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Volumn 7, Issue 1, 2013, Pages

Extrapolating the effect of deleterious nsSNPs in the binding adaptability of flavopiridol with CDK7 protein: A molecular dynamics approach

Author keywords

CDK7; Docking; Flavopiridol; Molecular dynamics; NsSNPs

Indexed keywords

ARGININE; CYCLIN DEPENDENT KINASE 7; FLAVOPIRIDOL; HISTIDINE; ISOLEUCINE; METHIONINE; MUTANT PROTEIN; THREONINE; AMINO ACID; CYCLIN DEPENDENT KINASE; CYCLIN-DEPENDENT KINASE-ACTIVATING KINASE; FLAVONOID; PIPERIDINE DERIVATIVE; PROTEIN BINDING;

EID: 84896279000     PISSN: 14739542     EISSN: 14797364     Source Type: Journal    
DOI: 10.1186/1479-7364-7-10     Document Type: Article
Times cited : (51)

References (77)
  • 1
    • 0029418115 scopus 로고
    • The regulation and functions of Cdk7
    • Shuttleworth J: The regulation and functions of Cdk7. Prog Cell Cycle Res 1995, 1:229-240.
    • (1995) Prog Cell Cycle Res , vol.1 , pp. 229-240
    • Shuttleworth, J.1
  • 2
    • 25444444192 scopus 로고    scopus 로고
    • CAK-Cyclin-Dependent Activating Kinase: A key kinase in cell cycle control and a target for Drugs?
    • Lolli G, Johnson LN: CAK-cyclin-dependent activating kinase: a key kinase in cell cycle control and a target for drugs? Cell Cycle 2005, 4:572-577. (Pubitemid 41359784)
    • (2005) Cell Cycle , vol.4 , Issue.4 , pp. 572-577
    • Lolli, G.1    Johnson, L.N.2
  • 3
    • 0034747803 scopus 로고    scopus 로고
    • Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop
    • Garrett S, Barton WA, Knights R, Jin P, Morgan DO: Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop. Mol Cell Biol 2001, 21:88-99.
    • (2001) Mol Cell Biol , vol.21 , pp. 88-99
    • Garrett, S.1    Barton, W.A.2    Knights, R.3    Jin, P.4    Morgan, D.O.5
  • 4
    • 0029893446 scopus 로고    scopus 로고
    • Expression of CDK7/CAK in normal and tumour cells of diverse histogenesis, cell-cycle position and differentiation
    • Bartkova J, Zemanova M, Bartek J: Expression of CDK7/CAK in normal and tumour cells of diverse histogenesis, cell cycle position and differentiation. Int J Cancer 1996, 66(6):732-737. (Pubitemid 26197939)
    • (1996) International Journal of Cancer , vol.66 , Issue.6 , pp. 732-737
    • Bartkova, J.1    Zemanova, M.2    Bartek, J.3
  • 7
    • 27144434812 scopus 로고    scopus 로고
    • Transcription inhibition by flavopiridol: Mechanism of chronic lymphocytic leukemia cell death
    • DOI 10.1182/blood-2005-04-1678
    • Chen R, Keating MJ, Gandhi V, Plunkett W: Transcription inhibition by flavopiridol: mechanism of chronic lymphocytic leukemia cell death. Blood 2005, 106(7):2513-9. (Pubitemid 41510827)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2513-2519
    • Chen, R.1    Keating, M.J.2    Gandhi, V.3    Plunkett, W.4
  • 9
    • 0141815505 scopus 로고    scopus 로고
    • Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation
    • DOI 10.1046/j.1432-1033.2003.03794.x
    • Palancade B, Bensaude O: Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation. Eur J Biochem 2003, 270:3859-3870. (Pubitemid 37193863)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.19 , pp. 3859-3870
    • Palancade, B.1    Bensaude, O.2
  • 10
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: The short and long of it
    • DOI 10.1101/gad.1235904
    • Sims RJ III, Belotserkovskaya R, Reinberg D: Elongation by RNA polymerase II: the short and long of it. Genes Dev 2004, 18:2437-2468. (Pubitemid 39362887)
