메뉴 건너뛰기




Volumn 33, Issue 8, 2015, Pages 1695-1709

Tryptophan to Glycine mutation in the position 116 leads to protein aggregation and decreases the stability of the LITAF protein

Author keywords

Charcot Marie Tooth disease; lipopolysaccharide induced TNF factor protein; molecular dynamics simulations; protein aggregation; SNP analysis

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; GLYCINE; LIPOPOLYSACCHARIDE INDUCED TUMOR NECROSIS FACTOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; TRYPTOPHAN; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; CODON; LITAF PROTEIN, HUMAN; NUCLEAR PROTEIN; TRANSCRIPTION FACTOR;

EID: 84930572258     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2014.968211     Document Type: Article
Times cited : (6)

References (57)
  • 4
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • B. Pullman (Ed.), Dordrecht: D. Riedel
    • Berendsen, H. J. C., Postma, J. P. M., Gunsteren, W. F. V., & Hermans, J. (1981). Interaction models for water in relation to protein hydration. In B. Pullman (Ed.), Intermolecular forces (pp. 331-342). Dordrecht: D. Riedel.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Gunsteren, W.F.V.3    Hermans, J.4
  • 5
    • 0017648231 scopus 로고
    • Peroneal muscular atrophy (PMA) and related disorders
    • Buchthal, F., & Behse, F. (1977). Peroneal muscular atrophy (PMA) and related disorders. Brain, 100, 41-66.
    • (1977) Brain , vol.100 , pp. 41-66
    • Buchthal, F.1    Behse, F.2
  • 6
    • 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, P. L., & Casadio, R. (2009). Functional annotations improve the predictive score of human disease-related mutations in proteins. Human Mutation, 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
  • 8
    • 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. (2008). A three state prediction of single point mutations on protein stability changes. BMC Bioinformatics, 9, S6.
    • (2008) BMC Bioinformatics , vol.9 , pp. S6
    • Capriotti, E.1    Fariselli, P.2    Rossi, I.3    Casadio, R.4
  • 11
    • 61549094352 scopus 로고    scopus 로고
    • Computational modeling of structurally conserved cancer mutations in the RET and MET kinases: The impact on protein structure, dynamics, and stability
    • Dixit, A., Torkamani, A., Schork, N. J., & Verkhivker, G. (2009). Computational modeling of structurally conserved cancer mutations in the RET and MET kinases: The impact on protein structure, dynamics, and stability. Biophysical Journal, 96, 858-874.
    • (2009) Biophysical Journal , vol.96 , pp. 858-874
    • Dixit, A.1    Torkamani, A.2    Schork, N.J.3    Verkhivker, G.4
  • 12
    • 0014301249 scopus 로고
    • Lower motor and primary sensory neuron diseases with peroneal muscular atrophy
    • Dyck, P. J., & Lambert, E. H. (1968). Lower motor and primary sensory neuron diseases with peroneal muscular atrophy. Archives of Neurology, 18, 603-618.
    • (1968) Archives of Neurology , vol.18 , pp. 603-618
    • Dyck, P.J.1    Lambert, E.H.2
  • 15
    • 70349257316 scopus 로고    scopus 로고
    • Hereditary motor and sensory neuropathy caused by a novel mutation in LITAF
    • Gerding, W. M., Koetting, J., Epplen, J. T., & Neusch, C. (2009). Hereditary motor and sensory neuropathy caused by a novel mutation in LITAF. Neuromuscular Disorders, 19, 701-703.
    • (2009) Neuromuscular Disorders , vol.19 , pp. 701-703
    • Gerding, W.M.1    Koetting, J.2    Epplen, J.T.3    Neusch, C.4
  • 17
    • 33645519597 scopus 로고    scopus 로고
    • A role for direct interactions in the modulation of rhodopsin by ω-3 polyunsaturated lipids
    • Grossfield, A., Feller, S. E., & Pitman, M. C. (2006). A role for direct interactions in the modulation of rhodopsin by ω-3 polyunsaturated lipids. Proceedings of the National Academy of Sciences, 103, 4888-4893.
    • (2006) Proceedings of the National Academy of Sciences , vol.103 , pp. 4888-4893
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 19
