메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

In silico screening and molecular dynamics simulation of disease-associated nsSNP in TYRP1 gene and its structural consequences in OCA3

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; TYROSINASE RELATED PROTEIN 1; MEMBRANE PROTEIN; OXIDOREDUCTASE; TYRP1 PROTEIN, HUMAN;

EID: 84880171829     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/697051     Document Type: Article
Times cited : (73)

References (67)
  • 1
    • 0026534062 scopus 로고
    • Assignment of the human TYRP (brown) locus to chromosome region 9p23 by nonradioactive in situ hybridization
    • 2-s2.0-0026534062 10.1016/0888-7543(92)90228-K
    • Murty V. V. V. S., Bouchard B., Mathew S., Vijayasaradhi S., Houghton A. N., Assignment of the human TYRP (brown) locus to chromosome region 9p23 by nonradioactive in situ hybridization. Genomics 1992 13 1 227 229 2-s2.0-0026534062 10.1016/0888-7543(92)90228-K
    • (1992) Genomics , vol.13 , Issue.1 , pp. 227-229
    • Murty, V.V.V.S.1    Bouchard, B.2    Mathew, S.3    Vijayasaradhi, S.4    Houghton, A.N.5
  • 2
    • 0026048137 scopus 로고
    • Structural organization of the pigment cell-specific gene located at the brown locus in mouse: Its promoter activity and alternatively spliced transcripts
    • 2-s2.0-0026048137
    • Shibahara S., Taguchi H., Muller R. M., Shibata K., Cohen T., Tomita Y., Tagami H., Structural organization of the pigment cell-specific gene located at the brown locus in mouse: its promoter activity and alternatively spliced transcripts. The Journal of Biological Chemistry 1991 266 24 15895 15901 2-s2.0-0026048137
    • (1991) The Journal of Biological Chemistry , vol.266 , Issue.24 , pp. 15895-15901
    • Shibahara, S.1    Taguchi, H.2    Muller, R.M.3    Shibata, K.4    Cohen, T.5    Tomita, Y.6    Tagami, H.7
  • 3
    • 0029095104 scopus 로고
    • Chromosomal structure of the human TYRP1 and TYRP2 loci and comparison of the tyrosinase-related protein gene family
    • 2-s2.0-0029095104 10.1006/geno.1995.1211
    • Sturm R. A., O'Sullivan B. J., Box N. F., Smith A. G., Smit S. E., Puttick E. R. J., Parsons P. G., Dunn I. S., Chromosomal structure of the human TYRP1 and TYRP2 loci and comparison of the tyrosinase-related protein gene family. Genomics 1995 29 1 24 34 2-s2.0-0029095104 10.1006/geno.1995.1211
    • (1995) Genomics , vol.29 , Issue.1 , pp. 24-34
    • Sturm, R.A.1    O'Sullivan, B.J.2    Box, N.F.3    Smith, A.G.4    Smit, S.E.5    Puttick, E.R.J.6    Parsons, P.G.7    Dunn, I.S.8
  • 4
    • 0031944118 scopus 로고    scopus 로고
    • Complete sequence and polymorphism study of the human TYRP1 gene encoding tyrosinase-related protein 1
    • 2-s2.0-0031944118 10.1007/s003359900678
    • Box N. F., Wyeth J. R., Mayne C. J., O'Gorman L. E., Martin N. G., Sturm R. A., Complete sequence and polymorphism study of the human TYRP1 gene encoding tyrosinase-related protein 1. Mammalian Genome 1998 9 1 50 53 2-s2.0-0031944118 10.1007/s003359900678
    • (1998) Mammalian Genome , vol.9 , Issue.1 , pp. 50-53
    • Box, N.F.1    Wyeth, J.R.2    Mayne, C.J.3    O'Gorman, L.E.4    Martin, N.G.5    Sturm, R.A.6
  • 5
    • 0026051621 scopus 로고
    • Biosynthesis and intracellular movement of the melanosomal membrane glycoprotein gp75, the human b (Brown) locus product
    • 2-s2.0-0026051621 10.1016/0014-4827(91)90256-T
    • Vijayasaradhi S., Doskoch P. M., Houghton A. N., Biosynthesis and intracellular movement of the melanosomal membrane glycoprotein gp75, the human b (Brown) locus product. Experimental Cell Research 1991 196 2 233 240 2-s2.0-0026051621 10.1016/0014-4827(91)90256-T
