Year |
Citation |
Score |
2007 |
Rios-Steiner JL, Murakami MT, Tulinsky A, Arni RK. Active and exo-site inhibition of human factor Xa: structure of des-Gla factor Xa inhibited by NAP5, a potent nematode anticoagulant protein from Ancylostoma caninum. Journal of Molecular Biology. 371: 774-86. PMID 17588602 DOI: 10.1016/J.Jmb.2007.05.042 |
0.495 |
|
2007 |
Murakami MT, Rios-Steiner J, Weaver SE, Tulinsky A, Geiger JH, Arni RK. Intermolecular interactions and characterization of the novel factor Xa exosite involved in macromolecular recognition and inhibition: crystal structure of human Gla-domainless factor Xa complexed with the anticoagulant protein NAPc2 from the hematophagous nematode Ancylostoma caninum. Journal of Molecular Biology. 366: 602-10. PMID 17173931 DOI: 10.1016/J.Jmb.2006.11.040 |
0.439 |
|
2004 |
Pineda AO, Zhang E, Guinto ER, Savvides SN, Tulinsky A, Di Cera E. Crystal structure of the thrombin mutant D221A/D222K: the Asp222:Arg187 ion-pair stabilizes the fast form. Biophysical Chemistry. 112: 253-6. PMID 15572256 DOI: 10.1016/J.Bpc.2004.07.027 |
0.476 |
|
2003 |
Bell BJ, Watanabe L, Rios-Steiner JL, Tulinsky A, Lebioda L, Arni RK. Structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida. Acta Crystallographica. Section D, Biological Crystallography. 59: 1454-8. PMID 12876349 DOI: 10.1107/S0907444903013192 |
0.458 |
|
2003 |
Hasan AA, Warnock M, Nieman M, Srikanth S, Mahdi F, Krishnan R, Tulinsky A, Schmaier AH. Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin. American Journal of Physiology. Heart and Circulatory Physiology. 285: H183-93. PMID 12598231 DOI: 10.1152/Ajpheart.00490.2002 |
0.404 |
|
2002 |
Abad MC, Arni RK, Grella DK, Castellino FJ, Tulinsky A, Geiger JH. The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin. Journal of Molecular Biology. 318: 1009-17. PMID 12054798 DOI: 10.1016/S0022-2836(02)00211-5 |
0.492 |
|
2001 |
Rios-Steiner JL, Schenone M, Mochalkin I, Tulinsky A, Castellino FJ. Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein. Journal of Molecular Biology. 308: 705-19. PMID 11350170 DOI: 10.1006/Jmbi.2001.4646 |
0.522 |
|
2000 |
Krishnan R, Sadler JE, Tulinsky A. Structure of the Ser195Ala mutant of human alpha--thrombin complexed with fibrinopeptide A(7--16): evidence for residual catalytic activity. Acta Crystallographica. Section D, Biological Crystallography. 56: 406-10. PMID 10739913 DOI: 10.1107/S0907444900001487 |
0.432 |
|
2000 |
St Charles R, Padmanabhan K, Arni RV, Padmanabhan KP, Tulinsky A. Structure of tick anticoagulant peptide at 1.6 A resolution complexed with bovine pancreatic trypsin inhibitor. Protein Science : a Publication of the Protein Society. 9: 265-72. PMID 10716178 DOI: 10.1110/Ps.9.2.265 |
0.484 |
|
2000 |
Krishnan R, Mochalkin I, Arni R, Tulinsky A. Structure of thrombin complexed with selective non-electrophilic inhibitors having cyclohexyl moieties at P1. Acta Crystallographica. Section D, Biological Crystallography. 56: 294-303. PMID 10713516 DOI: 10.1107/S0907444900000068 |
0.461 |
|
1999 |
Arni RK, Padmanabhan KP, Tulinsky A. Crystallization and preliminary diffraction data of a platelet-aggregation inhibitor from the venom of Agkistrodon piscivorus piscivorus (North American water moccasin). Acta Crystallographica. Section D, Biological Crystallography. 55: 1468-70. PMID 10417418 DOI: 10.1107/S0907444999006332 |
0.409 |
|
1999 |
St Charles R, Matthews JH, Zhang E, Tulinsky A. Bound structures of novel P3-P1' beta-strand mimetic inhibitors of thrombin. Journal of Medicinal Chemistry. 42: 1376-83. PMID 10212123 DOI: 10.1021/Jm980052N |
0.472 |
|
1999 |
Mochalkin I, Tulinsky A. Structures of thrombin retro-inhibited with SEL2711 and SEL2770 as they relate to factor Xa binding. Acta Crystallographica. Section D, Biological Crystallography. 55: 785-93. PMID 10089309 DOI: 10.1107/S0907444999000359 |
0.48 |
|
1999 |
Mochalkin I, Cheng B, Klezovitch O, Scanu AM, Tulinsky A. Recombinant kringle IV-10 modules of human apolipoprotein(a): structure, ligand binding modes, and biological relevance. Biochemistry. 38: 1990-8. PMID 10026282 DOI: 10.1021/Bi9820558 |
0.453 |
|
1999 |
Zhang E, St Charles R, Tulinsky A. Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant. Journal of Molecular Biology. 285: 2089-104. PMID 9925787 DOI: 10.1006/Jmbi.1998.2452 |
0.418 |
|
1999 |
Makedonopoulou S, Tulinsky A, Mavridis IM. The Dimeric Complex of Beta-Cyclodextrin with 1,13-tridecanedioic acid Supramolecular Chemistry. 11: 73-81. DOI: 10.1080/10610279908048718 |
0.398 |
|
1998 |
Krishnan R, Zhang E, Hakansson K, Arni RK, Tulinsky A, Lim-Wilby MS, Levy OE, Semple JE, Brunck TK. Highly selective mechanism-based thrombin inhibitors: structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes. Biochemistry. 37: 12094-103. PMID 9724521 DOI: 10.1021/Bi980840E |
0.454 |
|
1998 |
