메뉴 건너뛰기




Volumn 7, Issue 2, 1998, Pages 243-253

Hirunorms are true hirudin mimetics. The crystal structure of human α- thrombin-hirunorm V complex

Author keywords

Antithrombotics; Hirudin like binding mode; Hirunorms; Thrombin; Thrombin synthetic inhibitors; X ray crystal structure

Indexed keywords

HIRUDIN; HIRUNORM; HIRUNORM V; THROMBIN; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0031890648     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070203     Document Type: Article
Times cited : (21)

References (73)
  • 2
    • 0028821302 scopus 로고
    • Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: Structural functional and biomedical aspects
    • Ascenzi P, Amiconi G, Bode W, Bolognesi M, Coletta M, Menegatti E. 1995. Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: Structural functional and biomedical aspects. Mol Aspects Med 16:215-313.
    • (1995) Mol Aspects Med , vol.16 , pp. 215-313
    • Ascenzi, P.1    Amiconi, G.2    Bode, W.3    Bolognesi, M.4    Coletta, M.5    Menegatti, E.6
  • 3
    • 0025837452 scopus 로고
    • Crystallographic analysis at 30 Å resolution of the binding to human thrombin of four active site-directed inhibitors
    • Banner DW, Hadvary P. 1991. Crystallographic analysis at 30 Å resolution of the binding to human thrombin of four active site-directed inhibitors. J Biol Chem 266:20085-20093.
    • (1991) J Biol Chem , vol.266 , pp. 20085-20093
    • Banner, D.W.1    Hadvary, P.2
  • 7
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W, Huber R. 1992. Natural protein proteinase inhibitors and their interaction with proteinases. Eur J Biochem 204:443-452.
    • (1992) Eur J Biochem , vol.204 , pp. 443-452
    • Bode, W.1    Huber, R.2
  • 8
    • 0002987063 scopus 로고
    • X-ray crystal structures of human α-thrombin and of human thrombin-hirudin complex
    • Berliner LJ, ed. New York: Plenum Press
    • Bode W, Huber R, Rydel TJ, Tulinsky A. 1992a. X-ray crystal structures of human α-thrombin and of human thrombin-hirudin complex. In: Berliner LJ, ed. Thrombin structure and function. New York: Plenum Press.
    • (1992) Thrombin Structure and Function
    • Bode, W.1    Huber, R.2    Rydel, T.J.3    Tulinsky, A.4
  • 9
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. 1989. The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 8:3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 10
    • 0027050807 scopus 로고
    • The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W, Turk D, Karshikov A. 1992b. The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1:426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 11
    • 0026465007 scopus 로고
    • Refined 2.3 Å X-ray crystal structure of bovine trombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP 4-TAPAP and MQPA
    • Brandstetter H, Turk D, Hoeffken HW, Grosse D, Stürzebecher J, Martin PD, Edwards BFP, Bode W. 1992. Refined 2.3 Å X-ray crystal structure of bovine trombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP 4-TAPAP and MQPA. J Mol Biol 226:1085-1099.
    • (1992) J Mol Biol , vol.226 , pp. 1085-1099
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3    Grosse, D.4    Stürzebecher, J.5    Martin, P.D.6    Edwards, B.F.P.7    Bode, W.8
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. 1994. The CCP4 suite: Programs for protein crystallography Acta Crystallogr D 50:760-767.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-767
  • 13
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation maintenance and regulation
    • Davie EW, Fujikawa K, Kisiel W. 1991. The coagulation cascade: Initiation maintenance and regulation. Biochemistry 30: 10364-10370.
    • (1991) Biochemistry , vol.30 , pp. 10364-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 14
    • 0025906031 scopus 로고
    • A new class of potent thrombin inhibitors that incorporates a scissile pseudopeptide bond
    • DiMaio J, Gibb B, Munn D, Lefebre J, Ni F, Konishi Y. 1991. A new class of potent thrombin inhibitors that incorporates a scissile pseudopeptide bond. FEBS Lett 282:47-52.
    • (1991) FEBS Lett , vol.282 , pp. 47-52
    • DiMaio, J.1    Gibb, B.2    Munn, D.3    Lefebre, J.4    Ni, F.5    Konishi, Y.6
  • 15
    • 0026731584 scopus 로고
    • Synthesis of a homogeneous series of ketomethylene arginyl pseudopeptides and application to low molecular weight hirudin-like thrombin inhibitors
    • DiMaio J, Gibb B, Lefebre J, Konishi Y, Munn D, Yue SY. 1992. Synthesis of a homogeneous series of ketomethylene arginyl pseudopeptides and application to low molecular weight hirudin-like thrombin inhibitors. J Med Chem 35:3331-3341.
