Azerad R, Wu SM. Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase. The Journal of Biological Chemistry. 275: 32572-7. PMID 10934213 DOI: 10.1074/Jbc.M006808200 |
0.481 |
|
| 2000 |
Li T, Yang CT, Jin D, Stafford DW. Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase. The Journal of Biological Chemistry. 275: 18291-6. PMID 10748045 DOI: 10.1074/Jbc.M001790200 |
0.456 |
|
| 2000 |
Tie J, Wu S, Jin D, Nicchitta CV, Stafford DW. A topological study of the human γ-glutamyl carboxylase Blood. 96: 973-978. DOI: 10.1182/Blood.V96.3.973.015K55_973_978 |
0.365 |
|
| 1999 |
Stanley TB, Humphries J, High KA, Stafford DW. Amino acids responsible for reduced affinities of vitamin K-dependent propeptides for the carboxylase Biochemistry. 38: 15681-15687. PMID 10569955 DOI: 10.1021/Bi991544K |
0.453 |
|
| 1999 |
Houben RJTJ, Jin D, Stafford DW, Proost P, Ebberink RHM, Vermeer C, Soute BAM. Osteocalcin binds tightly to the γ-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins Biochemical Journal. 341: 265-269. PMID 10393081 DOI: 10.1042/0264-6021:3410265 |
0.387 |
|
| 1999 |
Stanley TB, Jin DY, Lin PJ, Stafford DW. The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase. The Journal of Biological Chemistry. 274: 16940-4. PMID 10358041 DOI: 10.1074/Jbc.274.24.16940 |
0.803 |
|
| 1999 |
Jin J, Chang J, Chang JY, Kelley RF, Stafford DW, Straight DL. Factor VIIa's first epidermal growth factor-like domain's role in catalytic activity. Biochemistry. 38: 1185-92. PMID 9930978 DOI: 10.1021/Bi981686Z |
0.33 |
|
| 1999 |
Snyder RO, Miao C, Meuse L, Tubb J, Donahue BA, Lin HF, Stafford DW, Patel S, Thompson AR, Nichols T, Read MS, Bellinger DA, Brinkhous KM, Kay MA. Correction of hemophilia B in canine and murine models using recombinant adeno-associated viral vectors Nature Medicine. 5: 64-70. PMID 9883841 DOI: 10.1038/4751 |
0.301 |
|
| 1999 |
Houben RJTJ, Jin D, Stafford DW, Proost P, Ebberink RHM, Vermeer C, Soute BAM. Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. Biochemical Journal. 341: 265-269. DOI: 10.1042/Bj3410265 |
0.484 |
|
| 1998 |
Stanley TB, Wu SM, Houben RJ, Mutucumarana VP, Stafford DW. Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase. Biochemistry. 37: 13262-8. PMID 9748333 DOI: 10.1021/Bi981031Y |
0.461 |
|
| 1998 |
Chang J, Jin J, Lollar P, Bode W, Brandstetter H, Hamaguchi N, Straight DL, Stafford DW. Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity. The Journal of Biological Chemistry. 273: 12089-94. PMID 9575152 DOI: 10.1074/Jbc.273.20.12089 |
0.325 |
|
| 1998 |
Wojcik EGC, Cheung WF, Van Den Berg M, Van Der Linden IK, Stafford DW, Bertina RM. Identification of residues in the Gla-domain of human factor IX involved in the binding to conformation specific antibodies Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1382: 91-101. PMID 9507074 DOI: 10.1016/S0167-4838(97)00149-0 |
0.317 |
|
| 1998 |
Brenner B, Sánchez-Vega B, Wu S, Lanir N, Stafford DW, Solera J. A Missense Mutation in γ-Glutamyl Carboxylase Gene Causes Combined Deficiency of All Vitamin K-Dependent Blood Coagulation Factors Blood. 92: 4554-4559. DOI: 10.1182/Blood.V92.12.4554.424K42_4554_4559 |
0.359 |
|
| 1997 |
Lin HF, Maeda N, Smithies O, Straight DL, Stafford DW. A coagulation factor IX-deficient mouse model for human hemophilia B. Blood. 90: 3962-6. PMID 9354664 DOI: 10.1182/Blood.V90.10.3962 |
0.321 |
|
| 1997 |