Liaw PC, Fredenburgh JC, Stafford AR, Tulinsky A, Austin RC, Weitz JI. Localization of the thrombin-binding domain on prothrombin fragment 2. The Journal of Biological Chemistry. 273: 8932-9. PMID 9535876 DOI: 10.1074/Jbc.273.15.8932 |
0.369 |
|
1998 |
Chang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ. Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry. 37: 3258-71. PMID 9521645 DOI: 10.1021/Bi972284E |
0.479 |
|
1998 |
Rios Steiner JL, Murakami M, Tulinsky A. Structure of thrombin inhibited by aeruginosin 298-A from a blue-green alga Journal of the American Chemical Society. 120: 597-598. DOI: 10.2210/Pdb1A2C/Pdb |
0.361 |
|
1997 |
Sabharwal AK, Padmanabhan K, Tulinsky A, Mathur A, Gorka J, Bajaj SP. Interaction of calcium with native and decarboxylated human factor X. Effect of proteolysis in the autolysis loop on catalytic efficiency and factor Va binding. The Journal of Biological Chemistry. 272: 22037-45. PMID 9268343 DOI: 10.1074/jbc.272.35.22037 |
0.311 |
|
1997 |
Zhang E, Tulinsky A. The molecular environment of the Na+ binding site of thrombin. Biophysical Chemistry. 63: 185-200. PMID 9108691 DOI: 10.1016/S0301-4622(96)02227-2 |
0.469 |
|
1996 |
Padmanabhan K, Tulinsky A. An ambiguous structure of a DNA 15-mer thrombin complex. Acta Crystallographica. Section D, Biological Crystallography. 52: 272-82. PMID 15299700 DOI: 10.1107/S0907444995013977 |
0.417 |
|
1996 |
Matthews JH, Krishnan R, Costanzo MJ, Maryanoff BE, Tulinsky A. Crystal structures of thrombin with thiazole-containing inhibitors: probes of the S1' binding site. Biophysical Journal. 71: 2830-9. PMID 8913620 DOI: 10.1016/S0006-3495(96)79479-1 |
0.473 |
|
1996 |
Krishnan R, Tulinsky A, Vlasuk GP, Pearson D, Vallar P, Bergum P, Brunck TK, Ripka WC. Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an alpha-keto-amide transition-state mimetic. Protein Science : a Publication of the Protein Society. 5: 422-33. PMID 8868478 DOI: 10.1002/Pro.5560050303 |
0.448 |
|
1996 |
Tulinsky A. Molecular Interactions of Thrombin. Seminars in Thrombosis and Hemostasis. 22: 117-24. PMID 8807707 DOI: 10.1055/S-2007-998998 |
0.425 |
|
1996 |
Ganesh V, Lee AY, Clardy J, Tulinsky A. Comparison of the structures of the cyclotheonamide A complexes of human alpha-thrombin and bovine beta-trypsin. Protein Science : a Publication of the Protein Society. 5: 825-35. PMID 8732754 DOI: 10.1002/Pro.5560050504 |
0.504 |
|
1996 |
Mathews II, Vanderhoff-Hanaver P, Castellino FJ, Tulinsky A. Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid. Biochemistry. 35: 2567-76. PMID 8611560 DOI: 10.1021/Bi9521351 |
0.482 |
|
1996 |
Matthews JH, Krishnan R, Costanzo MJ, Maryanoff BE, Tulinsky A. Thrombin complexes with thiazole-based inhibitors: useful probes of the S1' binding site Acta Crystallographica Section a Foundations of Crystallography. 52: C205-C205. DOI: 10.1107/S0108767396091131 |
0.382 |
|
1996 |
Rios Steiner JL, Tulinsky A. The crystal structure of α-thrombin with a new type of inhibitor: aeruginosin 298-A Acta Crystallographica Section a Foundations of Crystallography. 52: C206-C206. DOI: 10.1107/S0108767396091106 |
0.377 |
|
1996 |
St Charles R, Vanderhoff-Hanaver P, Boatman D, Ogdu C, Tulinsky A. Crystal structures of two thrombin complexes with novel peptide mimetic inhibitors Acta Crystallographica Section a Foundations of Crystallography. 52: C207-C207. DOI: 10.1107/S0108767396091076 |
0.403 |
|
1996 |
Zhang E, Arni RK, Levy OE, Tulinsky A. Stereochemical considerations in drug design: the crystal structures of human α-thrombin complexed with two tripeptidyl aldehyde inhibitors at 2.1 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 52: C209-C208. DOI: 10.1107/S0108767396091015 |
0.376 |
|
1996 |
Greco MN, Powell ET, Hecker LR, Andrade-Gordon P, Kauffman JA, Lewis JM, Ganesh V, Tulinsky A, Maryanoff BE. Novel thombin inhibitors that are based on a macrocyclic tripeptide motif Bioorganic and Medicinal Chemistry Letters. 6: 2947-2952. DOI: 10.1016/S0960-894X(96)00554-9 |
0.371 |
|
1996 |
Maryanoff BE, Zhang HC, Greco MN, Zhang E, Vanderhoff-Hanaver P, Tulinsky A. Transformation of the marine natural product cyclotheonamide A by aqueous base. X-ray analysis of a novel ligand complexed with human α-thrombin Tetrahedron Letters. 37: 3667-3670. DOI: 10.1016/0040-4039(96)00658-2 |
0.31 |
|
1995 |
Mathews II, Tulinsky A. Active-site mimetic inhibition of thrombin. Acta Crystallographica. Section D, Biological Crystallography. 51: 550-9. PMID 15299843 DOI: 10.1107/S0907444994013132 |
0.447 |
|
1995 |
Arni RK, Ward RJ, Gutierrez JM, Tulinsky A. Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom. Acta Crystallographica. Section D, Biological Crystallography. 51: 311-7. PMID 15299297 DOI: 10.1107/S0907444994011455 |
0.434 |
|
1995 |