    • (1991) Experimental Cell Research , vol.196 , Issue.2 , pp. 233-240
    • Vijayasaradhi, S.1    Doskoch, P.M.2    Houghton, A.N.3
  • 6
    • 0025321144 scopus 로고
    • Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity
    • 2-s2.0-0025321144 10.1073/pnas.87.12.4809
    • Halaban R., Moellmann G., Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proceedings of the National Academy of Sciences of the United States of America 1990 87 12 4809 4813 2-s2.0-0025321144 10.1073/pnas.87.12.4809
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.12 , pp. 4809-4813
    • Halaban, R.1    Moellmann, G.2
  • 8
    • 0023068990 scopus 로고
    • Mammalian monophenol monooxygenase (tyrosinase): Purification, properties, and reactions catalyzed
    • 2-s2.0-0023068990
    • Hearing V. J. Jr., Mammalian monophenol monooxygenase (tyrosinase): purification, properties, and reactions catalyzed. Methods in Enzymology 1987 142 154 165 2-s2.0-0023068990
    • (1987) Methods in Enzymology , vol.142 , pp. 154-165
    • Hearing, Jr.V.J.1
  • 9
    • 0023754652 scopus 로고
    • Some new aspects of eumelanin chemistry
    • 2-s2.0-0023754652
    • Prota G., Some new aspects of eumelanin chemistry. Progress in Clinical and Biological Research 1988 256 101 124 2-s2.0-0023754652
    • (1988) Progress in Clinical and Biological Research , vol.256 , pp. 101-124
    • Prota, G.1
  • 11
    • 0037902622 scopus 로고    scopus 로고
    • A chemist's view of melanogenesis
    • 2-s2.0-0037902622 10.1034/j.1600-0749.2003.00037.x
    • Ito S., A chemist's view of melanogenesis. Pigment Cell Research 2003 16 3 230 236 2-s2.0-0037902622 10.1034/j.1600-0749.2003.00037.x
    • (2003) Pigment Cell Research , vol.16 , Issue.3 , pp. 230-236
    • Ito, S.1
  • 12
    • 0028180488 scopus 로고
    • A new enzymatic function in the melanogenic pathway. The 5,6- dihydroxyindole-2-carboxylic acid oxidase activity of tyrosinase-related protein-1 (TRP1)
    • 2-s2.0-0028180488
    • Jiménez-Cervantes C., Solano F., Kobayashi T., Urabe K., Hearing V. J., Lozano J. A., Garcia-Borron J. C., A new enzymatic function in the melanogenic pathway. The 5,6- dihydroxyindole-2-carboxylic acid oxidase activity of tyrosinase-related protein-1 (TRP1). The Journal of Biological Chemistry 1994 269 27 17993 18000 2-s2.0-0028180488
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.27 , pp. 17993-18000
    • Jiménez-Cervantes, C.1    Solano, F.2    Kobayashi, T.3    Urabe, K.4    Hearing, V.J.5    Lozano, J.A.6    Garcia-Borron, J.C.7
  • 14
    • 0029031626 scopus 로고
    • Modulation of melanogenic protein expression during the switch from eu- to pheomelanogenesis
    • 2-s2.0-0029031626
    • Kobayashi T., Vieira W. D., Potterf B., Sakai C., Imokawa G., Hearing V. J., Modulation of melanogenic protein expression during the switch from eu- to pheomelanogenesis. Journal of Cell Science 1995 108 6 2301 2309 2-s2.0-0029031626
    • (1995) Journal of Cell Science , vol.108 , Issue.6 , pp. 2301-2309
    • Kobayashi, T.1    Vieira, W.D.2    Potterf, B.3    Sakai, C.4    Imokawa, G.5    Hearing, V.J.6
  • 15
    • 0033610797 scopus 로고    scopus 로고
    • Tyrosinase stabilization by Tyrp1 (the brown locus protein)
    • 2-s2.0-0033610797 10.1074/jbc.273.48.31801
    • Kobayashi T., Imokawa G., Bennett D. C., Hearing V. J., Tyrosinase stabilization by Tyrp1 (the brown locus protein). The Journal of Biological Chemistry 1999 273 48 31801 31805 2-s2.0-0033610797 10.1074/jbc.273.48.31801
