메뉴 건너뛰기




Volumn 23, Issue 6, 2014, Pages 833-842

Crystal structure of the nucleotide-Binding domain of mortalin, the mitochondrial Hsp70 chaperone

Author keywords

Chaperone inhibitor; Heat Shock protein 70; Mitochondria; Nucleotide binding; P53; Protein quality control

Indexed keywords

1 ETHYL 2 [[3 ETHYL 5 (3 METHYLBENZOTHIAZOLIN 2 YLIDENE) 4 OXOTHIAZOLIDIN 2 YLIDENE]METHYL]PYRIDINIUM CHLORIDE; CHAPERONE; GUANINE NUCLEOTIDE BINDING PROTEIN; HEAT SHOCK PROTEIN 70; MITOCHONDRIAL PROTEIN; MORTALIN; NUCLEOTIDE; NUCLEOTIDE EXCHANGE FACTOR GRPEL1; PROTEIN P53; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 84904261221     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2466     Document Type: Article
Times cited : (37)

References (71)
  • 1
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B (2005) Hsp70 chaperones: Cellular functions and molecular mechanism. Cell Mol Life Sci 62:670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 2
    • 34447528828 scopus 로고    scopus 로고
    • The heat-Shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • Daugaard MM, Rohde MM, Jäättel̈a MM (2007) The heat-Shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett 581:3702-3710.
    • (2007) FEBS Lett , vol.581 , pp. 3702-3710
    • Daugaard, M.M.1    Rohde, M.M.2    Jäättel̈a, M.M.3
  • 3
    • 0027414085 scopus 로고
    • Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype
    • Wadhwa R, Kaul SC, Ikawa Y, Sugimoto Y (1993) Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype. J Biol Chem 268:6615-6621.
    • (1993) J Biol Chem , vol.268 , pp. 6615-6621
    • Wadhwa, R.1    Kaul, S.C.2    Ikawa, Y.3    Sugimoto, Y.4
  • 4
    • 0024380865 scopus 로고
    • Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
    • Mizzen LA, Chang C, Garrels JI, Welch WJ (1989) Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J Biol Chem 264:20664-20675.
    • (1989) J Biol Chem , vol.264 , pp. 20664-20675
    • Mizzen, L.A.1    Chang, C.2    Garrels, J.I.3    Welch, W.J.4
  • 5
    • 33847651284 scopus 로고    scopus 로고
    • Three faces of mortalin: A housekeeper, guardian and killer
    • Kaul SC, Deocaris CC, Wadhwa R (2007) Three faces of mortalin: A housekeeper, guardian and killer. Exp Gerontol 42:263-274.
    • (2007) Exp Gerontol , vol.42 , pp. 263-274
    • Kaul, S.C.1    Deocaris, C.C.2    Wadhwa, R.3
  • 8
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu Q, D'Silva P, Walter W, Marszalek J, Craig EA (2003) Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300:139-141.
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 9
    • 0036257364 scopus 로고    scopus 로고
    • Voltage-Dependent anionselective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-Shock protein PBP74
    • Schwarzer C, Barnikol-Watanabe S, Thinnes FP, Hilschmann N (2002) Voltage-Dependent anionselective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-Shock protein PBP74. Int J Biochem Cell Biol 34:1059-1070.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1059-1070
    • Schwarzer, C.1    Barnikol-Watanabe, S.2    Thinnes, F.P.3    Hilschmann, N.4
  • 10
    • 14244268253 scopus 로고    scopus 로고
    • Effect of GRP75/ mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells
    • Liu Y, Liu W, Song X-D, Zuo J (2005) Effect of GRP75/ mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Mol Cell Biochem 268:45-51.
    • (2005) Mol Cell Biochem , vol.268 , pp. 45-51
    • Liu, Y.1    Liu, W.2    Song, X.-D.3    Zuo, J.4
  • 12
    • 0036346345 scopus 로고    scopus 로고
    • Hsp70 family member, mot-2/ mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein
    • Wadhwa R (2002) Hsp70 family member, mot-2/ mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein. Exp Cell Res 274:246-253.