Di Cera E, Guinto ER, Vindigni A, Dang QD, Ayala YM, Wuyi M, Tulinsky A. The Na+ binding site of thrombin. The Journal of Biological Chemistry. 270: 22089-92. PMID 7673182 DOI: 10.1074/Jbc.270.38.22089 |
0.439 |
|
1995 |
Håkansson K, Tulinsky A, Abelman MM, Miller TA, Vlasuk GP, Bergum PW, Lim-Wilby MS, Brunck TK. Crystallographic structure of a peptidyl keto acid inhibitor and human alpha-thrombin. Bioorganic & Medicinal Chemistry. 3: 1009-17. PMID 7582975 DOI: 10.1016/0968-0896(95)00096-Y |
0.465 |
|
1994 |
Johnson ME, Lin Z, Padmanabhan K, Tulinsky A, Kahn M. Conformational rearrangements required of the V3 loop of HIV-1 gp120 for proteolytic cleavage and infection. Febs Letters. 337: 4-8. PMID 8276110 DOI: 10.1016/0014-5793(94)80618-7 |
0.355 |
|
1994 |
Arni RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A. Structure of the non-covalent complex of prothrombin kringle 2 with PPACK-thrombin. Chemistry and Physics of Lipids. 67: 59-66. PMID 8187245 DOI: 10.1016/0009-3084(94)90124-4 |
0.504 |
|
1994 |
Mathews II, Padmanabhan KP, Ganesh V, Tulinsky A, Ishii M, Chen J, Turck CW, Coughlin SR, Fenton JW. Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Biochemistry. 33: 3266-79. PMID 8136362 DOI: 10.1021/Bi00177A018 |
0.4 |
|
1994 |
Seshadri TP, Skrzypczak-Jankun E, Yin M, Tulinsky A. Differences in the metal ion structure between Sr- and Ca-prothrombin fragment 1. Biochemistry. 33: 1087-92. PMID 8110739 DOI: 10.1021/Bi00171A006 |
0.328 |
|
1994 |
Rydel TJ, Yin M, Padmanabhan KP, Blankenship DT, Cardin AD, Correa PE, Fenton JW, Tulinsky A. Crystallographic structure of human gamma-thrombin. The Journal of Biological Chemistry. 269: 22000-6. PMID 8071320 DOI: 10.2210/Pdb2Hnt/Pdb |
0.492 |
|
1994 |
Padmanabhan K, Wu TP, Ravichandran KG, Tulinsky A. Kringle-kringle interactions in multimer kringle structures. Protein Science : a Publication of the Protein Society. 3: 898-910. PMID 8069221 DOI: 10.1002/Pro.5560030605 |
0.502 |
|
1994 |
Wu TP, Padmanabhan KP, Tulinsky A. The structure of recombinant plasminogen kringle 1 and the fibrin binding site. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 5: 157-66. PMID 8054447 |
0.369 |
|
1994 |
Christiansen WT, Tulinsky A, Castellino FJ. Functions of individual gamma-carboxyglutamic acid (Gla) residues of human protein c. Determination of functionally nonessential Gla residues and correlations with their mode of binding to calcium. Biochemistry. 33: 14993-5000. PMID 7999756 DOI: 10.1021/Bi00254A007 |
0.349 |
|
1994 |
Vijayalakshmi J, Padmanabhan KP, Mann KG, Tulinsky A. The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin. Protein Science : a Publication of the Protein Society. 3: 2254-71. PMID 7756983 DOI: 10.1002/Pro.5560031211 |
0.524 |
|
1993 |
Tulinsky A, Qiu X. Active site and exosite binding of alpha-thrombin. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 4: 305-12. PMID 8499567 |
0.338 |
|
1993 |
Arni RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A. Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Biochemistry. 32: 4727-37. PMID 8387813 DOI: 10.1021/Bi00069A006 |
0.495 |
|
1993 |
Qiu X, Yin M, Padmanabhan KP, Krstenansky JL, Tulinsky A. Structures of thrombin complexes with a designed and a natural exosite peptide inhibitor. The Journal of Biological Chemistry. 268: 20318-26. PMID 8376390 DOI: 10.2210/Pdb1Thr/Pdb |
0.444 |
|
1993 |
Maryanoff BE, Qiu X, Padmanabhan KP, Tulinsky A, Almond HR, Andrade-Gordon P, Greco MN, Kauffman JA, Nicolaou KC, Liu A. Molecular basis for the inhibition of human alpha-thrombin by the macrocyclic peptide cyclotheonamide A. Proceedings of the National Academy of Sciences of the United States of America. 90: 8048-52. PMID 8367461 DOI: 10.1073/Pnas.90.17.8048 |
0.44 |
|
1993 |
Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W. Structure of human des(1-45) factor Xa at 2.2 A resolution. Journal of Molecular Biology. 232: 947-66. PMID 8355279 DOI: 10.1006/Jmbi.1993.1441 |
0.477 |
|
1993 |
Padmanabhan K, Padmanabhan KP, Ferrara JD, Sadler JE, Tulinsky A. The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer. The Journal of Biological Chemistry. 268: 17651-4. PMID 8102368 DOI: 10.2210/Pdb1Hut/Pdb |
0.451 |
|
1992 |
Arni RK, Pal GP, Ravichandran KG, Tulinsky A, Walz FG, Metcalf P. Three-dimensional structure of Gln25-ribonuclease T1 at 1.84-A resolution: structural variations at the base recognition and catalytic sites. Biochemistry. 31: 3126-35. PMID 1554699 DOI: 10.1021/Bi00127A013 |
0.416 |
|
1992 |
Soriano-Garcia M, Padmanabhan K, de Vos AM, Tulinsky A. The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry. 31: 2554-66. PMID 1547238 DOI: 10.1021/Bi00124A016 |
0.357 |
|
1992 |
Nakanishi H, Chrusciel RA, Shen R, Bertenshaw S, Johnson ME, Rydel TJ, Tulinsky A, Kahn M. Peptide mimetics of the thrombin-bound structure of fibrinopeptide A. Proceedings of the National Academy of Sciences of the United States of America. 89: 1705-9. PMID 1542664 |