    • (1999) The Journal of Biological Chemistry , vol.273 , Issue.48 , pp. 31801-31805
    • Kobayashi, T.1    Imokawa, G.2    Bennett, D.C.3    Hearing, V.J.4
  • 16
    • 0033146457 scopus 로고    scopus 로고
    • Genetic and epigenetic control of the proliferation and differentiation of mouse epidermal melanocytes in culture
    • 2-s2.0-0033146457
    • Hirobe T., Abe H., Genetic and epigenetic control of the proliferation and differentiation of mouse epidermal melanocytes in culture. Pigment Cell Research 1999 12 3 147 163 2-s2.0-0033146457
    • (1999) Pigment Cell Research , vol.12 , Issue.3 , pp. 147-163
    • Hirobe, T.1    Abe, H.2
  • 17
    • 0026879472 scopus 로고
    • Light is a dominant mouse mutation resulting in premature cell death
    • 2-s2.0-0026879472
    • Johnson R., Jackson I. J., Light is a dominant mouse mutation resulting in premature cell death. Nature Genetics 1992 1 3 226 229 2-s2.0-0026879472
    • (1992) Nature Genetics , vol.1 , Issue.3 , pp. 226-229
    • Johnson, R.1    Jackson, I.J.2
  • 18
    • 0037100610 scopus 로고    scopus 로고
    • Selective down-regulation of tyrosinase family gene TYRP1 by inhibition of the activity of melanocyte transcription factor, MITF
    • 2-s2.0-0037100610
    • Fang D., Tsuji Y., Setaluri V., Selective down-regulation of tyrosinase family gene TYRP1 by inhibition of the activity of melanocyte transcription factor, MITF. Nucleic Acids Research 2002 30 14 3096 3106 2-s2.0-0037100610
    • (2002) Nucleic Acids Research , vol.30 , Issue.14 , pp. 3096-3106
    • Fang, D.1    Tsuji, Y.2    Setaluri, V.3
  • 19
    • 0035542883 scopus 로고    scopus 로고
    • Tyrp1 and oculocutaneous albinism type 3
    • 2-s2.0-0035542883 10.1034/j.1600-0749.2001.140603.x
    • Sarangarajan R., Boissy R. E., Tyrp1 and oculocutaneous albinism type 3. Pigment Cell Research 2001 14 6 437 444 2-s2.0-0035542883 10.1034/j.1600-0749. 2001.140603.x
    • (2001) Pigment Cell Research , vol.14 , Issue.6 , pp. 437-444
    • Sarangarajan, R.1    Boissy, R.E.2
  • 20
    • 0031690595 scopus 로고    scopus 로고
    • Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1
    • 2-s2.0-0031690595
    • Boissy R. E., Sakai C., Zhao H., Kobayashi T., Hearing V. J., Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1. Experimental Dermatology 1998 7 4 198 204 2-s2.0-0031690595
    • (1998) Experimental Dermatology , vol.7 , Issue.4 , pp. 198-204
    • Boissy, R.E.1    Sakai, C.2    Zhao, H.3    Kobayashi, T.4    Hearing, V.J.5
  • 21
    • 0028452014 scopus 로고
    • Human TRP-1 has tyrosine hydroxylase but no dopa oxidase activity
    • 2-s2.0-0028452014
    • Zhao H., Zhao Y., Nordlund J. J., Boissy R. E., Human TRP-1 has tyrosine hydroxylase but no dopa oxidase activity. Pigment Cell Research 1994 7 3 131 140 2-s2.0-0028452014
    • (1994) Pigment Cell Research , vol.7 , Issue.3 , pp. 131-140
    • Zhao, H.1    Zhao, Y.2    Nordlund, J.J.3    Boissy, R.E.4
  • 22
    • 0027639444 scopus 로고
    • From gene to protein: Determination of melanin synthesis
    • 2-s2.0-0027639444
    • Urabe K., Aroca P., Hearing V. J., From gene to protein: determination of melanin synthesis. Pigment Cell Research 1993 6 4 186 192 2-s2.0-0027639444
    • (1993) Pigment Cell Research , vol.6 , Issue.4 , pp. 186-192
    • Urabe, K.1    Aroca, P.2    Hearing, V.J.3
  • 23
    • 0035865591 scopus 로고    scopus 로고
    • The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase
    • 2-s2.0-0035865591 10.1042/0264-6021:3540131