    • (2004) Genes and Development , vol.18 , Issue.20 , pp. 2437-2468
    • Sims III, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 12
    • 0032429154 scopus 로고    scopus 로고
    • A DNA polymorphism discovery resource for research on human genetic variation
    • Collins FS, Brooks LD, Chakravarti A: A DNA polymorphism discovery resource for research on human genetic variation. Genome Res 1998, 8:1229-1231. (Pubitemid 29039095)
    • (1998) Genome Research , vol.8 , Issue.12 , pp. 1229-1231
    • Collins, F.S.1    Brooks, L.D.2    Chakravarti, A.3
  • 14
    • 32044453591 scopus 로고    scopus 로고
    • Identification and analysis of deleterious human SNPs
    • DOI 10.1016/j.jmb.2005.12.025, PII S0022283605015871
    • Yue P, Moult J: Identification and analysis of deleterious human SNPs. J Mol Biol 2006, 356:1263-1274. (Pubitemid 43199928)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.5 , pp. 1263-1274
    • Yue, P.1    Moult, J.2
  • 15
    • 0345863841 scopus 로고    scopus 로고
    • TopoSNP: A topographic database of non-synonymous single nucleotide polymorphisms with and without known disease association
    • Stitziel NO, Binkowski TA, Tseng YY, Kasif S, Liang J: topoSNP: a topographic database of non-synonymous single nucleotide polymorphisms with and without known disease association. Nucleic Acids Res 2004, 32:D520-D522. (Pubitemid 38081712)
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATA. ISSUE
    • Stitziel, N.O.1    Binkowski, T.A.2    Tseng, Y.Y.3    Kasif, S.4    Liang, J.5
  • 16
    • 34547611433 scopus 로고    scopus 로고
    • Structure SNP (StSNP): A web server for mapping and modeling nsSNPs on protein structures with linkage to metabolic pathways
    • Uzun A, Leslin CM, Abyzov A, Ilyin V: Structure SNP (StSNP): a web server for mapping and modeling nsSNPs on protein structures with linkage to metabolic pathways. Nucleic Acids Res 2007, 35:W384-W392.
    • (2007) Nucleic Acids Res , vol.35
    • Uzun, A.1    Leslin, C.M.2    Abyzov, A.3    Ilyin, V.4
  • 17
    • 38549146891 scopus 로고    scopus 로고
    • ColiSNP database server mapping nsSNPs on protein structures
    • DOI 10.1093/nar/gkm801
    • Kono H, Yuasa T, Nishiue S, Yura K: coliSNP database server mapping nsSNPs on protein structures. Nucleic Acids Res 2008, 36:D409-D413. (Pubitemid 351149758)
    • (2008) Nucleic Acids Research , vol.36 , Issue.SUPPL. 1
    • Kono, H.1    Yuasa, T.2    Nishiue, S.3    Yura, K.4
  • 19
    • 33748672451 scopus 로고    scopus 로고
    • SNPeffect v2.0: A new step in investigating the molecular phenotypic effects of human non-synonymous SNPs
    • DOI 10.1093/bioinformatics/btl348
    • Reumers J, Maurer-Stroh S, Schymkowitz J, Rousseau F: SNPeffect v2.0: a new step in investigating the molecular phenotypic effects of human non-synonymous SNPs. Bioinformatics 2006, 22:2183-2185. (Pubitemid 44390919)
    • (2006) Bioinformatics , vol.22 , Issue.17 , pp. 2183-2185
    • Reumers, J.1    Maurer-Stroh, S.2    Schymkowitz, J.3    Rousseau, F.4
  • 21
    • 33644876453 scopus 로고    scopus 로고
    • SNP500Cancer: A public resource for sequence validation, assay development, and frequency analysis for genetic variation in candidate genes
    • Packer BR, Yeager M, Burdett L, Welch R, Beerman M: SNP500Cancer: a public resource for sequence validation, assay development, and frequency analysis for genetic variation in candidate genes. Nucleic Acids Res 2006, 34:D617-D621.