0.313 |
|
1992 |
Szyperski T, Güntert P, Stone SR, Tulinsky A, Bode W, Huber R, Wüthrich K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51). Journal of Molecular Biology. 228: 1206-11. PMID 1474586 DOI: 10.1016/0022-2836(92)90326-F |
0.458 |
|
1992 |
Qiu X, Padmanabhan KP, Carperos VE, Tulinsky A, Kline T, Maraganore JM, Fenton JW. Structure of the hirulog 3-thrombin complex and nature of the S' subsites of substrates and inhibitors. Biochemistry. 31: 11689-97. PMID 1445905 DOI: 10.1021/Bi00162A004 |
0.485 |
|
1992 |
Hamaguchi N, Charifson P, Darden T, Xiao L, Padmanabhan K, Tulinsky A, Hiskey R, Pedersen L. Molecular dynamics simulation of bovine prothrombin fragment 1 in the presence of calcium ions. Biochemistry. 31: 8840-8. PMID 1390671 DOI: 10.1021/Bi00152A021 |
0.381 |
|
1992 |
Karshikov A, Bode W, Tulinsky A, Stone SR. Electrostatic interactions in the association of proteins: an analysis of the thrombin-hirudin complex. Protein Science : a Publication of the Protein Society. 1: 727-35. PMID 1363935 DOI: 10.1002/Pro.5560010605 |
0.371 |
|
1992 |
de Vos AM, Ultsch MH, Kelley RF, Padmanabhan K, Tulinsky A, Westbrook ML, Kossiakoff AA. Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution. Biochemistry. 31: 270-9. PMID 1310033 DOI: 10.1021/Bi00116A037 |
0.497 |
|
1991 |
Charifson PS, Darden T, Tulinsky A, Hughey JL, Hiskey RG, Pedersen LG. Solution conformations of the gamma-carboxyglutamic acid domain of bovine prothrombin fragment 1, residues 1-65. Proceedings of the National Academy of Sciences of the United States of America. 88: 424-8. PMID 1988943 DOI: 10.1073/Pnas.88.2.424 |
0.405 |
|
1991 |
Skrzypczak-Jankun E, Carperos VE, Ravichandran KG, Tulinsky A, Westbrook M, Maraganore JM. Structure of the hirugen and hirulog 1 complexes of alpha-thrombin. Journal of Molecular Biology. 221: 1379-93. PMID 1942057 DOI: 10.1016/0022-2836(91)90939-4 |
0.517 |
|
1991 |
Rydel TJ, Tulinsky A, Bode W, Huber R. Refined structure of the hirudin-thrombin complex. Journal of Molecular Biology. 221: 583-601. PMID 1920434 DOI: 10.1016/0022-2836(91)80074-5 |
0.515 |
|
1991 |
Seshadri TP, Tulinsky A, Skrzypczak-Jankun E, Park CH. Structure of bovine prothrombin fragment 1 refined at 2.25 A resolution. Journal of Molecular Biology. 220: 481-94. PMID 1856869 DOI: 10.1016/0022-2836(91)90025-2 |
0.428 |
|
1991 |
Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM. The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4. Biochemistry. 30: 10589-94. PMID 1657149 DOI: 10.1021/Bi00107A030 |
0.466 |
|
1991 |
Mulichak AM, Tulinsky A, Ravichandran KG. Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution. Biochemistry. 30: 10576-88. PMID 1657148 DOI: 10.1021/Bi00107A029 |
0.521 |
|
1990 |
Rydel TJ, Ravichandran KG, Tulinsky A, Bode W, Huber R, Roitsch C, Fenton JW. The structure of a complex of recombinant hirudin and human alpha-thrombin. Science (New York, N.Y.). 249: 277-80. PMID 2374926 DOI: 10.1126/Science.2374926 |
0.454 |
|
1990 |
Mulichak AM, Tulinsky A. Structure of the lysine-fibrin binding subsite of human plasminogen kringle 4. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 1: 673-9. PMID 1966798 |
0.435 |
|
1989 |
Soriano-Garcia M, Park CH, Tulinsky A, Ravichandran KG, Skrzypczak-Jankun E. Structure of Ca2+ prothrombin fragment 1 including the conformation of the Gla domain. Biochemistry. 28: 6805-10. PMID 2819034 DOI: 10.1021/Bi00443A004 |
0.429 |
|
1989 |
Skrzypczak-Jankun E, Rydel TJ, Tulinsky A, Fenton JW, Mann KG. Human D-Phe-Pro-Arg-CH2-alpha-thrombin crystallization and diffraction data. Journal of Molecular Biology. 206: 755-7. PMID 2738917 DOI: 10.1016/0022-2836(89)90582-2 |
0.393 |
|
1988 |
Tulinsky A, Park CH, Mao B, Llinás M. Lysine/fibrin binding sites of kringles modeled after the structure of kringle 1 of prothrombin. Proteins. 3: 85-96. PMID 3135547 DOI: 10.1002/Prot.340030203 |
0.453 |
|
1988 |
Tulinsky A, Park CH, Skrzypczak-Jankun E. Structure of prothrombin fragment 1 refined at 2.8 A resolution. Journal of Molecular Biology. 202: 885-901. PMID 2845102 DOI: 10.1016/0022-2836(88)90565-7 |
0.508 |
|
1987 |
Tulinsky A, Blevins RA. Structure of a tetrahedral transition state complex of alpha-chymotrypsin dimer at 1.8-A resolution. The Journal of Biological Chemistry. 262: 7737-43. PMID 3584139 |
0.348 |
|
1987 |
Ramesh V, Petros AM, Llinás M, Tulinsky A, Park CH. Proton magnetic resonance study of lysine-binding to the kringle 4 domain of human plasminogen. The structure of the binding site. Journal of Molecular Biology. 198: 481-98. PMID 2828641 DOI: 10.1016/0022-2836(87)90295-6 |
0.396 |
|
1987 |
Motta A, Laursen RA, Llinás M, Tulinsky A, Park CH. Complete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: structure of the ligand-binding site. Biochemistry. 26: 3827-36. PMID 2820478 DOI: 10.1021/Bi00387A014 |
0.464 |
|