  • 21
    • 83655169803 scopus 로고    scopus 로고
    • Influence of the pathogenic mutations T188K/R/A on the structural stability and misfolding of human prion protein: Insight from molecular dynamics simulations
    • Guo, J., Ning, L., Ren, H., Liu, H., & Yao, X. (2012). Influence of the pathogenic mutations T188K/R/A on the structural stability and misfolding of human prion protein: Insight from molecular dynamics simulations. Biochimica et Biophysica Acta (BBA) - General Subjects, 1820, 116-123.
    • (2012) Biochimica et Biophysica Acta (BBA) - General Subjects , vol.1820 , pp. 116-123
    • Guo, J.1    Ning, L.2    Ren, H.3    Liu, H.4    Yao, X.5
  • 22
    • 0018942439 scopus 로고
    • The clinical features of hereditary motor and sensory neuropathy types I and II
    • Harding, A. E., & Thomas, P. K. (1980). The clinical features of hereditary motor and sensory neuropathy types I and II. Brain, 103, 259-280.
    • (1980) Brain , vol.103 , pp. 259-280
    • Harding, A.E.1    Thomas, P.K.2
  • 26
    • 79957621519 scopus 로고    scopus 로고
    • Prediction of missense mutation functionality depends on both the algorithm and sequence alignment employed
    • Hicks, S., Wheeler, D. A., Plon, S. E., & Kimmel, M. (2011). Prediction of missense mutation functionality depends on both the algorithm and sequence alignment employed. Human Mutation, 32, 661-668.
    • (2011) Human Mutation , vol.32 , pp. 661-668
    • Hicks, S.1    Wheeler, D.A.2    Plon, S.E.3    Kimmel, M.4
  • 27
    • 60749104999 scopus 로고    scopus 로고
    • Next generation tools for the annotation of human SNPs
    • Karchin, R. (2009). Next generation tools for the annotation of human SNPs. Briefings in Bioinformatics, 10, 35-52.
    • (2009) Briefings in Bioinformatics , vol.10 , pp. 35-52
    • Karchin, R.1
  • 29
    • 77957764152 scopus 로고    scopus 로고
    • 2Struc: The secondary structure server
    • Klose, D. P., Wallace, B. A., & Janes, R. W. (2010). 2Struc: The secondary structure server. Bioinformatics, 26, 2624-2625.
    • (2010) Bioinformatics , vol.26 , pp. 2624-2625
    • Klose, D.P.1    Wallace, B.A.2    Janes, R.W.3
  • 30
    • 68149165614 scopus 로고    scopus 로고
    • Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm
    • Kumar, P., Henikoff, S., & Ng, P. C. (2009). Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm. Nature Protocols, 4, 1073-1081.
    • (2009) Nature Protocols , vol.4 , pp. 1073-1081
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 31
    • 0030659457 scopus 로고    scopus 로고
    • PDBsum: A web-based database of summaries and analyses of all PDB structures
    • Laskowski, R. A. (1997). PDBsum: A web-based database of summaries and analyses of all PDB structures. Trends in Biochemical Sciences, 22, 488-490.
    • (1997) Trends in Biochemical Sciences , vol.22 , pp. 488-490
    • Laskowski, R.A.1
  • 33
    • 84871997901 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking
    • Lee, S. M., Chin, L. S., & Li, L. (2012). Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking. Journal of Cell Biology, 199, 799-816.
    • (2012) Journal of Cell Biology , vol.199 , pp. 799-816
    • Lee, S.M.1    Chin, L.S.2    Li, L.3
  • 34
    • 80054037232 scopus 로고    scopus 로고
    • Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE protein mislocalization and degradation by the proteasome and aggresome-autophagy pathways
    • Lee, S. M., Olzmann, J. A., Chin, L.-S., & Li, L. (2011). Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE protein mislocalization and degradation by the proteasome and aggresome-autophagy pathways. Journal of Cell Science, 124, 3319-3331.
    • (2011) Journal of Cell Science , vol.124 , pp. 3319-3331
    • Lee, S.M.1    Olzmann, J.A.2    Chin, L.-S.3    Li, L.4
  • 35
    • 70350671733 scopus 로고    scopus 로고
    • Automated inference of molecular mechanisms of disease from amino acid substitutions