    • (2006) Nucleic Acids Res , vol.34
    • Packer, B.R.1    Yeager, M.2    Burdett, L.3    Welch, R.4    Beerman, M.5
  • 22
    • 33846071416 scopus 로고    scopus 로고
    • PolyDoms: A whole genome database for the identification of non-synonymous coding SNPs with the potential to impact disease
    • DOI 10.1093/nar/gkl826
    • Jegga AG, Gowrisankar S, Chen J, Aronow BJ: PolyDoms: a whole genome database for the identification of non-synonymous coding SNPs with the potential to impact disease. Nucleic Acids Res 2007, 35:D700-D706. (Pubitemid 46056295)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL. 1
    • Jegga, A.G.1    Gowrisankar, S.2    Chen, J.3    Aronow, B.J.4
  • 23
    • 57649232146 scopus 로고    scopus 로고
    • An integrated database-pipeline system for studying single nucleotide polymorphisms and diseases
    • Yang JO, Hwang S, Oh J, Bhak J, Sohn TK: An integrated database-pipeline system for studying single nucleotide polymorphisms and diseases. BMC Bioinformatics 2008, 12:S19.
    • (2008) BMC Bioinformatics , vol.12
    • Yang, J.O.1    Hwang, S.2    Oh, J.3    Bhak, J.4    Sohn, T.K.5
  • 24
    • 79952764520 scopus 로고    scopus 로고
    • Performance of mutation pathogenicity prediction methods on missense variants
    • Thusberg J, Olatubosun A, Vihinen M: Performance of mutation pathogenicity prediction methods on missense variants. Hum Mutat 2011, 32:358-68.
    • (2011) Hum Mutat , vol.32 , pp. 358-368
    • Thusberg, J.1    Olatubosun, A.2    Vihinen, M.3
  • 25
    • 11844281294 scopus 로고    scopus 로고
    • A neural-network-based method for predicting protein stability changes upon single point mutations
    • Capriotti E, Fariselli P, Casadio R: A neural-network-based method for predicting protein stability changes upon single point mutations. Bioinformatics 2004, 20:63-68.
    • (2004) Bioinformatics , vol.20 , pp. 63-68
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 26
    • 78650659877 scopus 로고    scopus 로고
    • Molecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370S
    • Offman MN, Krol M, Silman I, Sussman JL, Futerman AH: Molecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370S. J Biol Chem 2010, 285:42105-42114.
    • (2010) J Biol Chem , vol.285 , pp. 42105-42114
    • Offman, M.N.1    Krol, M.2    Silman, I.3    Sussman, J.L.4    Futerman, A.H.5
  • 27
    • 80052690225 scopus 로고    scopus 로고
    • Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-b -glucosidase mutant that causes Gaucher disease
    • Offman MN, Krol M, Rost B, Silman I, Sussman JL: Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-b -glucosidase mutant that causes Gaucher disease. Protein Engineering Design & Selection 2011, 24(10):773-5.
    • (2011) Protein Engineering Design & Selection , vol.24 , Issue.10 , pp. 773-775
    • Offman, M.N.1    Krol, M.2    Rost, B.3    Silman, I.4    Sussman, J.L.5
  • 28
    • 68149165614 scopus 로고    scopus 로고
    • SIFT: Predicting the effects of coding nonsynonymous variants on protein function using the SIFT algorithm
    • Kumar P, Henikoff S, Ng PC: SIFT: predicting the effects of coding nonsynonymous variants on protein function using the SIFT algorithm. Nat Protoc 2009, 4:1073-81.
    • (2009) Nat Protoc , vol.4 , pp. 1073-1081
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 29
    • 0036713510 scopus 로고    scopus 로고
    • Human non-synonymous SNPs: Server and survey
    • Ramensky V, Bork P, Sunyaev S: Human non-synonymous SNPs: server and survey. Nucleic Acids Res 2002, 30:3894-3900. (Pubitemid 35012462)
    • (2002) Nucleic Acids Research , vol.30 , Issue.17 , pp. 3894-3900
    • Ramensky, V.1    Bork, P.2    Sunyaev, S.3
  • 30
    • 33846067524 scopus 로고    scopus 로고
    • PANTHER version 6: Protein sequence and function evolution data with expanded representation of biological pathways
    • Mi H, Guo N, Kejariwal A, Thomas PD: PANTHER version 6: protein sequence and function evolution data with expanded representation of biological pathways. Nucleic Acids Res 2007, 35:247-52.