1987 |
Tulinsky A, Park CH, Mao B, Llinas M. Lysine/fibrin binding sites of kringles modelled after the structure of prothrombin fragment 1 Acta Crystallographica Section a Foundations of Crystallography. 43: C29-C29. DOI: 10.1107/S010876738708468X |
0.337 |
|
1986 |
Fillers JP, Ravichandran KG, Abdalmuhdi I, Tulinsky A, Chang CK. Crystal and molecular structure of anthracene and biphenylene pillared cofacial diporphyrins. Journal of the American Chemical Society. 108: 417-24. PMID 22175456 DOI: 10.1002/Chin.198623056 |
0.403 |
|
1986 |
Park CH, Tulinsky A. Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1. Biochemistry. 25: 3977-82. PMID 3741841 DOI: 10.1021/Bi00362A001 |
0.454 |
|
1986 |
Skrzypczak-Jankun E, Tulinsky A, Fillers JP, Kumar KG, Wood HG. Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase. Journal of Molecular Biology. 188: 495-8. PMID 3735431 DOI: 10.1016/0022-2836(86)90172-5 |
0.416 |
|
1985 |
Blevins RA, Tulinsky A. The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution. The Journal of Biological Chemistry. 260: 4264-75. PMID 3980476 |
0.312 |
|
1985 |
Tulinsky A, Park CH, Rydel TJ. The structure of prothrombin fragment 1 at 3.5-A resolution. The Journal of Biological Chemistry. 260: 10771-8. PMID 3839793 |
0.318 |
|
1982 |
Lebioda L, Hatada MH, Tulinsky A, Mavridis IM. Comparison of the folding of 2-keto-3-deoxy-6-phosphogluconate aldolase, triosephosphate isomerase and pyruvate kinase. Implications in molecular evolution. Journal of Molecular Biology. 162: 445-58. PMID 7161802 DOI: 10.1016/0022-2836(82)90537-X |
0.357 |
|
1982 |
Mavridis IM, Hatada MH, Tulinsky A, Lebioda L. Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2 . 8 A resolution. Journal of Molecular Biology. 162: 419-44. PMID 7161801 DOI: 10.1016/0022-2836(82)90536-8 |
0.417 |
|
1981 |
Hatada M, Tulinsky A, Chang C. Additions and Corrections - Crystal and Molecular Structure of Cofacial Dicopper Hexyldiporphyrin-7 Journal of the American Chemical Society. 103: 5623-5623. DOI: 10.1021/Ja00408A601 |
0.404 |
|
1980 |
Martin PD, Tulinsky A, Walz FG. Crystallization of ribonuclease T1. Journal of Molecular Biology. 136: 95-7. PMID 6767852 DOI: 10.1016/0022-2836(80)90368-X |
0.332 |
|
1980 |
Hatada MH, Tulinsky A, Chang CK. Crystal and molecular structure of cofacial dicopper hexyldiporphyrin-7 Journal of the American Chemical Society. 102: 7115-7116. DOI: 10.1021/Ja00543A044 |
0.402 |
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1978 |
Tulinsky A, Mavridis I, Mann RF. Expression of functionality of alpha-chymotrypsin. An alternate binding mode in the substrate specificity site. The Journal of Biological Chemistry. 253: 1074-8. PMID 624719 |
0.366 |
|
1976 |
Mavridis IM, Tulinsky A. The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-A resolution. Biochemistry. 15: 4410-7. PMID 974067 DOI: 10.1021/Bi00665A010 |
0.433 |
|
1976 |
Mavridis A, Tulinsky A. Crystal and molecular structure of dimethoxyporphinatogermanium(IV) Inorganic Chemistry. 15: 2723-2727. DOI: 10.1021/Ic50165A030 |
0.404 |
|
1973 |
Tulinsky A, Wright LH. An X-ray crystallographic investigation of exchange of localized sulfate ions in crystals of alpha-chymotrypsin. Journal of Molecular Biology. 81: 47-56. PMID 4768603 DOI: 10.1016/0022-2836(73)90246-5 |
0.383 |
|
1973 |
Tulinsky A, Vandlen RL, Morimoto CN, Mani NV, Wright LH. Variability in the tertiary structure of alpha-chymotrypsin at 2.8-A resolution. Biochemistry. 12: 4185-92. PMID 4745666 DOI: 10.1021/Bi00745A023 |
0.315 |
|
1967 |
Silvers SJ, Tulinsky A. The crystal and molecular structure of triclinic tetraphenylporphyrin Journal of the American Chemical Society. 89: 3331-3337. PMID 6042769 DOI: 10.1021/Ja00989A036 |
0.402 |
|
1967 |
Baenziger NC, Nelson AD, Tulinsky A, Bloor JH, Popov AI. Two independent determinations of the crystal and molecular structure of the iodine monochloride complex of pentamethylenetetrazole Journal of the American Chemical Society. 89: 6463-6465. DOI: 10.1021/Ja01001A014 |
0.414 |
|
1966 |
Davis RE, Tulinsky A. The x-ray structure determination of thujic acid (7,7-dimethylcycloheptatriene-3-carboxylic acid). Journal of the American Chemical Society. 88: 4583-8. PMID 5918038 DOI: 10.1021/Ja00972A008 |
0.438 |
|
1962 |
Davis RE, Tulinsky A. The structure of thujic acid: 7,7 dimethylcycloheptatriene-3-carboxylic acid Tetrahedron Letters. 3: 839-846. |
0.426 |
|
1958 |
Tulinsky A, White JG. Rigid-body torsional vibrations in three typical members of a class of benzene derivatives Acta Crystallographica. 11: 7-14. DOI: 10.1107/S0365110X58000037 |
0.343 |
|
Low-probability matches (unlikely to be authored by this person) |
1993 |
Guevara J, Jan AY, Knapp R, Tulinsky A, Morrisett JD. Comparison of ligand-binding sites of modeled apo[a] kringle-like sequences in human lipoprotein[a]. Arteriosclerosis and Thrombosis : a Journal of Vascular Biology / American Heart Association. 13: 758-70. PMID 8387333 |