    • Olivares C., Jiménez-Cervantes C., Lozano J. A., Solano F., García-Borrón J. C., The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase. Biochemical Journal 2001 354 1 131 139 2-s2.0-0035865591 10.1042/0264-6021:3540131
    • (2001) Biochemical Journal , vol.354 , Issue.1 , pp. 131-139
    • Olivares, C.1    Jiménez-Cervantes, C.2    Lozano, J.A.3    Solano, F.4    García-Borrón, J.C.5
  • 24
    • 0033815702 scopus 로고    scopus 로고
    • Mutational analysis of the modulation of tyrosinase by tyrosinase-related proteins 1 and 2 in vitro
    • 2-s2.0-0033815702 10.1034/j.1600-0749.2000.130510.x
    • Manga P., Sato K., Ye L., Beermann F., Lynn Lamoreux M., Orlow S. J., Mutational analysis of the modulation of tyrosinase by tyrosinase-related proteins 1 and 2 in vitro. Pigment Cell Research 2000 13 5 364 374 2-s2.0-0033815702 10.1034/j.1600-0749.2000.130510.x
    • (2000) Pigment Cell Research , vol.13 , Issue.5 , pp. 364-374
    • Manga, P.1    Sato, K.2    Ye, L.3    Beermann, F.4    Lynn Lamoreux, M.5    Orlow, S.J.6
  • 27
    • 4544336084 scopus 로고    scopus 로고
    • Integrated evaluation of DNA sequence variants of unknown clinical significance: Application to BRCA1 and BRCA2
    • 2-s2.0-4544336084 10.1086/424388
    • Goldgar D. E., Easton D. F., Deffenbaugh A. M., Monteiro A. N. A., Tavtigian S. V., Couch F. J., Integrated evaluation of DNA sequence variants of unknown clinical significance: application to BRCA1 and BRCA2. American Journal of Human Genetics 2004 75 4 535 544 2-s2.0-4544336084 10.1086/424388
    • (2004) American Journal of Human Genetics , vol.75 , Issue.4 , pp. 535-544
    • Goldgar, D.E.1    Easton, D.F.2    Deffenbaugh, A.M.3    Monteiro, A.N.A.4    Tavtigian, S.V.5    Couch, F.J.6
  • 28
    • 60749104999 scopus 로고    scopus 로고
    • Next generation tools for the annotation of human SNPs
    • 2-s2.0-60749104999 10.1093/bib/bbn047
    • Karchin R., Next generation tools for the annotation of human SNPs. Briefings in Bioinformatics 2009 10 1 35 52 2-s2.0-60749104999 10.1093/bib/bbn047
    • (2009) Briefings in Bioinformatics , vol.10 , Issue.1 , pp. 35-52
    • Karchin, R.1
  • 29
    • 84872379319 scopus 로고    scopus 로고
    • Mutational analysis of TYR gene and its structural consequences in OCA1A
    • Balu K., Purohit R., Mutational analysis of TYR gene and its structural consequences in OCA1A. Gene 2013 513 1 184 195
    • (2013) Gene , vol.513 , Issue.1 , pp. 184-195
    • Balu, K.1    Purohit, R.2
  • 30
    • 79958089433 scopus 로고    scopus 로고
    • Relationship between mutation of serine residue at 315th position in M. tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: An in silico analysis
    • 2-s2.0-79958089433 10.1007/s00894-010-0785-6
    • Purohit R., Rajendran V., Sethumadhavan R., Relationship between mutation of serine residue at 315th position in M. tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: an in silico analysis. Journal of Molecular Modeling 2011 17 4 869 877 2-s2.0-79958089433 10.1007/s00894-010-0785-6
    • (2011) Journal of Molecular Modeling , vol.17 , Issue.4 , pp. 869-877
    • Purohit, R.1    Rajendran, V.2    Sethumadhavan, R.3
  • 31
    • 79959449643 scopus 로고    scopus 로고
    • Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants
    • 2-s2.0-79959449643
    • Purohit R., Rajendran V., Sethumadhavan R., Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants. Journal of Biomolecular Structure and Dynamics 2011 29 1 137 152 2-s2.0-79959449643
    • (2011) Journal of Biomolecular Structure and Dynamics , vol.29 , Issue.1 , pp. 137-152