Wu SM, Mutucumarana VP, Stafford DW. Purification of gamma-glutamyl carboxylase from bovine liver. Methods in Enzymology. 282: 346-57. PMID 9330300 DOI: 10.1016/S0076-6879(97)82119-2 |
0.353 |
|
| 1997 |
Chang JY, Monroe DM, Stafford DW, Brinkhous KM, Roberts HR. Replacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B Journal of Clinical Investigation. 100: 886-892. PMID 9259588 DOI: 10.1172/Jci119604 |
0.322 |
|
| 1997 |
Wolberg AS, Stafford DW, Erie DA. Human factor IX binds to specific sites on the collagenous domain of collagen IV. The Journal of Biological Chemistry. 272: 16717-20. PMID 9201971 DOI: 10.1074/Jbc.272.27.16717 |
0.382 |
|
| 1997 |
Stanley TB, Stafford DW, Olivera BM, Bandyopadhyay PK. Identification of a vitamin K-dependent carboxylase in the venom duct of a Conus snail. Febs Letters. 407: 85-8. PMID 9141486 DOI: 10.1016/S0014-5793(97)00299-8 |
0.474 |
|
| 1997 |
Wu SM, Mutucumarana VP, Geromanos S, Stafford DW. The propeptide binding site of the bovine gamma-glutamyl carboxylase. The Journal of Biological Chemistry. 272: 11718-22. PMID 9115224 DOI: 10.1074/Jbc.272.18.11718 |
0.424 |
|
| 1997 |
Wolberg AS, Morris DP, Stafford DW. Factor IX activation by factor XIa proceeds without release of a free intermediate Biochemistry. 36: 4074-4079. PMID 9100000 DOI: 10.1021/Bi962274Y |
0.304 |
|
| 1996 |
Chu K, Wu SM, Stanley T, Stafford DW, High KA. A mutation in the propeptide of factor IX leads to warfarin sensitivity by a novel mechanism Journal of Clinical Investigation. 98: 1619-1625. PMID 8833911 DOI: 10.1172/Jci118956 |
0.418 |
|
| 1996 |
Wolberg AS, Li L, Cheung WF, Hamaguchi N, Pedersen LG, Stafford DW. Characterization of gamma-carboxyglutamic acid residue 21 of human factor IX. Biochemistry. 35: 10321-7. PMID 8756687 DOI: 10.1021/Bi960502I |
0.581 |
|
| 1996 |
Cheung WF, Stafford DW, Sugo T. Localization of a calcium-dependent epitope to the amino terminal region of the Gla domain of human factor IX. Thrombosis Research. 81: 65-73. PMID 8747521 DOI: 10.1016/0049-3848(95)00214-6 |
0.367 |
|
| 1995 |
Cheung WF, Wolberg AS, Stafford DW, Smith KJ. Localization of a metal-dependent epitope to the amino terminal residues 33-40 of human factor IX Thrombosis Research. 80: 419-427. PMID 8588203 DOI: 10.1016/0049-3848(95)00194-V |
0.373 |
|
| 1995 |
Morris DP, Stevens RD, Wright DJ, Stafford DW. Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate. The Journal of Biological Chemistry. 270: 30491-8. PMID 8530480 DOI: 10.1074/Jbc.270.51.30491 |
0.448 |
|
| 1995 |
Cheung WF, Stafford DW. Localization of an epitope of a calcium-dependent monoclonal antibody to the N-terminal region of the Gla domain of human factor VII. Thrombosis Research. 79: 199-206. PMID 7676406 DOI: 10.1016/0049-3848(95)00105-Z |
0.315 |
|
| 1995 |
Chang JY, Stafford DW, Straight DL. The roles of factor VII's structural domains in tissue factor binding. Biochemistry. 34: 12227-32. PMID 7547964 DOI: 10.1021/Bi00038A017 |
0.351 |
|
| 1994 |
Ahmad SS, Rawala-Sheikh R, Cheung WF, Jameson BA, Stafford DW, Walsh PN. High-affinity, specific factor IXa binding to platelets is mediated in part by residues 3-11. Biochemistry. 33: 12048-55. PMID 7918424 DOI: 10.1021/Bi00206A006 |
0.367 |
|
| 1994 |
Hamaguchi N, Stafford D. In Vitro Mutagenesis Study of Two Critical Glutamic Acids in the Calcium Binding Loop of the Factor IX Heavy Chain Thrombosis and Haemostasis. 72: 856-861. DOI: 10.1055/S-0038-1648974 |
0.373 |
|
| 1993 |