0.3 |
|
1967 |
Schmidt WH, Tulinsky A. The crystal and molecular structure of 2-desylidene-1,3-dithiolane Tetrahedron Letters. 8: 5311-5314. |
0.295 |
|
1980 |
Hatada MH, Tulinsky A, Chang CK. Crystal and molecular structure of cofacial dicopper hexyldiporphyrin-7 [8] Journal of the American Chemical Society. 102: 7115-7116. |
0.295 |
|
1991 |
Watt W, Tulinsky A, Swenson RP, Watenpaugh KD. Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures. Journal of Molecular Biology. 218: 195-208. PMID 2002503 DOI: 10.1016/0022-2836(91)90884-9 |
0.292 |
|
1974 |
Mavridis A, Tulinsky A, Liebman MN. Asymmetrical changes in the tertiary structure of alpha-chymotrypsin with change in pH. Biochemistry. 13: 3661-6. PMID 4850680 DOI: 10.1021/Bi00715A006 |
0.289 |
|
1981 |
Lebioda L, Hatada MH, Mavridis I, Tulinsky A. Comparison of the structures of KDPG aldolase and triose phosphate isomerase Acta Crystallographica Section a Foundations of Crystallography. 37: C43-C43. DOI: 10.1107/S0108767381098310 |
0.279 |
|
1997 |
Castellino F, McCance S, Chang Y, Mochalkin I, Tulinsky A. 159 Structure and ligand binding properties of the kringle 5 domain of human plasminogen Fibrinolysis and Proteolysis. 11: 45. DOI: 10.1016/S0268-9499(97)80275-5 |
0.278 |
|
1997 |
Castellino FJ, McCance SG, Chang Y, Mochalkin I, Tulinsky A. Structure and ligand binding properties of the kringle 5 domain of human plasminogen Fibrinolysis and Proteolysis. 11: 45. |
0.278 |
|
1964 |
Silvers S, Tulinsky A. The Triclinic Crystal Form of α,β,γ,δ-Tetraphenylporphine Journal of the American Chemical Society. 86: 927-928. DOI: 10.1021/Ja01059A040 |
0.275 |
|
1973 |
Tulinsky A. The structure of free base porphine: an average of three independent structures Annals of the New York Academy of Sciences. 206: 47-69. PMID 4518401 |
0.271 |
|
1996 |
Costanzo MJ, Maryanoff BE, Hecker LR, Schott MR, Yabut SC, Zhang HC, Andrade-Gordon P, Kauffman JA, Lewis JM, Krishnan R, Tulinsky A. Potent thrombin inhibitors that probe the S1 subsite: tripeptide transition state analogues based on a heterocycle-activated carbonyl group. Journal of Medicinal Chemistry. 39: 3039-43. PMID 8759623 DOI: 10.1021/Jm9603274 |
0.271 |
|
1992 |
Berkowitz P, Huh NW, Brostrom KE, Panek MG, Weber DJ, Tulinsky A, Pedersen LG, Hiskey RG. A metal ion-binding site in the kringle region of bovine prothrombin fragment 1. The Journal of Biological Chemistry. 267: 4570-6. PMID 1311313 |
0.271 |
|
1989 |
Mulichak AM, Park CH, Tulinsky A, Petros AM, Llinás M. Human plasminogen kringle 4. Crystallization and preliminary diffraction data of two different crystal forms. The Journal of Biological Chemistry. 264: 1922-3. PMID 2914886 |
0.267 |
|
1985 |
Blevins RA, Tulinsky A. Comparison of the independent solvent structures of dimeric alpha-chymotrypsin with themselves and with gamma-chymotrypsin. The Journal of Biological Chemistry. 260: 8865-72. PMID 3894349 |
0.267 |
|
1972 |
Chen BML, Tulinsky A. Redetermination of the structure of porphine Journal of the American Chemical Society. 94: 4144-4151. PMID 5036641 |
0.267 |
|
1969 |
Timkovich R, Tulinsky A. The structure of aquomagnesium tetraphenylporphyrin Journal of the American Chemical Society. 91: 4430-4432. |
0.266 |
|
1962 |
Silvers S, Tulinsky A. The structure of akuammidine Tetrahedron Letters. 3: 339-343. |
0.265 |
|
1962 |
Tulinsky A. The structure of mitomycin A [5] Journal of the American Chemical Society. 84: 3188-3190. |
0.263 |
|
1962 |
Tulinsky A. The Structure of Mitomycin A″ Journal of the American Chemical Society. 84: 3188-3190. DOI: 10.1021/ja00875a034 |
0.263 |
|
1967 |
Tulinsky A, Van Den Hende JH. The crystal and molecular structure of N-brosylmitomycin A Journal of the American Chemical Society. 89: 2905-2911. PMID 6043811 |
0.261 |
|
1975 |
Pinnavaia TJ, Barnett BL, Podolsky G, Tulinsky A. Crystal and molecular structure of tetrakis(2,2,6,6-tetramethyl-3,5-heptanedionato)niobium(IV). Square antiprismatic M(bidentate)4 stereoisomer Journal of the American Chemical Society. 97: 2712-2717. DOI: 10.1021/ja00843a021 |
0.256 |
|
1975 |
Pinnavaia TJ, Barnett BL, Podolsky G, Tulinsky A. Crystal and molecular structure of tetrakis-(2,2,6,6-tetramethyl-3,5-heptanedionato)niobium(IV). A square antiprismatic M(bidentate)4 stereoisomer Journal of the American Chemical Society. 97: 2712-2717. |
0.256 |
|
1972 |
Codding PW, Tulinsky A. Structure of tetra-n-propylporphine. An average structure for the free base macrocycle from three independent determinations Journal of the American Chemical Society. 94: 4151-4157. PMID 5036642 |
0.254 |
|
1991 |
Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM. The refined structure of the ∈-aminocaproic acid complex of human plasminogen kringle 4 Biochemistry. 30: 10589-10594. |