    • Purohit, R.1    Rajendran, V.2    Sethumadhavan, R.3
  • 32
    • 84867464864 scopus 로고    scopus 로고
    • In silico prediction of a disease-associated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ)
    • 10.1016/j.fob.2012.09.003
    • Kumar A., Rajendran V., Sethumadhavan R., Purohit R., In silico prediction of a disease-associated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ). FEBS Open Biology 2012 2 285 293 10.1016/j.fob.2012.09.003
    • (2012) FEBS Open Biology , vol.2 , pp. 285-293
    • Kumar, A.1    Rajendran, V.2    Sethumadhavan, R.3    Purohit, R.4
  • 33
    • 84892966839 scopus 로고    scopus 로고
    • Relationship between a point mutation S97C in CK1 δ protein and its affect on ATP-binding affinity
    • 10.1080/07391102.2013.770373
    • Kumar A., Rajendran V., Sethumadhavan R., Purohit R., Relationship between a point mutation S97C in CK1 δ protein and its affect on ATP-binding affinity. Journal of Biomolecular Structure & Dynamics 2013 10.1080/07391102.2013.770373
    • (2013) Journal of Biomolecular Structure & Dynamics
    • Kumar, A.1    Rajendran, V.2    Sethumadhavan, R.3    Purohit, R.4
  • 35
    • 84864771186 scopus 로고    scopus 로고
    • In silico investigation of molecular mechanism of laminopathy caused by a point mutation (R482W) in lamin A/C protein
    • 2-s2.0-80053579648 10.1007/s00726-011-1108-7
    • Rajendran V., Purohit R., Sethumadhavan R., In silico investigation of molecular mechanism of laminopathy caused by a point mutation (R482W) in lamin A/C protein. Amino Acids 2012 43 2 603 615 2-s2.0-80053579648 10.1007/s00726-011-1108-7
    • (2012) Amino Acids , vol.43 , Issue.2 , pp. 603-615
    • Rajendran, V.1    Purohit, R.2    Sethumadhavan, R.3
  • 36
    • 84883652794 scopus 로고    scopus 로고
    • In-silico analysis of Betaine Aldehyde Dehydrogenase2 of Oryza sativa and significant mutations responsible for fragrance
    • 10.1080/17429145.2012.758785
    • Balu K., Purohit R., In-silico analysis of Betaine Aldehyde Dehydrogenase2 of Oryza sativa and significant mutations responsible for fragrance. Journal of Plant Interactions 2012 1 13 10.1080/17429145.2012.758785
    • (2012) Journal of Plant Interactions , pp. 1-13
    • Balu, K.1    Purohit, R.2
  • 37
    • 84887212608 scopus 로고    scopus 로고
    • Investigation of binding phenomenon of NSP3 and p130Cas mutants and their effect on cell signalling
    • 10.1007/s12013-013-9551-6
    • Balu K., Rajendran V., Sethumadhavan R., Purohit R., Investigation of binding phenomenon of NSP3 and p130Cas mutants and their effect on cell signalling. Cell Biochemistry and Biophysics 2013 1 11 10.1007/s12013-013-9551-6
    • (2013) Cell Biochemistry and Biophysics , pp. 1-11
    • Balu, K.1    Rajendran, V.2    Sethumadhavan, R.3    Purohit, R.4
  • 39
    • 68149165614 scopus 로고    scopus 로고
    • Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm
    • 2-s2.0-68149165614 10.1038/nprot.2009.86
    • Kumar P., Henikoff S., Ng P. C., Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm. Nature Protocols 2009 4 7 1073 1082 2-s2.0-68149165614 10.1038/nprot.2009.86
    • (2009) Nature Protocols , vol.4 , Issue.7 , pp. 1073-1082
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 40
    • 43349096923 scopus 로고    scopus 로고
    • A three-state prediction of single point mutations on protein stability changes
    • 2-s2.0-43349096923 10.1186/1471-2105-9-S2-S6
    • Capriotti E., Fariselli P., Rossi I., Casadio R., A three-state prediction of single point mutations on protein stability changes. BMC Bioinformatics 2008 9 2, article S6 2-s2.0-43349096923 10.1186/1471-2105-9-S2-S6