    • (2007) Nucleic Acids Res , vol.35 , pp. 247-252
    • Mi, H.1    Guo, N.2    Kejariwal, A.3    Thomas, P.D.4
  • 31
    • 43349096923 scopus 로고    scopus 로고
    • A three-state prediction of single point mutations on protein stability changes
    • Capriotti E, Fariselli P, Rossi I, Casadio R: A three-state prediction of single point mutations on protein stability changes. BMC Bioinformatics 2008, 9 (Suppl 2):S6.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 2
    • Capriotti, E.1    Fariselli, P.2    Rossi, I.3    Casadio, R.4
  • 32
    • 67749137351 scopus 로고    scopus 로고
    • Functional annotations improve the predictive score of human disease-related mutations in proteins
    • Calabrese R, Capriotti E, Fariselli P, Martelli PL, Casadio R: Functional annotations improve the predictive score of human disease-related mutations in proteins. Human Mutation 2009, 30:1237-1244.
    • (2009) Human Mutation , vol.30 , pp. 1237-1244
    • Calabrese, R.1    Capriotti, E.2    Fariselli, P.3    Martelli, P.L.4    Casadio, R.5
  • 33
    • 33751013750 scopus 로고    scopus 로고
    • Predicting the insurgence of human genetic diseases associated to single point protein mutations with support vector machines and evolutionary information
    • DOI 10.1093/bioinformatics/btl423
    • Capriotti E, Calabrese R, Casadio R: Predicting the insurgence of human genetic diseases associated to single point protein mutations with support vector machines and evolutionary information. Bioinformatics 2006, 22:2729-2734. (Pubitemid 44742391)
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2729-2734
    • Capriotti, E.1    Calabrese, R.2    Casadio, R.3
  • 34
    • 34547100092 scopus 로고    scopus 로고
    • SNAP: Predict effect of non-synonymous polymorphisms on function
    • DOI 10.1093/nar/gkm238
    • Bromberg Y, Rost B: SNAP: predict effect of non-synonymous polymorphisms on function. Nucleic Acids Res 2007, 35:3823-3835. (Pubitemid 47244674)
    • (2007) Nucleic Acids Research , vol.35 , Issue.11 , pp. 3823-3835
    • Bromberg, Y.1    Rost, B.2
  • 35
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E: GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 2008, 4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 38
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK: AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J. Comput Chem 2009, 30:2785-2791.
    • (2009) J. Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5
  • 41
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its new supplement TREMBL
    • Amos B, Rolf A: The SWISS-PROT protein sequence data bank and its new supplement TREMBL. Nucleic Acids Res 1996, 24:21-25.
    • (1996) Nucleic Acids Res , vol.24 , pp. 21-25
    • Amos, B.1    Rolf, A.2
  • 43
    • 7944231428 scopus 로고    scopus 로고
    • The crystal structure of human CDK7 and its protein recognition properties
    • DOI 10.1016/j.str.2004.08.013, PII S0969212604003429
    • Lolli G, Lowe ED, Brown NR, Johnson LN: The crystal structure of human CDK7 and its protein recognition properties. Structure 2004, 12:2067-79. (Pubitemid 39469404)
    • (2004) Structure , vol.12 , Issue.11 , pp. 2067-2079
    • Lolli, G.1    Lowe, E.D.2    Brown, N.R.3    Johnson, L.N.4
  • 45
    • 78651287426 scopus 로고    scopus 로고
    • DrugBank 3.0: A comprehensive resource for 'Omics' research on drugs
    • Knox C, Law V, Jewison T, Liu P, Ly S: DrugBank 3.0: a comprehensive resource for 'Omics' research on drugs. Nucleic Acids Res 2011, 39 (Database issue):D1035-41.
    • (2011) Nucleic Acids Res , vol.39 , Issue.DATA. ISSUE
    • Knox, C.1    Law, V.2    Jewison, T.3    Liu, P.4    Ly, S.5
  • 49
    • 0030043489 scopus 로고    scopus 로고
    • Cation-p interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty DA: Cation-p interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 1996, 271:163-168. (Pubitemid 26033294)
    • (1996) Science , vol.271 , Issue.5246 , pp. 163-168
    • Dougherty, D.A.1
  • 50
    • 0033578302 scopus 로고    scopus 로고
    • Cation-p interactions in structural biology
    • Gallivan JP, Dougherty DA: Cation-p interactions in structural biology. Proc Natl Acad Sci 1999, 96:9459-9464.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 52
    • 0027433237 scopus 로고
    • Alteration of the phosphorylation state of p34cdc2 kinase by the flavone L86-8275 in breast carcinoma cells. Correlation with decreased HI kinase activity
    • Worland PJ, Kaur G, Stetler-Stevenson M, Sebers S, Sartor O: Alteration of the phosphorylation state of p34cdc2 kinase by the flavone L86-8275 in breast carcinoma cells. Correlation with decreased HI kinase activity. Biochem Pharmacol 1993, 46:1831.