0.252 |
|
1981 |
Frentrup MA, Tulinsky A. Comparison of the independent structures of α-chymotrypsin dimer at 1.8 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 37: C42-C42. DOI: 10.1107/S0108767381098322 |
0.248 |
|
1973 |
Vandlen RL, Tulinsky A. Changes in the tertiary structure of α-chymotrypsin with change in pH; pH 4.2-6.7 Biochemistry. 12: 4193-4200. PMID 4745667 DOI: 10.1021/Bi00745A024 |
0.248 |
|
1988 |
Rodríguez A, Tablero M, Arreguín B, Hernández A, Arreguín R, Soriano-García M, Tulinsky A, Park CH, Seshadri TP. Preliminary x-ray investigation of an orthorhombic crystal of hevein. The Journal of Biological Chemistry. 263: 4047-8. PMID 3346234 |
0.246 |
|
1981 |
Gaier JR, Tulinsky A, Liener IE. Formation, crystallization, and preliminary crystallographic data of the ternary complex of alpha-chymotrypsin, beta-trypsin, and the Bowman-Birk inhibitor. The Journal of Biological Chemistry. 256: 11417-9. PMID 7298611 |
0.245 |
|
1977 |
Tulinsky A, Chen BM. The crystal and molecular structure of chloro-alpha,beta,gamma,delta-tetraphenylporphinatomanganese(III). Journal of the American Chemical Society. 99: 3647-51. PMID 858872 |
0.245 |
|
1979 |
Raghavan NV, Tulinsky A. The structure of α-chymotrypsin. II. Fourier phase refinement and extension of the dimeric structure at 1.8 Å resolution by density modification Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 35: 1776-1785. DOI: 10.1107/S0567740879007767 |
0.243 |
|
1980 |
Kung WH, Tulinsky A, Nelsestuen GL. Crystallization and preliminary X-ray data of proteins derived from prothrombin. The Journal of Biological Chemistry. 255: 10523-5. PMID 7430133 |
0.241 |
|
1993 |
Wu TP, Yee V, Tulinsky A, Chrusciel RA, Nakanishi H, Shen R, Priebe C, Kahn M. The structure of a designed peptidomimetic inhibitor complex of alpha-thrombin. Protein Engineering. 6: 471-8. PMID 8415574 |
0.224 |
|
1979 |
Johnson JD, El-Bayoumi MA, Weber LD, Tulinsky A. Interaction of alpha-chymotrypsin with the fluorescent probe 1-anilinonaphthalene-8-sulfonate in solution. Biochemistry. 18: 1292-6. PMID 427115 |
0.223 |
|
1996 |
Bajaj SP, Matthews II, Matthews JH, Tulinsky A. Low-temperature structure of the thrombin–hirugen complex at 1.7 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 52: C9-C9. DOI: 10.1107/S0108767396098625 |
0.218 |
|
1993 |
Guevara J, Spurlino J, Jan AY, Yang CY, Tulinsky A, Prasad BV, Gaubatz JW, Morrisett JD. Proposed mechanisms for binding of apo[a] kringle type 9 to apo B-100 in human lipoprotein[a]. Biophysical Journal. 64: 686-700. PMID 8386013 DOI: 10.1016/S0006-3495(93)81428-0 |
0.213 |
|
1988 |
Mulichak AM, Skrzypczak-Jankun E, Rydel TJ, Tulinsky A, Preiss J. Crystallization and preliminary diffraction data of Escherichia coli ADP glucose pyrophosphorylase. The Journal of Biological Chemistry. 263: 17237-8. PMID 2846559 |
0.209 |
|
1964 |
Silvers S, Tulinsky A. The triclinic crystal form of αβ,γ,δ-tetraphenylporphine [2] Journal of the American Chemical Society. 86: 927-928. |
0.208 |
|
1977 |
TULINSKY A, CHEN BML. ChemInform Abstract: THE CRYSTAL AND MOLECULAR STRUCTURE OF CHLORO-α,β,Γ,Δ-TETRAPHENYLPORPHINATOMANGANESE(III) Chemischer Informationsdienst. 8: no-no. DOI: 10.1002/chin.197733077 |
0.207 |
|
1973 |
Tulinsky A, Vandlen RL, Morimoto CN, Venkit Mani N, Wright LH. Variability in the tertiary structure of α-chymotrypsin at 2.8-Å resolution Biochemistry. 12: 4185-4192. |
0.204 |
|
1964 |
Tulinsky A. The structure of isoquinocycline A. An x-ray crystallographic determination [34] Journal of the American Chemical Society. 86: 5368-5369. |
0.202 |
|
1984 |
Tulinsky A, Blevins RA. Restrained least-squares refinement of chymotrypsin dimer at 1.65 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 40: C17-C17. DOI: 10.1107/S0108767384099323 |
0.201 |
|
1973 |
Tulinsky A, Mani NV, Morimoto CN, Vandlen RL. The structure of α-chymotrypsin. I. The refinement of the heavy-atom isomorphous derivatives at 2.8 Å resolution Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 29: 1309-1322. DOI: 10.1107/S0567740873004437 |
0.201 |
|
1983 |
Chang CK, Hatada MH, Tulinsky A. Synthesis and molecular structure of formylporphyrin. Intrinsic properties of porphyrin a Journal of the Chemical Society, Perkin Transactions 2. 371-378. DOI: 10.1039/P29830000371 |
0.19 |
|
1990 |
Collen D, Lijnen HR, Bulens F, Vandamme AM, Tulinsky A, Nelles L. Biochemical and functional characterization of human tissue-type plasminogen activator variants with mutagenized kringle domains. The Journal of Biological Chemistry. 265: 12184-91. PMID 2115513 |
0.188 |
|
1959 |
Tulinsky A, Worthington CR. Basic beryllium acetate. II. The structure analysis Acta Crystallographica. 12: 626-634. DOI: 10.1107/S0365110X59001864 |
0.187 |
|
1996 |