    • (2002) Exp Cell Res , vol.274 , pp. 246-253
    • Wadhwa, R.1
  • 14
    • 11144349225 scopus 로고    scopus 로고
    • Mortalin is over-Expressed by colorectal adenocarcinomas and correlates with poor survival
    • Dundas SR, Lawrie LC, Rooney PH, Murray GI (2005) Mortalin is over-Expressed by colorectal adenocarcinomas and correlates with poor survival. J Pathol 205: 74-81.
    • (2005) J Pathol , vol.205 , pp. 74-81
    • Dundas, S.R.1    Lawrie, L.C.2    Rooney, P.H.3    Murray, G.I.4
  • 16
    • 33646496005 scopus 로고    scopus 로고
    • Mortalin-Based cytoplasmic sequestration of p53 in a nonmammalian cancer model
    • Walker C, Böttger S, Low B (2006) Mortalin-Based cytoplasmic sequestration of p53 in a nonmammalian cancer model. Am J Pathol 168:1526-1530.
    • (2006) Am J Pathol , vol.168 , pp. 1526-1530
    • Walker, C.1    Böttger, S.2    Low, B.3
  • 17
    • 0033256455 scopus 로고    scopus 로고
    • NIH 3T3 cells malignantly transformed by mot-2 show inactivation and cytoplasmic sequestration of the p53 protein
    • Wadhwa R, Takano S, Mitsui Y, Kaul SC (1999) NIH 3T3 cells malignantly transformed by mot-2 show inactivation and cytoplasmic sequestration of the p53 protein. Cell Res 9:261-269.
    • (1999) Cell Res , vol.9 , pp. 261-269
    • Wadhwa, R.1    Takano, S.2    Mitsui, Y.3    Kaul, S.C.4
  • 18
    • 33748286872 scopus 로고    scopus 로고
    • Mortalin controls centrosome duplication via modulating centrosomal localization of p53
    • Ma Z, Izumi H, Kanai M, Kabuyama Y, Ahn NG, Fukasawa K (2006) Mortalin controls centrosome duplication via modulating centrosomal localization of p53. Oncogene 25:5377-5390.
    • (2006) Oncogene , vol.25 , pp. 5377-5390
    • Ma, Z.1    Izumi, H.2    Kanai, M.3    Kabuyama, Y.4    Ahn, N.G.5    Fukasawa, K.6
  • 20
    • 84904247615 scopus 로고    scopus 로고
    • Mortalin expression in normal and neoplastic tissues
    • Kaul S, Wadhwa R, New York: Springer
    • Nomikos A, Dundas SR, Murray GI, Mortalin expression in normal and neoplastic tissues. In: Kaul S, Wadhwa R, Eds. (2012) Mortalin biology: life, stress and death. New York: Springer, pp 257-265.
    • (2012) Mortalin Biology: Life, Stress and Death. , pp. 257-265
    • Nomikos, A.1    Dundas, S.R.2    Murray, G.I.3
  • 21
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-Amyloidinduced neurotoxicity in SH-SY5Y cells
    • Qu M, Zhou Z, Xu S, Chen C, Yu Z, Wang D (2011) Mortalin overexpression attenuates beta-amyloidinduced neurotoxicity in SH-SY5Y cells. Brain Res 1368:336-345.
    • (2011) Brain Res , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5    Wang, D.6
  • 22
    • 13644254746 scopus 로고    scopus 로고
    • Reduction in mortalin level by its antisense expression causes senescence-Like growth arrest in human immortalized cells
    • Wadhwa R, Takano S, Taira K, Kaul SC (2004) Reduction in mortalin level by its antisense expression causes senescence-Like growth arrest in human immortalized cells. J Gene Med 6:439-444.
