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Results: 1-17 |
Results: 17

Authors: ABRAHAMS JP DEGRAAFF RAG
Citation: Jp. Abrahams et Rag. Degraaff, NEW DEVELOPMENTS IN PHASE REFINEMENT, Current opinion in structural biology, 8(5), 1998, pp. 601-605

Authors: SKINNER R CHANG WSW JIN L PEI X HUNTINGTON JA ABRAHAMS JP CARRELL RW LOMAS DA
Citation: R. Skinner et al., IMPLICATIONS FOR FUNCTION AND THERAPY OF A 2.9 ANGSTROM STRUCTURE OF BINARY-COMPLEXED ANTITHROMBIN, Journal of Molecular Biology, 283(1), 1998, pp. 9-14

Authors: ELLIOTT PR ABRAHAMS JP LOMAS DA
Citation: Pr. Elliott et al., WILD-TYPE ALPHA(1)-ANTITRYPSIN IS IN THE CANONICAL INHIBITORY CONFORMATION, Journal of Molecular Biology, 275(3), 1998, pp. 419-425

Authors: SHIRAKIHARA Y LESLIE AGW ABRAHAMS JP WALKER JE UEDA T SEKIMOTO Y KAMBARA M SAIKA K KAGAWA Y YOSHIDA M
Citation: Y. Shirakihara et al., THE CRYSTAL-STRUCTURE OF THE NUCLEOTIDE-FREE ALPHA-3-BETA-3 SUBCOMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3 IS A SYMMETRICAL TRIMER, Structure, 5(6), 1997, pp. 825-836

Authors: WARDELL MR SKINNER R CARTER DC TWIGG PD ABRAHAMS JP
Citation: Mr. Wardell et al., IMPROVED DIFFRACTION OF ANTITHROMBIN CRYSTALS GROWN IN MICROGRAVITY, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 622-625

Authors: ABRAHAMS JP
Citation: Jp. Abrahams, BIAS REDUCTION IN PHASE REFINEMENT BY MODIFIED INTERFERENCE FUNCTIONS- INTRODUCING THE GAMMA-CORRECTION, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 371-376

Authors: CARRELL R SKINNER R JIN L ABRAHAMS JP
Citation: R. Carrell et al., STRUCTURAL MOBILITY OF ANTITHROMBIN AND ITS MODULATION BY HEPARIN, Thrombosis and haemostasis, 78(1), 1997, pp. 516-519

Authors: JIN L ABRAHAMS JP SKINNER R PETITOU M PIKE RN CARRELL RW
Citation: L. Jin et al., THE ANTICOAGULANT ACTIVATION OF ANTITHROMBIN BY HEPARIN, Proceedings of the National Academy of Sciences of the United Statesof America, 94(26), 1997, pp. 14683-14688

Authors: SKINNER R ABRAHAMS JP WHISSTOCK JC LESK AM CARRELL RW WARDELL MR
Citation: R. Skinner et al., THE 2.6-ANGSTROM STRUCTURE OF ANTITHROMBIN INDICATES A CONFORMATIONALCHANGE AT THE HEPARIN-BINDING SITE, Journal of Molecular Biology, 266(3), 1997, pp. 601-609

Authors: ELLIOTT PR LOMAS DA CARRELL RW ABRAHAMS JP
Citation: Pr. Elliott et al., INHIBITORY CONFORMATION OF THE REACTIVE LOOP OF ALPHA(1)-ANTITRYPSIN, Nature structural biology, 3(8), 1996, pp. 676-681

Authors: ABRAHAMS JP LESLIE AGW
Citation: Jp. Abrahams et Agw. Leslie, METHODS USED IN THE STRUCTURE DETERMINATION OF BOVINE MITOCHONDRIAL F1 ATPASE, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 30-42

Authors: ABRAHAMS JP BUCHANAN SK VANRAAIJ MJ FEARNLEY IM LESLIE AGW WALKER JE
Citation: Jp. Abrahams et al., THE STRUCTURE OF BOVINE F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN, Proceedings of the National Academy of Sciences of the United Statesof America, 93(18), 1996, pp. 9420-9424

Authors: VANRAAIJ MJ ABRAHAMS JP LESLIE AGW WALKER JE
Citation: Mj. Vanraaij et al., THE STRUCTURE OF BOVINE F1-ATPASE COMPLEXED WITH THE ANTIBIOTIC INHIBITOR AUROVERTIN-B, Proceedings of the National Academy of Sciences of the United Statesof America, 93(14), 1996, pp. 6913-6917

Authors: ABRAHAMS JP LESLIE AGW LUTTER R WALKER JE
Citation: Jp. Abrahams et al., THE STRUCTURE OF BOVINE MITOCHONDRIAL F1-ATPASE - AN INSIGHT INTO ATPSYNTHESIS, Biophysical journal, 70(2), 1996, p.

Authors: ABRAHAMS JP LESLIE AGW LUTTER R WALKER JE
Citation: Jp. Abrahams et al., STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA, Nature, 370(6491), 1994, pp. 621-628

Authors: ABRAHAMS JP LUTTER R TODD RJ VANRAAIJ MJ LESLIE AGW WALKER JE
Citation: Jp. Abrahams et al., INHERENT ASYMMETRY OF THE STRUCTURE OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA AT 6.5 ANGSTROM RESOLUTION, EMBO journal, 12(5), 1993, pp. 1775-1780

Authors: WARDELL MR ABRAHAMS JP BRUCE D SKINNER R LESLIE AGW
Citation: Mr. Wardell et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF 2 CONFORMATIONS OF INTACT HUMAN ANTITHROMBIN, Journal of Molecular Biology, 234(4), 1993, pp. 1253-1258
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