Tulinsky A. Chapter 35. The Protein Structure Project, 1950-1959: First Concerted Effort of a Protein Structure Determination in the U.S. Annual Reports in Medicinal Chemistry. 31: 357-366. DOI: 10.1016/S0065-7743(08)60474-1 |
0.186 |
|
1991 |
Tulinsky A. The structures of domains of blood proteins. Thrombosis and Haemostasis. 66: 16-31. PMID 1926046 |
0.185 |
|
1981 |
Frentrup MA, Tulinsky A. A precise and accurate method of measuring Kendrew model coordinates Journal of Applied Crystallography. 14: 439-443. DOI: 10.1107/S0021889881009722 |
0.17 |
|
1973 |
Moustakali I, Tulinsky A. Structure of Copper (II) n-propylporphine. Effect of a metallo substitution on the free base macrocycle. Journal of the American Chemical Society. 95: 6811-5. PMID 4746277 DOI: 10.1021/ja00801a047 |
0.162 |
|
1973 |
MOUSTAKALI I, TULINSKY A. ChemInform Abstract: STRUCTURE OF COPPER(II) N-PROPYLPORPHINE, EFFECT OF A METALLO SUBSTITUTION ON THE FREE BASE MACROCYCLE Chemischer Informationsdienst. 4: no-no. DOI: 10.1002/chin.197349415 |
0.16 |
|
1979 |
Weber LD, Tulinsky A, Johnson JD, El-Bayoumi MA. Expression of functionality of alpha-chymotrypsin. The structure of a fluorescent probe--alpha-chymotrypsin complex and the nature of its pH dependence. Biochemistry. 18: 1297-303. PMID 34424 |
0.15 |
|
1986 |
Tulinsky A, Blevins RA. Least‐squares refinement of two protein molecules per asymmetric unit with and without non‐crystallographic symmetry restrained Acta Crystallographica Section B. 42: 198-200. DOI: 10.1107/S010876818609835X |
0.148 |
|
1980 |
Weber LD, Tulinsky A. The monoclinic structure of a fluorescent probe: ammonium 1-anilino-8-naphthalenesulfonate (ANS) monohydrate Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 36: 611-614. DOI: 10.1107/S0567740880003913 |
0.145 |
|
1971 |
Vandlen RL, Tulinsky A. Automatic crystal alignment and intensity data collection with a computer controlled diffractometer Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 27: 437-442. DOI: 10.1107/S0567740871002346 |
0.142 |
|
1973 |
Vandlen RL, Ersfeld DL, Tulinsky A, Wood WA. Confirmation of a trimeric subunit arrangement for 2-keto-3-deoxy-6-phosphogluconic aldolase using x-ray crystallographic methods Journal of Biological Chemistry. 248: 2251-2253. PMID 4690603 |
0.138 |
|
1996 |
Levy OE, Semple JE, Lim ML, Reiner J, Rote WE, Dempsey E, Richard BM, Zhang E, Tulinsky A, Ripka WC, Nutt RF. Potent and selective thrombin inhibitors incorporating the constrained arginine mimic l-3-piperidyl(N-guanidino)alanine at P1. Journal of Medicinal Chemistry. 39: 4527-30. PMID 8917638 DOI: 10.1021/jm960607j |
0.103 |
|
1959 |
Tulinsky A. Basic beryllium acetate. III. Evidence for chemical bonding; assessment of accuracy Acta Crystallographica. 12: 634-637. DOI: 10.1107/S0365110X59001876 |
0.096 |
|
1983 |
Lebioda L, Hatada MH, Tulinsky A. A rapid and precise method of measuring Kendrew-model coordinates with theodolites Journal of Applied Crystallography. 16: 270-273. DOI: 10.1107/S0021889883010365 |
0.09 |
|
1996 |
Semple JE, Rowley DC, Brunck TK, Ha-Uong T, Minami NK, Owens TD, Tamura SY, Goldman EA, Siev DV, Ardecky RJ, Carpenter SH, Ge Y, Richard BM, Nolan TG, HÃ¥kanson K, ... Tulinsky A, et al. Design, synthesis, and evolution of a novel, selective, and orally bioavailable class of thrombin inhibitors: P1-argininal derivatives incorporating P3-P4 lactam sulfonamide moieties. Journal of Medicinal Chemistry. 39: 4531-6. PMID 8917639 DOI: 10.1021/jm960572n |
0.088 |
|
1978 |
Hibbard LS, Tulinsky A. Expression of functionality of alpha-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation. Biochemistry. 17: 5460-8. PMID 728409 |
0.078 |
|
1985 |
Tulinsky A. Diffraction methods for biologic macromolecules. Phase refinement/extension by density modification. Methods in Enzymology. 115: 77-89. PMID 4079799 |
0.073 |
|
1977 |
Timkovich R, Tulinsky A. Coordination and geometry of gold in chloro(α,β,γ,δ-tetraphenylporphinato)gold(III) Inorganic Chemistry. 16: 962-963. |
0.067 |
|
1972 |
CODDING PW, TULINSKY A. ChemInform Abstract: STRUKTUR VON TETRA-N-PROPYL-PORPHIN, GEMITTELTE STRUKTUR FUER DEN MAKRORING DER FREIEN BASE AUS DREI UNABHAENGIGEN BESTIMMUNGEN Chemischer Informationsdienst. 3. DOI: 10.1002/chin.197235106 |
0.05 |
|
1972 |
CHEN BML, TULINSKY A. ChemInform Abstract: NEUBESTIMMUNG DER STRUKTUR VON PORPHIN Chemischer Informationsdienst. 3. DOI: 10.1002/chin.197235105 |
0.037 |
|
1963 |
Tulinsky A. Direct Analysis of Differaction by Matter. Journal of the American Chemical Society. 85: 1368-1368. DOI: 10.1021/ja00892a052 |
0.035 |
|
1985 |
Tulinsky A. Phase refinement/extension by density modification Methods in Enzymology. 115: 77-89. DOI: 10.1016/0076-6879(85)15008-1 |
0.033 |
|
1959 |
Tulinsky A, Worthington CR, Pignataro F. Basic beryllium acetate. I. The collection of intensity data Acta Crystallographica. 12: 623-626. DOI: 10.1107/S0365110X59001852 |
0.029 |
|
Hide low-probability matches. |