    • (1992) J Med Chem , vol.35 , pp. 3331-3341
    • DiMaio, J.1    Gibb, B.2    Lefebre, J.3    Konishi, Y.4    Munn, D.5    Yue, S.Y.6
  • 16
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 47:392-400.
    • (1991) Acta Crystallogr A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 20
    • 0026102830 scopus 로고
    • Thrombin structure and function: Why thrombin is the primary target for antithrombotics
    • Fenton JW II, Ofosu FA, Moon DG, Maraganore JM. 1991. Thrombin structure and function: Why thrombin is the primary target for antithrombotics. Blood Coag Fibrinol 2:69-75.
    • (1991) Blood Coag Fibrinol , vol.2 , pp. 69-75
    • Fenton II, J.W.1    Ofosu, F.A.2    Moon, D.G.3    Maraganore, J.M.4
  • 21
    • 0023770729 scopus 로고
    • Anion binding exosite of human α-thrombin and fibrinogen recognition
    • Fenton JW II, Olson TA, Zabinski MP, Wilner GD. 1988. Anion binding exosite of human α-thrombin and fibrinogen recognition. Biochemistry 27:7106-7112.
    • (1988) Biochemistry , vol.27 , pp. 7106-7112
    • Fenton II, J.W.1    Olson, T.A.2    Zabinski, M.P.3    Wilner, G.D.4
  • 22
    • 0029896898 scopus 로고    scopus 로고
    • Crystal structure of two new bifunctional nonsubstrate type thrombin inhibitors complexed with human α-thrombin
    • Féthière J, Tsuda Y, Coulombe R, Konishi Y, Cygler M. 1996. Crystal structure of two new bifunctional nonsubstrate type thrombin inhibitors complexed with human α-thrombin. Protein Sci 5:1174-1183.
    • (1996) Protein Sci , vol.5 , pp. 1174-1183
    • Féthière, J.1    Tsuda, Y.2    Coulombe, R.3    Konishi, Y.4    Cygler, M.5
  • 24
    • 0028276982 scopus 로고
    • Retro-binding tripeptide thrombin active-site inhibitors: Discovery synthesis and molecular modeling
    • Iwanowicz E, J Lau WF, Lin J, Roberts DGM, Seiler SM. 1994. Retro-binding tripeptide thrombin active-site inhibitors: Discovery synthesis and molecular modeling. J Med Chem 37:2122-2124.
    • (1994) J Med Chem , vol.37 , pp. 2122-2124
    • Iwanowicz, E.J.1    Lau, W.F.2    Lin, J.3    Roberts, D.G.M.4    Seiler, S.M.5
  • 25
    • 0025174706 scopus 로고
    • Inhibition of coagulation and thrombin induced platelet activities by a synthetic dodecapeptide modeled on the carboxy terminus of hirudin
    • Jakubowski JA, Maraganore JM. 1990. Inhibition of coagulation and thrombin induced platelet activities by a synthetic dodecapeptide modeled on the carboxy terminus of hirudin. Blood 75:399-406.
    • (1990) Blood , vol.75 , pp. 399-406
    • Jakubowski, J.A.1    Maraganore, J.M.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones TA, Zou JY, Cowan S, Kieldgaard M. 1991. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kieldgaard, M.4
  • 27
    • 0021327417 scopus 로고
    • Selective inhibition of thrombin by 2R,4R-4-methyl-1-N2-[3-methyl-1,2,3,4-tetrahydro-8-quinolinyl sulphonyl-L-arginyl]-2-piperidine-carboxylic
    • Kikumoto R, Tamao Y, Tezuka T, Tonomura S, Hara N, Ninomiya K, Hijikata A, Okamoto S. 1984. Selective inhibition of thrombin by 2R,4R-4-methyl-1-N2-[3-methyl-1,2,3,4-tetrahydro-8-quinolinyl sulphonyl-L-arginyl]-2-piperidine-carboxylic. Biochemistry 23:85-89.
    • (1984) Biochemistry , vol.23 , pp. 85-89
    • Kikumoto, R.1    Tamao, Y.2    Tezuka, T.3    Tonomura, S.4    Hara, N.5    Ninomiya, K.6    Hijikata, A.7    Okamoto, S.8
  • 28
    • 0025823257 scopus 로고
    • Hirulog peptides with scissile bond replacements resistant to thrombin cleavage
    • Kline T, Hammond C, Bourdan P, Maraganore J. 1991. Hirulog peptides with scissile bond replacements resistant to thrombin cleavage. Biochem Biophys Res Commun 177:1049-1055.