    • Li, B., Krishnan, V. G., Mort, M. E., Xin, F., Kamati, K. K., Cooper, D. N., ⋯ Radivojac, P. (2009). Automated inference of molecular mechanisms of disease from amino acid substitutions. Bioinformatics, 25, 2744-2750.
    • (2009) Bioinformatics , vol.25 , 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    Radivojac, P.7
  • 36
    • 0031892597 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease: Lessons in genetic mechanisms
    • Lupski, J. R. (1998). Charcot-Marie-Tooth disease: Lessons in genetic mechanisms. Molecular Medicine, 4, 3-11.
    • (1998) Molecular Medicine , vol.4 , pp. 3-11
    • Lupski, J.R.1
  • 38
    • 0026879838 scopus 로고
    • Peripheral myelin protein-22 gene maps in the duplication in chromosome 17p11.2 associated with Charcot-Marie-Tooth 1A
    • Matsunami, N., Smith, B., Ballard, L., William Lensch, M., Robertson, M., Albertsen, H., ⋯ Chance, P. F. (1992). Peripheral myelin protein-22 gene maps in the duplication in chromosome 17p11.2 associated with Charcot-Marie-Tooth 1A. Nature Genetics, 1, 176-179.
    • (1992) Nature Genetics , vol.1 , pp. 176-179
    • Matsunami, N.1    Smith, B.2    Ballard, L.3    William Lensch, M.4    Robertson, M.5    Albertsen, H.6    Chance, P.F.7
  • 39
    • 0035933717 scopus 로고    scopus 로고
    • Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET- 1
    • Moriwaki, Y., Begum, N. A., Kobayashi, M., Matsumoto, M., Toyoshima, K., & Seya, T. (2001). Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET- 1. Journal of Biological Chemistry, 276, 23065-23076.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 23065-23076
    • Moriwaki, Y.1    Begum, N.A.2    Kobayashi, M.3    Matsumoto, M.4    Toyoshima, K.5    Seya, T.6
  • 40
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS forcefield parameter sets 53A5 and 53A6
    • Oostenbrink, C., Villa, A., Mark, A. E., & Gunsteren, W. F. V. (2004). A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS forcefield parameter sets 53A5 and 53A6. Journal of Computational Chemistry, 25, 1656-1676.
    • (2004) Journal of Computational Chemistry , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Gunsteren, W.F.V.4
  • 41
    • 0026879614 scopus 로고
    • The gene for the peripheral myelin protein PMP-22 is a candidate for Charcot-Marie-Tooth disease type 1A
    • Patel, P. I., Roa, B. B., Welcher, A. A., Schoener-Scott, R., Trask, B. J., Pentao, L., ⋯ Suter, U. (1992). The gene for the peripheral myelin protein PMP-22 is a candidate for Charcot-Marie-Tooth disease type 1A. Nature Genetics, 1, 159-165.
    • (1992) Nature Genetics , vol.1 , pp. 159-165
    • Patel, P.I.1    Roa, B.B.2    Welcher, A.A.3    Schoener-Scott, R.4    Trask, B.J.5    Pentao, L.6    Suter, U.7
  • 46
    • 0016266593 scopus 로고
    • Genetic and clinical aspects of Charcot-Marie-Tooth's disease
    • Skre, H. (1974). Genetic and clinical aspects of Charcot-Marie-Tooth's disease. Clinical Genetics, 6, 98-118.
    • (1974) Clinical Genetics , vol.6 , pp. 98-118
    • Skre, H.1
  • 47
    • 0037435540 scopus 로고    scopus 로고
    • Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-Marie-Tooth disease 1C
    • Street, V. A., Bennett, C. L., Goldy, J. D., Shirk, A. J., Kleopa, K. A., Tempel, B. L., ⋯ Chance, P. F. (2003). Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-Marie-Tooth disease 1C. Neurology, 60, 22-26.
    • (2003) Neurology , vol.60 , pp. 22-26
    • Street, V.A.1    Bennett, C.L.2    Goldy, J.D.3    Shirk, A.J.4    Kleopa, K.A.5    Tempel, B.L.6    Chance, P.F.7
  • 48
    • 65649108490 scopus 로고    scopus 로고
    • Pathogenic or not? And if so, then how? Studying the effects of missense mutations using bioinformatics methods
    • Thusberg, J., & Vihinen, M. (2009). Pathogenic or not? and if so, then how? Studying the effects of missense mutations using bioinformatics methods. Human Mutation, 30, 703-714.
    • (2009) Human Mutation , vol.30 , pp. 703-714
    • Thusberg, J.1    Vihinen, M.2
  • 49
    • 0026879615 scopus 로고