Hamaguchi N, Roberts H, Stafford DW. Mutations in the catalytic domain of factor IX that are related to the subclass hemophilia Bm. Biochemistry. 32: 6324-9. PMID 8518277 DOI: 10.1021/Bi00076A004 |
0.397 |
|
| 1992 |
Toomey JR, Smith KJ, Roberts HR, Stafford DW. The endothelial cell binding determinant of human factor IX resides in the gamma-carboxyglutamic acid domain. Biochemistry. 31: 1806-8. PMID 1310619 DOI: 10.1021/Bi00121A031 |
0.371 |
|
| 1991 |
Wu SM, Morris DP, Stafford DW. Identification and purification to near homogeneity of the vitamin K-dependent carboxylase. Proceedings of the National Academy of Sciences of the United States of America. 88: 2236-40. PMID 2006163 DOI: 10.1073/Pnas.88.6.2236 |
0.47 |
|
| 1991 |
Wu SM, Cheung WF, Frazier D, Stafford DW. Cloning and expression of the cDNA for human γ-glutamyl carboxylase Science. 254: 1634-1636. PMID 1749935 DOI: 10.1126/Science.1749935 |
0.416 |
|
| 1988 |
Ware J, Toomey JR, Stafford DW. Localization of a factor VIII-inhibiting antibody epitope to a region between residues 338 and 362 of factor VIII heavy chain. Proceedings of the National Academy of Sciences of the United States of America. 85: 3165-9. PMID 2452445 DOI: 10.1073/Pnas.85.9.3165 |
0.329 |
|
| 1987 |
Lin SW, Dunn JJ, Studier FW, Stafford DW. Expression of human factor IX and its subfragments in Escherichia coli and generation of antibodies to the subfragments. Biochemistry. 26: 5267-74. PMID 2823876 DOI: 10.1021/Bi00391A009 |
0.337 |
|
| 1987 |
Davis L, McGraw R, Ware J, Roberts H, Stafford D. Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B Blood. 69: 140-143. DOI: 10.1182/Blood.V69.1.140.Bloodjournal691140 |
0.344 |
|
| 1985 |
McGraw RA, Davis LM, Noyes CM, Lundblad RL, Roberts HR, Graham JB, Stafford DW. Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX. Proceedings of the National Academy of Sciences of the United States of America. 82: 2847-51. PMID 3857619 DOI: 10.1073/Pnas.82.9.2847 |
0.303 |
|
| 1983 |
Sittman DB, Stafford DW. Purification and characterization of the RNA polymerases of the sea urchin, Lytechinus variegatus. Preparative Biochemistry. 13: 21-39. PMID 6856583 DOI: 10.1080/00327488308068732 |
0.676 |
|
| 1975 |
Christopher CW, Sittman DB, Stafford DW. Phenylalanine transfer ribonucleic acid synthetase from Drosophila melanogaster. Purification and properties. Archives of Biochemistry and Biophysics. 166: 94-101. PMID 235897 DOI: 10.1016/0003-9861(75)90369-0 |
0.689 |
|
| 1972 |
Pelley JW, Stafford DW. Studies on the enzymatic binding of aminoacyl transfer ribonucleic acid to ribosomes in a Drosophila in vitro system. Biochemistry. 9: 3408-14. PMID 4941834 DOI: 10.1021/Bi00819A019 |
0.356 |
|
| 1970 |
Pelley JW, Stafford DW. Partial purification of the aminoacyl-tRNA binding enzyme from Drosophila larvae. Biochimica Et Biophysica Acta. 204: 400-5. PMID 5441186 DOI: 10.1016/0005-2787(70)90159-0 |
0.344 |
|
| 1964 |
STAFFORD DW, SOFER WH, IVERSON RM. DEMONSTRATION OF POLYRIBOSOMES AFTER FERTILIZATION OF THE SEA URCHIN EGG. Proceedings of the National Academy of Sciences of the United States of America. 52: 313-6. PMID 14206596 DOI: 10.1073/pnas.52.2.313 |
0.649 |
|
| 1964 |
STAFFORD DW, IVERSON RM. RADIOAUTOGRAPHIC EVIDENCE FOR THE INCORPORATION OF LEUCINE-CARBON-14 INTO THE MITOTIC APPARATUS. Science (New York, N.Y.). 143: 580-1. PMID 14080326 DOI: 10.1126/science.143.3606.580 |
0.649 |
|
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