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 1049-1055
    • Kline, T.1    Hammond, C.2    Bourdan, P.3    Maraganore, J.4
  • 29
    • 0029879577 scopus 로고    scopus 로고
    • Synthesis structure and structure-activity relationships of divalent thrombin inhibitors containing an α-keto-amide transition state mimetic
    • Krishnan R, Tulinsky A, Vlasuk GP, Pearson D, Vallar P, Bergum P, Brunck TK, Ripka WC. 1996. Synthesis structure and structure-activity relationships of divalent thrombin inhibitors containing an α-keto-amide transition state mimetic. Protein Sci 5:422-433.
    • (1996) Protein Sci , vol.5 , pp. 422-433
    • Krishnan, R.1    Tulinsky, A.2    Vlasuk, G.P.3    Pearson, D.4    Vallar, P.5    Bergum, P.6    Brunck, T.K.7    Ripka, W.C.8
  • 30
    • 0025240978 scopus 로고
    • Development of MDL 28050 a small antithrombin agent based on a functional domain of the leech protein hirudin
    • Krstenansky JL, Broersma RJ, Owen TJ, Payne MH, Yates MT, Mao SJ. 1990a. Development of MDL 28050 a small antithrombin agent based on a functional domain of the leech protein hirudin. Thromb Haemostasis 63:208-214.
    • (1990) Thromb Haemostasis , vol.63 , pp. 208-214
    • Krstenansky, J.L.1    Broersma, R.J.2    Owen, T.J.3    Payne, M.H.4    Yates, M.T.5    Mao, S.J.6
  • 32
    • 0023203870 scopus 로고
    • Anticoagulant peptides: Nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site of thrombin
    • Krstenansky JL, Owen TJ, Yates MT, Mao SJT. 1987. Anticoagulant peptides: Nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site of thrombin. J Med Chem 30:1688-1691.
    • (1987) J Med Chem , vol.30 , pp. 1688-1691
    • Krstenansky, J.L.1    Owen, T.J.2    Yates, M.T.3    Mao, S.J.T.4
  • 33
    • 0023723033 scopus 로고
    • Design synthesis and antithrombin activity for conformationally restricted analogs of peptide anticoagulants based on the C-terminal region of the leech peptide hirudin
    • Krstenansky JL, Owen TJ, Yates MT, Mao SJT. 1988. Design synthesis and antithrombin activity for conformationally restricted analogs of peptide anticoagulants based on the C-terminal region of the leech peptide hirudin. Biochim Biophys Acta 957:53-59.
    • (1988) Biochim Biophys Acta , vol.957 , pp. 53-59
    • Krstenansky, J.L.1    Owen, T.J.2    Yates, M.T.3    Mao, S.J.T.4
  • 34
    • 0025091511 scopus 로고
    • The C-terminal binding domain of hirullin P18 antithrombic activity and comparison to hirudin peptides
    • Krstenansky JL, Owen TJ, Yates MT, Mao SJT. 1990b. The C-terminal binding domain of hirullin P18 antithrombic activity and comparison to hirudin peptides. FEBS Lett 269:425-429.
    • (1990) FEBS Lett , vol.269 , pp. 425-429
    • Krstenansky, J.L.1    Owen, T.J.2    Yates, M.T.3    Mao, S.J.T.4
  • 35
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M, Kato I. 1980. Protein inhibitors of proteinases. Annu Rev Biochem 49:593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 37
    • 0029984910 scopus 로고    scopus 로고
    • Rational design of true hirudin mimetics: Synthesis and characterization of multisite-directed α-thrombin inhibitors
    • Lombardi A, Nastri F, Della Morte R, Rossi A, De Rosa A, Staiano N, Pedone C, Pavone V. 1996. Rational design of true hirudin mimetics: Synthesis and characterization of multisite-directed α-thrombin inhibitors. J Med Chem 39:2008-2017.