    • (2004) J Gene Med , vol.6 , pp. 439-444
    • Wadhwa, R.1    Takano, S.2    Taira, K.3    Kaul, S.C.4
  • 23
    • 80052036411 scopus 로고    scopus 로고
    • Induction of mutant p53-Dependent apoptosis in human hepatocellular carcinoma by targeting stress protein mortalin
    • Lu W-J, Lee NP, Kaul SC, Lan F, Poon RTP, Wadhwa R, Luk JM (2011) Induction of mutant p53-Dependent apoptosis in human hepatocellular carcinoma by targeting stress protein mortalin. Int J Cancer 129:1806- 1814.
    • (2011) Int J Cancer , vol.129 , pp. 1806-1814
    • Lu, W.-J.1    Lee, N.P.2    Kaul, S.C.3    Lan, F.4    Poon, R.T.P.5    Wadhwa, R.6    Luk, J.M.7
  • 25
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • Wadhwa R, Sugihara T, Yoshida A, Nomura H, Reddel RR, Simpson R, Maruta H, Kaul SC (2000) Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res 60:6818-6821.
    • (2000) Cancer Res , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 26
    • 74949095086 scopus 로고    scopus 로고
    • Mortalin inhibitors sensitize K562 leukemia cells to complement-Dependent cytotoxicity
    • Pilzer D, Saar M, Koya K, Fishelson Z (2010) Mortalin inhibitors sensitize K562 leukemia cells to complement-Dependent cytotoxicity. Int J Cancer 126: 1428-1435.
    • (2010) Int J Cancer , vol.126 , pp. 1428-1435
    • Pilzer, D.1    Saar, M.2    Koya, K.3    Fishelson, Z.4
  • 31
    • 79960691369 scopus 로고    scopus 로고
    • Biochemical and structural studies on the high affinity of Hsp70 for ADP
    • Arakawa A, Handa N, Shirouzu M, Yokoyama S (2011) Biochemical and structural studies on the high affinity of Hsp70 for ADP. Protein Sci 20:1367-1379.
    • (2011) Protein Sci , vol.20 , pp. 1367-1379
    • Arakawa, A.1    Handa, N.2    Shirouzu, M.3    Yokoyama, S.4
  • 32
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenström P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38:W545-W549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 35
    • 0034837025 scopus 로고    scopus 로고
    • ATPase-Defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release
    • Barthel TK, Zhang J, Walker GC (2001) ATPase-Defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release. J Bacteriol 183:5482-5490.
    • (2001) J Bacteriol , vol.183 , pp. 5482-5490
    • Barthel, T.K.1    Zhang, J.2    Walker, G.C.3
  • 36
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
    • Flaherty KM, Wilbanks SM, DeLuca-Flaherty C, McKay DB (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J Biol Chem 269:12899-12907.
    • (1994) J Biol Chem , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    Deluca-Flaherty, C.3    McKay, D.B.4
  • 37
    • 84878617377 scopus 로고    scopus 로고
    • Real-Time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET
    • Sikor M, Mapa K, Voithenberg von LV, Mokranjac D, Lamb DC (2013) Real-Time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET. EMBO J 32:1639-1649.
    • (2013) EMBO J , vol.32 , pp. 1639-1649
    • Sikor, M.1    Mapa, K.2    Voithenberg Von, L.V.3    Mokranjac, D.4    Lamb, D.C.5
  • 39
    • 84864517463 scopus 로고    scopus 로고
    • Enhanced J-Protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease
    • Goswami AV, Samaddar M, Sinha D, Purushotham J, D'Silva P (2012) Enhanced J-Protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease. Hum Mol Genet 21:3317-3332.