    • (1993) Biochem Pharmacol , vol.46 , pp. 1831
    • Worland, P.J.1    Kaur, G.2    Stetler-Stevenson, M.3    Sebers, S.4    Sartor, O.5
  • 53
    • 0000570024 scopus 로고
    • Basis of biological specificity
    • Fersht AR: Basis of biological specificity. Trends Biochem Sci 1984, 9:145-147.
    • (1984) Trends Biochem Sci , vol.9 , pp. 145-147
    • Fersht, A.R.1
  • 54
    • 0026584344 scopus 로고
    • Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
    • Shirley BA, Stanssens P, Hahn U, Pace CN: Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry 1992, 31:725-32.
    • (1992) Biochemistry , vol.31 , pp. 725-732
    • Shirley, B.A.1    Stanssens, P.2    Hahn, U.3    Pace, C.N.4
  • 55
    • 77956276773 scopus 로고    scopus 로고
    • Computational analysis of missense mutations causing Snyder-Robinson syndrome
    • Zhang Z, Teng S, Wang L, Schwartz CE, Alexov E: Computational analysis of missense mutations causing Snyder-Robinson syndrome. Hum Mutat 2010, 31:1043-9.
    • (2010) Hum Mutat , vol.31 , pp. 1043-1049
    • Zhang, Z.1    Teng, S.2    Wang, L.3    Schwartz, C.E.4    Alexov, E.5
  • 56
    • 42949163017 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms that cause structural changes in the cyclic AMP receptor protein transcriptional regulator of the tuberculosis vaccine strain Mycobacterium bovis BCG alter global gene expression without attenuating growth
    • DOI 10.1128/IAI.01410-07
    • Hunt DM, Saldanha JW, Brennan JF, Benjamin P, Strom M: Single nucleotide polymorphisms that cause structural changes in the cyclic AMP receptor protein transcriptional regulator of the tuberculosis vaccine strain Mycobacterium bovis BCG alter global gene expression without attenuating growth. Infect Immun 2008, 76:2227-34. (Pubitemid 351656159)
    • (2008) Infection and Immunity , vol.76 , Issue.5 , pp. 2227-2234
    • Hunt, D.M.1    Saldanha, J.W.2    Brennan, J.F.3    Benjamin, P.4    Strom, M.5    Cole, J.A.6    Spreadbury, C.L.7    Buxton, R.S.8
  • 57
    • 0034897806 scopus 로고    scopus 로고
    • Missense polymorphism in the human carboxypeptidase e gene alters enzymatic activity
    • Chen H, Jawahar S, Qian Y, Duong Q, Chan G: Missense polymorphism in the human carboxypeptidase E gene alters enzymatic activity. Hum Mutat 2001, 18:120-131.
    • (2001) Hum Mutat , vol.18 , pp. 120-131
    • Chen, H.1    Jawahar, S.2    Qian, Y.3    Duong, Q.4    Chan, G.5
  • 58
    • 70350638919 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants in TMPRSS6 associated with hemoglobin levels
    • Chambers JC, Zhang WLY, Sehmi J, Wass MN, Zabaneh D: Genome-wide association study identifies variants in TMPRSS6 associated with hemoglobin levels. Nat Genet 2009, 41:1170-2.
    • (2009) Nat Genet , vol.41 , pp. 1170-1172
    • Chambers, J.C.1    Zhang, W.L.Y.2    Sehmi, J.3    Wass, M.N.4    Zabaneh, D.5
  • 59
    • 82255193117 scopus 로고    scopus 로고
    • Association between DNA-repair polymorphisms and survival in pancreatic cancer patients treated with combination chemotherapy
    • Giovannetti E, Pacetti P, Reni M, Leon LG, Mambrini A: Association between DNA-repair polymorphisms and survival in pancreatic cancer patients treated with combination chemotherapy. Pharmacogenomics 2011, 12:1641-52.