    • (1996) J Med Chem , vol.39 , pp. 2008-2017
    • Lombardi, A.1    Nastri, F.2    Della Morte, R.3    Rossi, A.4    De Rosa, A.5    Staiano, N.6    Pedone, C.7    Pavone, V.8
  • 38
    • 0030040580 scopus 로고    scopus 로고
    • Crystallographic determination of the structures of human α-thrombin complexed with BMS-186282 and BMS-189090
    • Malley MF, Tabernero L, Chang CY, Ohringer SL, Roberts DGM, Das J, Sack JS. 1996. Crystallographic determination of the structures of human α-thrombin complexed with BMS-186282 and BMS-189090. Protein Sci 5:221-228.
    • (1996) Protein Sci , vol.5 , pp. 221-228
    • Malley, M.F.1    Tabernero, L.2    Chang, C.Y.3    Ohringer, S.L.4    Roberts, D.G.M.5    Das, J.6    Sack, J.S.7
  • 39
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • Maraganore JM, Bourdon P, Jablonski J, Ramachandran KL, Fenton JWII. 1990. Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin. Biochemistry 29:7095-7101.
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, J.3    Ramachandran, K.L.4    Fenton II, J.W.5
  • 40
    • 0027968823 scopus 로고
    • The development of hirudin as an antithrombotic drug
    • Markwardt F. 1994. The development of hirudin as an antithrombotic drug. Thrombosis Res 74:1-23.
    • (1994) Thrombosis Res , vol.74 , pp. 1-23
    • Markwardt, F.1
  • 42
    • 0028209977 scopus 로고
    • Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes
    • Mathews II, Padmanabhan KP, Ganesh V, Tulinsky A, Isshii M, Chen J, Turck CW, Coughlin SR. 1994. Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes. Biochemistry 33:3266-3279.
    • (1994) Biochemistry , vol.33 , pp. 3266-3279
    • Mathews, I.I.1    Padmanabhan, K.P.2    Ganesh, V.3    Tulinsky, A.4    Isshii, M.5    Chen, J.6    Turck, C.W.7    Coughlin, S.R.8
  • 46
    • 0027366387 scopus 로고
    • Changes in interaction in complexes of hirudin derivatives and human α-thrombin due to different crystal forms
    • Priestle JP, Rahuel J, Rink H, Tones M, Grütter MG. 1993. Changes in interaction in complexes of hirudin derivatives and human α-thrombin due to different crystal forms. Protein Sci 2:1630-1642.
    • (1993) Protein Sci , vol.2 , pp. 1630-1642
    • Priestle, J.P.1    Rahuel, J.2    Rink, H.3    Tones, M.4    Grütter, M.G.5
  • 48
    • 0027218963 scopus 로고
    • Structures of thrombin complexes with a designed and a natural exosite peptide inhibitor
    • Qiu X, Yin M, Padmanabhan KP, Krstenansky JL, Tulinsky A. 1993. Structures of thrombin complexes with a designed and a natural exosite peptide inhibitor. J Biol Chem 268:20318-20326.
    • (1993) J Biol Chem , vol.268 , pp. 20318-20326
    • Qiu, X.1    Yin, M.2    Padmanabhan, K.P.3    Krstenansky, J.L.4    Tulinsky, A.5
  • 50
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel TJ, Tulinsky A, Bode W, Huber R. 1991. Refined structure of the hirudin-thrombin complex. J Mol Biol 221:583-601.
    • (1991) J Mol Biol , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 51
    • 0031569368 scopus 로고    scopus 로고
    • Serendipity meets precision: The integration of structure-based drug design and combinatorial chemistry for efficient drug discovery
    • Salemme FR, Spurlino J, Bone R. 1997. Serendipity meets precision: The integration of structure-based drug design and combinatorial chemistry for efficient drug discovery. Structure 5:319-324.
    • (1997) Structure , vol.5 , pp. 319-324
    • Salemme, F.R.1    Spurlino, J.2    Bone, R.3
  • 52
    • 0014211618 scopus 로고
    • On the size of the active site in proteinases I papain
    • Schechter I, Berger A. 1967. On the size of the active site in proteinases I papain. Biochem Biophys Res Commun 27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 54
    • 0022521744 scopus 로고
    • Kinetic of the inhibition of thrombin by hirudin
    • Stone SR, Hofsteengc J. 1986. Kinetic of the inhibition of thrombin by hirudin. Biochemistry 25:4622-4628.
    • (1986) Biochemistry , vol.25 , pp. 4622-4628
    • Stone, S.R.1    Hofsteengc, J.2
  • 55
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs MT, Bode W. 1993. A player of many parts: The spotlight falls on thrombin's structure. Thromb Res 69:1-58.