    • (2012) Hum Mol Genet , vol.21 , pp. 3317-3332
    • Goswami, A.V.1    Samaddar, M.2    Sinha, D.3    Purushotham, J.4    D'Silva, P.5
  • 40
    • 84858955705 scopus 로고    scopus 로고
    • Reactivation of protein aggregates by mortalin and Tid1-The human mitochondrial Hsp70 chaperone system
    • Iosefson O, Sharon S, Goloubinoff P, Azem A (2012) Reactivation of protein aggregates by mortalin and Tid1-The human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones 17:57-66.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 57-66
    • Iosefson, O.1    Sharon, S.2    Goloubinoff, P.3    Azem, A.4
  • 41
    • 0032516866 scopus 로고    scopus 로고
    • Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-Like proteins, the Co-Chaperones of specific Hsp70 members
    • Naylor DJ, Stines AP, Hoogenraad NJ, Høj PB (1998) Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-Like proteins, the Co-Chaperones of specific Hsp70 members. J Biol Chem 273:21169-21177.
    • (1998) J Biol Chem , vol.273 , pp. 21169-21177
    • Naylor, D.J.1    Stines, A.P.2    Hoogenraad, N.J.3    Høj, P.B.4
  • 42
    • 0035804671 scopus 로고    scopus 로고
    • Identification and characterization of a human mitochondrial homologue of the bacterial co-Chaperone GrpE
    • Choglay AA, Chapple JP, Blatch GL, Cheetham ME (2001) Identification and characterization of a human mitochondrial homologue of the bacterial co-Chaperone GrpE. Gene 267:125-134.
    • (2001) Gene , vol.267 , pp. 125-134
    • Choglay, A.A.1    Chapple, J.P.2    Blatch, G.L.3    Cheetham, M.E.4
  • 43
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 44
    • 84862289262 scopus 로고    scopus 로고
    • Crystal structure of DnaK protein complexed with nucleotide exchange factor GrpE in DnaK chaperone system: Insight into intermolecular communication
    • Wu C-C, Naveen V, Chien C-H, Chang Y-W, Hsiao C-D (2012) Crystal structure of DnaK protein complexed with nucleotide exchange factor GrpE in DnaK chaperone system: Insight into intermolecular communication. J Biol Chem 287:21461-21470.
    • (2012) J Biol Chem , vol.287 , pp. 21461-21470
    • Wu, C.-C.1    Naveen, V.2    Chien, C.-H.3    Chang, Y.-W.4    Hsiao, C.-D.5
  • 45
    • 0035052323 scopus 로고    scopus 로고
    • An N-Terminal region of mot-2 binds to p53 in vitro
    • Kaul SC, Reddel RR, Mitsui Y, Wadhwa R (2001) An N-Terminal region of mot-2 binds to p53 in vitro. Neoplasia 3:110-114.
    • (2001) Neoplasia , vol.3 , pp. 110-114
    • Kaul, S.C.1    Reddel, R.R.2    Mitsui, Y.3    Wadhwa, R.4
  • 46
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-Bound open conformation of Hsp70 chaperones
    • Kityk R, Kopp J, Sinning I, Mayer MP (2012) Structure and dynamics of the ATP-Bound open conformation of Hsp70 chaperones. Mol Cell 48:863-874.
    • (2012) Mol Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 48
    • 28244470279 scopus 로고    scopus 로고
    • Activation of wild type p53 function by its mortalinbinding, cytoplasmically localizing carboxyl terminus peptides
    • Kaul SC, Aida S, Yaguchi T, Kaur K, Wadhwa R (2005) Activation of wild type p53 function by its mortalinbinding, cytoplasmically localizing carboxyl terminus peptides. J Biol Chem 280:39373-39379.
    • (2005) J Biol Chem , vol.280 , pp. 39373-39379
    • Kaul, S.C.1    Aida, S.2    Yaguchi, T.3    Kaur, K.4    Wadhwa, R.5
  • 49
    • 77950370585 scopus 로고    scopus 로고
    • Reconstitution of the mitochondrial Hsp70 (mortalin)-P53 interaction using purified proteins-Identification of additional interacting regions
    • Iosefson O, Azem A (2010) Reconstitution of the mitochondrial Hsp70 (mortalin)-P53 interaction using purified proteins-Identification of additional interacting regions. FEBS Lett 584:1080-1084.