    • (2008) BMC Bioinformatics , vol.9 , Issue.2 ARTICLE S6
    • Capriotti, E.1    Fariselli, P.2    Rossi, I.3    Casadio, R.4
  • 42
    • 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
    • 2-s2.0-33751013750 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 22 2729 2734 2-s2.0-33751013750 10.1093/bioinformatics/btl423
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2729-2734
    • Capriotti, E.1    Calabrese, R.2    Casadio, R.3
  • 43
    • 67749137351 scopus 로고    scopus 로고
    • Functional annotations improve the predictive score of human disease-related mutations in proteins
    • 2-s2.0-67749137351 10.1002/humu.21047
    • Calabrese R., Capriotti E., Fariselli P., Martelli P. L., Casadio R., Functional annotations improve the predictive score of human disease-related mutations in proteins. Human Mutation 2009 30 8 1237 1244 2-s2.0-67749137351 10.1002/humu.21047
    • (2009) Human Mutation , vol.30 , Issue.8 , pp. 1237-1244
    • Calabrese, R.1    Capriotti, E.2    Fariselli, P.3    Martelli, P.L.4    Casadio, R.5
  • 44
    • 25144496606 scopus 로고    scopus 로고
    • PMUT: A web-based tool for the annotation of pathological mutations on proteins
    • 2-s2.0-25144496606 10.1093/bioinformatics/bti486
    • Ferrer-Costa C., Gelpí J. L., Zamakola L., Parraga I., de la Cruz X., Orozco M., PMUT: a web-based tool for the annotation of pathological mutations on proteins. Bioinformatics 2005 21 14 3176 3178 2-s2.0-25144496606 10.1093/bioinformatics/bti486
    • (2005) Bioinformatics , vol.21 , Issue.14 , pp. 3176-3178
    • Ferrer-Costa, C.1    Gelpí, J.L.2    Zamakola, L.3    Parraga, I.4    De La Cruz, X.5    Orozco, M.6
  • 45
    • 70350671733 scopus 로고    scopus 로고
    • Automated inference of molecular mechanisms of disease from amino acid substitutions
    • 2-s2.0-70350671733 10.1093/bioinformatics/btp528
    • Li B., Krishnan V. G., Mort M. E., Xin F., Kamati K. K., Cooper D. N., Mooney S. D., Radivojac P., Automated inference of molecular mechanisms of disease from amino acid substitutions. Bioinformatics 2009 25 21 2744 2750 2-s2.0-70350671733 10.1093/bioinformatics/btp528
    • (2009) Bioinformatics , vol.25 , Issue.21 , pp. 2744-2750
    • Li, B.1    Krishnan, V.G.2    Mort, M.E.3    Xin, F.4    Kamati, K.K.5    Cooper, D.N.6    Mooney, S.D.7    Radivojac, P.8
  • 46
    • 58149189856 scopus 로고    scopus 로고
    • McKusick's Online Mendelian Inheritance in Man (OMIM®)
    • 2-s2.0-58149189856 10.1093/nar/gkn665
    • Amberger J., Bocchini C. A., Scott A. F., Hamosh A., McKusick's Online Mendelian Inheritance in Man (OMIM®). Nucleic Acids Research 2009 37 1 D793 D796 2-s2.0-58149189856 10.1093/nar/gkn665
    • (2009) Nucleic Acids Research , vol.37 , Issue.1
    • Amberger, J.1    Bocchini, C.A.2    Scott, A.F.3    Hamosh, A.4
  • 48
    • 2342596530 scopus 로고    scopus 로고
    • The Swiss-Prot variant page and the ModSNP database: A resource for sequence and structure information on human protein variants
    • 2-s2.0-2342596530 10.1002/humu.20021
    • Yip Y. L., Scheib H., Diemand A. V., Gattiker A., Famiglietti L. M., Gasteiger E., Bairoch A., The Swiss-Prot variant page and the ModSNP database: a resource for sequence and structure information on human protein variants. Human Mutation 2004 23 5 464 470 2-s2.0-2342596530 10.1002/humu.20021
    • (2004) Human Mutation , vol.23 , Issue.5 , pp. 464-470
    • Yip, Y.L.1    Scheib, H.2    Diemand, A.V.3    Gattiker, A.4    Famiglietti, L.M.5    Gasteiger, E.6    Bairoch, A.7