    • (2011) Pharmacogenomics , vol.12 , pp. 1641-1652
    • Giovannetti, E.1    Pacetti, P.2    Reni, M.3    Leon, L.G.4    Mambrini, A.5
  • 60
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • DOI 10.1002/humu.22
    • Wang Z, Moult J: SNPs, protein structure, and disease. Hum Mutat 2001, 17:263-270. (Pubitemid 32268400)
    • (2001) Human Mutation , vol.17 , Issue.4 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 61
    • 44149083268 scopus 로고    scopus 로고
    • Effect of deleterious nsSNP on the HER2 receptor based on stability and binding affinity with Herceptin: A computational approach
    • Rajasekaran R, George Priya Doss C, Sudandiradoss C, Ramanathan K, Purohit R, Sethumadhavan R: Effect of deleterious nsSNP on the HER2 receptor based on stability and binding affinity with Herceptin: a computational approach. C R Biol 2008, 331(6):409-417.
    • (2008) C R Biol , vol.331 , Issue.6 , pp. 409-417
    • Rajasekaran, R.1    George Priya Doss, C.2    Sudandiradoss, C.3    Ramanathan, K.4    Purohit, R.5    Sethumadhavan, R.6
  • 62
    • 80054886709 scopus 로고    scopus 로고
    • In silico identification and analysis of drug resistant mutants of ABL tyrosine kinase based on detrimental missense mutations
    • Rajasekaran R, George Priya Doss C, Arun Prasad G, Sethumadhavan R: In silico identification and analysis of drug resistant mutants of ABL tyrosine kinase based on detrimental missense mutations. Curr Signal Transd T 2011, 6:396-404.
    • (2011) Curr Signal Transd T , vol.6 , pp. 396-404
    • Rajasekaran, R.1    George Priya Doss, C.2    Arun Prasad, G.3    Sethumadhavan, R.4
  • 63
    • 46649114390 scopus 로고    scopus 로고
    • Identification and structural comparison of deleterious mutations in nsSNPs of ABL1 gene in chronic myeloid leukemia a bioinformatics study
    • George Priya Doss C, Sudandiradoss C, Rajasekaran R, Rituraj P, Ramanathan K, Rao S: Identification and structural comparison of deleterious mutations in nsSNPs of ABL1 gene in chronic myeloid leukemia a bioinformatics study. J Biomed Inform 2008, 41(4):607-612.
    • (2008) J Biomed Inform , vol.41 , Issue.4 , pp. 607-612
    • George Priya Doss, C.1    Sudandiradoss, C.2    Rajasekaran, R.3    Rituraj, P.4    Ramanathan, K.5    Rao, S.6
  • 64
    • 61349150041 scopus 로고    scopus 로고
    • Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange
    • Hsu YH, Johnson DA, Traugh JA: Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. J Biol Chem 2008, 283:36397-36405.
    • (2008) J Biol Chem , vol.283 , pp. 36397-36405
    • Hsu, Y.H.1    Johnson, D.A.2    Traugh, J.A.3
  • 65
    • 61849183478 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase (Btk): Function, regulation, and transformation with special emphasis on the PH domain
    • Mohamed AJ, Yu L, Backesjo CM, Vargas L, Faryal R: Bruton's tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain. Immunol Rev 2009, 228:58-73.
    • (2009) Immunol Rev , vol.228 , pp. 58-73
    • Mohamed, A.J.1    Yu, L.2    Backesjo, C.M.3    Vargas, L.4    Faryal, R.5
  • 66
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • Muller CW, Schlauderer GJ, Reinstein J, Schulz GE: Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure 1996, 4:147-156. (Pubitemid 126658978)
    • (1996) Structure , vol.4 , Issue.2 , pp. 147-156
    • Muller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 67
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen M: Relationship of protein flexibility to thermostability. Protein Eng 1987, 1:477-480.
    • (1987) Protein Eng , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 68
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: Predicting amino acid changes that affect protein function
    • DOI 10.1093/nar/gkg509
    • Ng PC, Henikoff S: SIFT: predicting amino acid changes that affect protein function. Nucleic Acids Res 2003, 13:3812-3814. (Pubitemid 37442253)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 69
    • 0035026704 scopus 로고    scopus 로고
    • SIFT: Predicting deleterious amino acid changes that affect protein function
    • Ng PC, Henikoff S: SIFT: predicting deleterious amino acid changes that affect protein function. Genome Res 2001, 11:863-874.
    • (2001) Genome Res , vol.11 , pp. 863-874
    • Ng, P.C.1    Henikoff, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.