    • (2010) FEBS Lett , vol.584 , pp. 1080-1084
    • Iosefson, O.1    Azem, A.2
  • 51
    • 77649190277 scopus 로고    scopus 로고
    • Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer
    • Ahn BY, Trinh DLN, Zajchowski LD, Lee B, Elwi AN, Kim SW (2009) Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer. Oncogene 29:1155-1166.
    • (2009) Oncogene , vol.29 , pp. 1155-1166
    • Ahn, B.Y.1    Trinh, D.L.N.2    Zajchowski, L.D.3    Lee, B.4    Elwi, A.N.5    Kim, S.W.6
  • 52
    • 79957464247 scopus 로고    scopus 로고
    • Direct interaction between p53 and Tid1 proteins affects p53 mitochondrial localization and apoptosisy as a target for cancer therapy?
    • Trinh DLN, Elwi AN, Kim S-W (2010) Direct interaction between p53 and Tid1 proteins affects p53 mitochondrial localization and apoptosisy as a target for cancer therapy? Oncotarget 1:405-422.
    • (2010) Oncotarget , vol.1 , pp. 405-422
    • Trinh, D.L.N.1    Elwi, A.N.2    Kim, S.-W.3
  • 54
    • 77951106537 scopus 로고    scopus 로고
    • Kinetic and structural characterization of human mortalin
    • Luo W-I, Dizin E, Yoon T, Cowan JA (2010) Kinetic and structural characterization of human mortalin. Protein Expr Purif 72:75-81.
    • (2010) Protein Expr Purif , vol.72 , pp. 75-81
    • Luo, W.-I.1    Dizin, E.2    Yoon, T.3    Cowan, J.A.4
  • 55
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield P, Garrard S, Derewenda Z (1999) Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr Purif 15:34-39.
    • (1999) Protein Expr Purif , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 56
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-Type catalytic proficiency
    • Kapust RB, Tózsér J, Fox JD, Anderson DE, Cherry S, Copeland TD, Waugh DS (2001) Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-Type catalytic proficiency. Protein Eng 14:993-1000.
    • (2001) Protein Eng , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tózsér, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 65
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y (2010) I-TASSER: A unified platform for automated protein structure and function prediction. Nat Protoc 5:725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 67
    • 33750210515 scopus 로고    scopus 로고
    • Homology modeling using parametric alignment ensemble generation with consensus and energy-Based model selection
    • Chivian D, Baker D (2006) Homology modeling using parametric alignment ensemble generation with consensus and energy-Based model selection. Nucleic Acids Res 34:e112.
    • (2006) Nucleic Acids Res , vol.34
    • Chivian, D.1    Baker, D.2
  • 69
    • 79955716232 scopus 로고    scopus 로고
    • Rosetta FlexPepDock ab-Initio: Simultaneous folding, docking and refinement of peptides onto their receptors
    • Raveh B, London N, Zimmerman L, Schueler-Furman O (2011) Rosetta FlexPepDock ab-initio: Simultaneous folding, docking and refinement of peptides onto their receptors. PLoS ONE 6:e18934.
    • (2011) PLoS ONE , vol.6
    • Raveh, B.1    London, N.2    Zimmerman, L.3    Schueler-Furman, O.4
  • 70
    • 70349597601 scopus 로고    scopus 로고
    • Electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • Moriarty NW, Grosse-Kunstleve RW, Adams PD (2009) electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation. Acta Crystallogr D65:1074-1080.
    • (2009) Acta Crystallogr D , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 71
    • 58149094776 scopus 로고    scopus 로고
    • RosettaLigand docking with full ligand and receptor flexibility
    • Davis IW, Baker D (2009) RosettaLigand docking with full ligand and receptor flexibility. J Mol Biol 385:381-392.
    • (2009) J Mol Biol , vol.385 , pp. 381-392
    • Davis, I.W.1    Baker, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.