  • 49
    • 40549095676 scopus 로고    scopus 로고
    • Annotating single amino acid polymorphisms in the UniProt/Swiss-Prot knowledgebase
    • 2-s2.0-40549095676 10.1002/humu.20671
    • Yip Y. L., Famiglietti M., Gos A., Duek P. D., David F. P. A., Gateau A., Bairoch A., Annotating single amino acid polymorphisms in the UniProt/Swiss-Prot knowledgebase. Human Mutation 2008 29 3 361 366 2-s2.0-40549095676 10.1002/humu.20671
    • (2008) Human Mutation , vol.29 , Issue.3 , pp. 361-366
    • Yip, Y.L.1    Famiglietti, M.2    Gos, A.3    Duek, P.D.4    David, F.P.A.5    Gateau, A.6    Bairoch, A.7
  • 51
    • 0035346185 scopus 로고    scopus 로고
    • Swiss-PDB viewer (Deep View)
    • 2-s2.0-0035346185
    • Kaplan W., Littlejohn T. G., Swiss-PDB viewer (Deep View). Briefings in Bioinformatics 2001 2 2 195 197 2-s2.0-0035346185
    • (2001) Briefings in Bioinformatics , vol.2 , Issue.2 , pp. 195-197
    • Kaplan, W.1    Littlejohn, T.G.2
  • 52
    • 46249092554 scopus 로고    scopus 로고
    • GRGMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • 2-s2.0-46249092554 10.1021/ct700301q
    • Hess B., Kutzner C., van der Spoel D., Lindahl E., GRGMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. Journal of Chemical Theory and Computation 2008 4 3 435 447 2-s2.0-46249092554 10.1021/ct700301q
    • (2008) Journal of Chemical Theory and Computation , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 53
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • 2-s2.0-39449115394 10.1186/1471-2105-9-40
    • Zhang Y., I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008 9, article 40 2-s2.0-39449115394 10.1186/1471-2105-9-40
    • (2008) BMC Bioinformatics , vol.940
    • Zhang, Y.1
  • 54
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • 2-s2.0-0030339738
    • Laskowski R. A., Rullmann J. A. C., MacArthur M. W., Kaptein R., Thornton J. M., AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. Journal of Biomolecular NMR 1996 8 4 477 486 2-s2.0-0030339738
    • (1996) Journal of Biomolecular NMR , vol.8 , Issue.4 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 55
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 2-s2.0-34547566446 10.1093/nar/gkm290
    • Wiederstein M., Sippl M. J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Research 2007 35 W407 W410 2-s2.0-34547566446 10.1093/nar/gkm290
    • (2007) Nucleic Acids Research , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 57
    • 0029170114 scopus 로고
    • Molecular dynamics simulations on solvated biomolecular systems: The particle mesh Ewald method leads to stable trajectories of DNA, RNA, and proteins
    • 2-s2.0-0029170114
    • Cheatham T. E. III, Miller J. L., Fox T., Darden T. A., Kollman P. A., Molecular dynamics simulations on solvated biomolecular systems: the particle mesh Ewald method leads to stable trajectories of DNA, RNA, and proteins. Journal of the American Chemical Society 1995 117 14 4193 4194 2-s2.0-0029170114
    • (1995) Journal of the American Chemical Society , vol.117 , Issue.14 , pp. 4193-4194
    • Iii, E.C.T.1    Miller, J.L.2    Fox, T.3    Darden, T.A.4    Kollman, P.A.5
  • 58
    • 33845430353 scopus 로고    scopus 로고
    • Beaverton, Ore, USA Center For Coastal and Land-Margin Research, Oregon Graduate Institute of Science and Technology
    • Turner P. J., XMGRACE, Version 5.1.19 2005 Beaverton, Ore, USA Center For Coastal and Land-Margin Research, Oregon Graduate Institute of Science and Technology