    • (1993) Thromb Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 56
    • 0029083512 scopus 로고
    • Structure and specificity in coagulation and its inhibition
    • Stubbs MT, Bode W. 1995. Structure and specificity in coagulation and its inhibition. Trends Cardiovasc Med 5:157-166.
    • (1995) Trends Cardiovasc Med , vol.5 , pp. 157-166
    • Stubbs, M.T.1    Bode, W.2
  • 59
    • 0021670934 scopus 로고
    • Inhibition of bovine and human thrombins by derivatives of benzamidines
    • Stürzebecher J, Markwardt F, Voigt B, Wagner G. 1984. Inhibition of bovine and human thrombins by derivatives of benzamidines. Thromb Res 36:457-467.
    • (1984) Thromb Res , vol.36 , pp. 457-467
    • Stürzebecher, J.1    Markwardt, F.2    Voigt, B.3    Wagner, G.4
  • 60
    • 0020527888 scopus 로고
    • Cyclic amides of Na-arylsulfonylamino acylated 4-amidinophenylalanine - Tight binding of thrombin
    • Stürzebecher J, Markwardt F, Voigt B, Wagner G, Walsmann P. 1983. Cyclic amides of Na-arylsulfonylamino acylated 4-amidinophenylalanine - Tight binding of thrombin. Thromb Res 29:635-642.
    • (1983) Thromb Res , vol.29 , pp. 635-642
    • Stürzebecher, J.1    Markwardt, F.2    Voigt, B.3    Wagner, G.4    Walsmann, P.5
  • 61
    • 0027298337 scopus 로고
    • Design of a linker for trivalent thrombin inhibitors: Interaction of the main chain of the linker with thrombin
    • Szewczuk Z, Gibbs BF, Yue SY, Purisima E, Zdanov A, Cygler M, Konishi Y. 1993. Design of a linker for trivalent thrombin inhibitors: Interaction of the main chain of the linker with thrombin. Biochemistry 32:3396-3404.
    • (1993) Biochemistry , vol.32 , pp. 3396-3404
    • Szewczuk, Z.1    Gibbs, B.F.2    Yue, S.Y.3    Purisima, E.4    Zdanov, A.5    Cygler, M.6    Konishi, Y.7
  • 63
    • 0016212942 scopus 로고
    • The binding of thrombin to the surface of human platelets
    • Tollefsen DM, Feagler JR, Majerus PW. 1974. The binding of thrombin to the surface of human platelets. J Biol Chem 249:2646-2651.
    • (1974) J Biol Chem , vol.249 , pp. 2646-2651
    • Tollefsen, D.M.1    Feagler, J.R.2    Majerus, P.W.3
  • 64
    • 84913050729 scopus 로고
    • An efficient general purpose least squares refinement program for macromolecular structures
    • Tronrud D, TenEyck LF, Matthews BW. 1987. An efficient general purpose least squares refinement program for macromolecular structures. Acta Crystallogr A 34:489-501.
    • (1987) Acta Crystallogr A , vol.34 , pp. 489-501
    • Tronrud, D.1    TenEyck, L.F.2    Matthews, B.W.3
  • 65
    • 0028559927 scopus 로고
    • Design of potent bivalent thrombin inhibitors based on hirudin sequence: Incorporation of nonsubstrate-type active site inhibitors
    • Tsuda Y, Cygler M, Gibbs BF, Pedyczac A, Féthière J, Vue SY, Konishi Y. 1994. Design of potent bivalent thrombin inhibitors based on hirudin sequence: Incorporation of nonsubstrate-type active site inhibitors. Biochemistry 33:14443-14451.
    • (1994) Biochemistry , vol.33 , pp. 14443-14451
    • Tsuda, Y.1    Cygler, M.2    Gibbs, B.F.3    Pedyczac, A.4    Féthière, J.5    Vue, S.Y.6    Konishi, Y.7
  • 67
    • 0028784163 scopus 로고
    • Two heads are heiter than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht A, Lamba D, Bauer M, Huber R, Friedrich T, Kröger B, Höffken W, Bode W. 1995. Two heads are heiter than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 14:5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • Van De Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kröger, B.6    Höffken, W.7    Bode, W.8
  • 69
    • 0028586082 scopus 로고
    • The isomorphous structure of prethrombin 2 hirugen- and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin
    • Vijayalakshmi J, Padmanabhan KP, Mann KG, Tulinsky A. 1994. The isomorphous structure of prethrombin 2 hirugen- and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin. Protein Sci 3:2254-2271.
    • (1994) Protein Sci , vol.3 , pp. 2254-2271
    • Vijayalakshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.