    • The peripheral myelin protein gene PMP-22 is contained within the Charcot-Marie-Tooth disease type 1A duplication
    • Timmerman, V., Nelis, E., Van Hul, W., Nieuwenhuijsen, B. W., Chen, K. L., Wang, S., ⋯ Van Broeckhoven, C. (1992). The peripheral myelin protein gene PMP-22 is contained within the Charcot-Marie-Tooth disease type 1A duplication. Nature Genetics, 1, 171-175.
    • (1992) Nature Genetics , vol.1 , pp. 171-175
    • Timmerman, V.1    Nelis, E.2    Van Hul, W.3    Nieuwenhuijsen, B.W.4    Chen, K.L.5    Wang, S.6    Van Broeckhoven, C.7
  • 50
    • 84874546855 scopus 로고    scopus 로고
    • Version 5.1.19. Beaverton, OR: Central for costal and Land-Margin Research; Oregon Graduate Institute of Science and Technology
    • Turner, P. J. (2005). XMGRACE, Version 5.1.19. Beaverton, OR: Central for costal and Land-Margin Research; Oregon Graduate Institute of Science and Technology.
    • (2005) XMGRACE
    • Turner, P.J.1
  • 52
    • 84897934338 scopus 로고    scopus 로고
    • Protein aggregation due to nsSNP resulting in P56S VABP protein is associated with amyotrophic lateral sclerosis
    • Vinay Kumar, C., Kumar, K. M., Swetha, R., Ramaiah, S., & Anbarasu, A. (2014). Protein aggregation due to nsSNP resulting in P56S VABP protein is associated with amyotrophic lateral sclerosis. Journal of Theoretical Biology, 354, 72-80.
    • (2014) Journal of Theoretical Biology , vol.354 , pp. 72-80
    • Vinay Kumar, C.1    Kumar, K.M.2    Swetha, R.3    Ramaiah, S.4    Anbarasu, A.5
  • 53
    • 0031943222 scopus 로고    scopus 로고
    • Mutations in the early growth response 2 (EGR2) gene are associated with hereditary myelinopathies
    • Warner, L. E., Mancias, P., Butler, I. J., McDonald, C. M., Keppen, L., Koob, K., & Lupski, J. R. (1998). Mutations in the early growth response 2 (EGR2) gene are associated with hereditary myelinopathies. Nature Genetics, 18, 382-384.
    • (1998) Nature Genetics , vol.18 , pp. 382-384
    • Warner, L.E.1    Mancias, P.2    Butler, I.J.3    McDonald, C.M.4    Keppen, L.5    Koob, K.6    Lupski, J.R.7
  • 54
    • 0029848695 scopus 로고    scopus 로고
    • Absence of-PMP22 coding region mutations in CMT1A duplication patients: Further evidence supporting gene dosage as a mechanism for charcot-marie-tooth disease type 1A
    • Warner, L. E., Roa, B. B., & Lupski, J. R. (1996). Absence of-PMP22 coding region mutations in CMT1A duplication patients: Further evidence supporting gene dosage as a mechanism for charcot-marie-tooth disease type 1A. Human Mutation, 8, 362-365.
    • (1996) Human Mutation , vol.8 , pp. 362-365
    • Warner, L.E.1    Roa, B.B.2    Lupski, J.R.3
  • 55
    • 0035895664 scopus 로고    scopus 로고
    • Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases
    • Waterman, H., & Yarden, Y. (2001). Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases. FEBS Letters, 490, 142-152.
    • (2001) FEBS Letters , vol.490 , pp. 142-152
    • Waterman, H.1    Yarden, Y.2
  • 56
    • 84555202613 scopus 로고    scopus 로고
    • The Trp-cage miniprotein with single-site mutations: Studies of stability and dynamics using molecular dynamics
    • Wu, X., Yang, G., Zu, Y., Fu, Y., Zhou, L., & Yuan, X. (2011). The Trp-cage miniprotein with single-site mutations: Studies of stability and dynamics using molecular dynamics. Computational and Theoretical Chemistry, 973, 1-8.
    • (2011) Computational and Theoretical Chemistry , vol.973 , pp. 1-8
    • Wu, X.1    Yang, G.2    Zu, Y.3    Fu, Y.4    Zhou, L.5    Yuan, X.6
  • 57
    • 81155134049 scopus 로고    scopus 로고
    • Oculocutaneous albinism type 3 (OCA3): Analysis of two novel mutations in TYRP1 gene in two Chinese patients
    • Zhang, K. H., Li, Z., Lei, J., Pang, T., Xu, B., Jiang, W. Y., & Li, H. Y. (2011). Oculocutaneous Albinism type 3 (OCA3): Analysis of two novel mutations in TYRP1 gene in two Chinese patients. Cell Biochemistry and Biophysics, 61, 523-529.
    • (2011) Cell Biochemistry and Biophysics , vol.61 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.