    • (2005) XMGRACE, Version 5.1.19
    • Turner, P.J.1
  • 60
    • 65649108490 scopus 로고    scopus 로고
    • Pathogenic or not? and if so, then how? Studying the effects of missense mutations using bioinformatics methods
    • 2-s2.0-65649108490 10.1002/humu.20938
    • Thusberg J., Vihinen M., Pathogenic or not? and if so, then how? Studying the effects of missense mutations using bioinformatics methods. Human Mutation 2009 30 5 703 714 2-s2.0-65649108490 10.1002/humu.20938
    • (2009) Human Mutation , vol.30 , Issue.5 , pp. 703-714
    • Thusberg, J.1    Vihinen, M.2
  • 61
    • 79957621519 scopus 로고    scopus 로고
    • Prediction of missense mutation functionality depends on both the algorithm and sequence alignment employed
    • 2-s2.0-79957621519 10.1002/humu.21490
    • Hicks S., Wheeler D. A., Plon S. E., Kimmel M., Prediction of missense mutation functionality depends on both the algorithm and sequence alignment employed. Human Mutation 2011 32 6 661 668 2-s2.0-79957621519 10.1002/humu.21490
    • (2011) Human Mutation , vol.32 , Issue.6 , pp. 661-668
    • Hicks, S.1    Wheeler, D.A.2    Plon, S.E.3    Kimmel, M.4
  • 62
    • 81155134049 scopus 로고    scopus 로고
    • Oculocutaneous Albinism type 3 (OCA3): Analysis of two novel mutations in TYRP1 gene in two Chinese patients
    • 2-s2.0-81155134049 10.1007/s12013-011-9234-0
    • Zhang K.-H., Li Z., Lei J., Pang T., Xu B., Jiang W.-Y., Li H.-Y., Oculocutaneous Albinism type 3 (OCA3): analysis of two novel mutations in TYRP1 gene in two Chinese patients. Cell Biochemistry and Biophysics 2011 61 3 523 529 2-s2.0-81155134049 10.1007/s12013-011-9234-0
    • (2011) Cell Biochemistry and Biophysics , vol.61 , Issue.3 , pp. 523-529
    • Zhang, K.-H.1    Li, Z.2    Lei, J.3    Pang, T.4    Xu, B.5    Jiang, W.-Y.6    Li, H.-Y.7
  • 63
    • 6344223617 scopus 로고    scopus 로고
    • A flexible approach for understanding protein stability
    • 2-s2.0-6344223617 10.1016/j.febslet.2004.09.057
    • Livesay D. R., Dallakyan S., Wood G. G., Jacobs D. J., A flexible approach for understanding protein stability. FEBS Letters 2004 576 3 468 476 2-s2.0-6344223617 10.1016/j.febslet.2004.09.057
    • (2004) FEBS Letters , vol.576 , Issue.3 , pp. 468-476
    • Livesay, D.R.1    Dallakyan, S.2    Wood, G.G.3    Jacobs, D.J.4
  • 64
    • 84861149876 scopus 로고    scopus 로고
    • Changes in lysozyme flexibility upon mutation are frequent, large and long-ranged
    • 100240
    • Verma D., Jacobs D. J., Livesay D. R., Changes in lysozyme flexibility upon mutation are frequent, large and long-ranged. PLoS Computational Biology 2012 8 3 100240
    • (2012) PLoS Computational Biology , vol.8 , Issue.3
    • Verma, D.1    Jacobs, D.J.2    Livesay, D.R.3
  • 66
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • 2-s2.0-0020997912
    • Kabsch W., Sander C., Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983 22 12 2577 2637 2-s2.0-0020997912
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 67
    • 84878135768 scopus 로고    scopus 로고
    • DNA variations in oculocutaneous Albinism: An updated mutation List and current outstanding issues in molecular diagnostics
    • 10.1002/humu.22315
    • Simeonov D. R., Wang X., Wang C., DNA variations in oculocutaneous Albinism: an updated mutation List and current outstanding issues in molecular diagnostics. Human Mutation 2013 34 6 827 835 10.1002/humu.22315
    • (2013) Human Mutation , vol.34 , Issue.6 , pp. 827-835
    • Simeonov, D.R.1    Wang, X.2    Wang, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.