메뉴 건너뛰기




Volumn 20, Issue 2, 2014, Pages 184-191

Maximum-likelihood approaches reveal signatures of positive selection in IL genes in mammals

Author keywords

IL receptors; ILs; maximum likelihood; positive selection

Indexed keywords

INTERLEUKIN 1; INTERLEUKIN 10; INTERLEUKIN 12P35; INTERLEUKIN 12P40; INTERLEUKIN 13; INTERLEUKIN 14; INTERLEUKIN 17; INTERLEUKIN 17B; INTERLEUKIN 17C; INTERLEUKIN 17F; INTERLEUKIN 18; INTERLEUKIN 19; INTERLEUKIN 1ALPHA; INTERLEUKIN 1B; INTERLEUKIN 2; INTERLEUKIN 20; INTERLEUKIN 22; INTERLEUKIN 23; INTERLEUKIN 24; INTERLEUKIN 25; INTERLEUKIN 26; INTERLEUKIN 27A; INTERLEUKIN 27B; INTERLEUKIN 29; INTERLEUKIN 34; INTERLEUKIN 36A; INTERLEUKIN 36G; INTERLEUKIN 4; INTERLEUKIN 5; INTERLEUKIN 6; UNCLASSIFIED DRUG;

EID: 84892774920     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/1753425913486687     Document Type: Article
Times cited : (19)

References (62)
  • 1
    • 27744487611 scopus 로고    scopus 로고
    • Gamma chain receptor interleukins: Evidence for positive selection driving the evolution of cell-to-cell communicators in the mammalian immune system
    • O'Connell MJ, McInerney JO. Gamma chain receptor interleukins: evidence for positive selection driving the evolution of cell-to-cell communicators in the mammalian immune system. J Mol Evol. 2005 ; 61: 608-619
    • (2005) J Mol Evol , vol.61 , pp. 608-619
    • O'Connell, M.J.1    McInerney, J.O.2
  • 2
    • 0033814540 scopus 로고    scopus 로고
    • Fast evolution of interleukin-2 in mammals and positive selection in ruminants
    • Zelus D, Robinson-Rechavi M, Delacre M, et al. Fast evolution of interleukin-2 in mammals and positive selection in ruminants. J Mol Evol. 2000 ; 51: 234-244
    • (2000) J Mol Evol , vol.51 , pp. 234-244
    • Zelus, D.1    Robinson-Rechavi, M.2    Delacre, M.3
  • 4
    • 0033866763 scopus 로고    scopus 로고
    • Positive selection in the evolution of mammalian interleukin-2 genes
    • Zhang J, Nei M. Positive selection in the evolution of mammalian interleukin-2 genes. Mol Biol Evol. 2000 ; 17: 1413-1416
    • (2000) Mol Biol Evol , vol.17 , pp. 1413-1416
    • Zhang, J.1    Nei, M.2
  • 5
    • 79952279446 scopus 로고    scopus 로고
    • Evolutionary divergence and functions of the human interleukin (IL) gene family
    • Brocker C, Thompson D, Matsumoto A, et al. Evolutionary divergence and functions of the human interleukin (IL) gene family. Hum Genomics. 2010 ; 5: 30-55
    • (2010) Hum Genomics , vol.5 , pp. 30-55
    • Brocker, C.1    Thompson, D.2    Matsumoto, A.3
  • 6
    • 68049135942 scopus 로고    scopus 로고
    • Detecting signatures of selection from DNA sequences using Datamonkey
    • Poon AF, Frost SD, Pond SL. Detecting signatures of selection from DNA sequences using Datamonkey. Methods Mol Biol. 2009 ; 537: 163-183
    • (2009) Methods Mol Biol , vol.537 , pp. 163-183
    • Poon, A.F.1    Frost, S.D.2    Pond, S.L.3
  • 7
    • 0037408241 scopus 로고    scopus 로고
    • Interleukin is as interleukin does
    • Schrader JW. Interleukin is as interleukin does. J Immunol Methods. 2003 ; 276: 1-3
    • (2003) J Immunol Methods , vol.276 , pp. 1-3
    • Schrader, J.W.1
  • 8
    • 33745499027 scopus 로고    scopus 로고
    • Regulation of innate and adaptive immune responses by the related cytokines IL-12, IL-23, and IL-27
    • Beadling C, Slifka MK. Regulation of innate and adaptive immune responses by the related cytokines IL-12, IL-23, and IL-27. Arch Immunol Ther Exp (Warsz). 2006 ; 54: 15-24
    • (2006) Arch Immunol Ther Exp (Warsz) , vol.54 , pp. 15-24
    • Beadling, C.1    Slifka, M.K.2
  • 9
    • 79952291528 scopus 로고    scopus 로고
    • Interleukins, from 1 to 37, and interferon-gamma: Receptors, functions, and roles in diseases
    • e1-e70
    • Akdis M, Burgler S, Crameri R, et al. Interleukins, from 1 to 37, and interferon-gamma: receptors, functions, and roles in diseases. J Allergy Clin Immunol. 2011 ; 127: 701-721 e1-e70
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 701-721
    • Akdis, M.1    Burgler, S.2    Crameri, R.3
  • 10
    • 0037119351 scopus 로고    scopus 로고
    • Cytokine and cytokine receptor pleiotropy and redundancy
    • Ozaki K, Leonard WJ. Cytokine and cytokine receptor pleiotropy and redundancy. J Biol Chem. 2002 ; 277: 29355-29358
    • (2002) J Biol Chem , vol.277 , pp. 29355-29358
    • Ozaki, K.1    Leonard, W.J.2
  • 11
  • 12
    • 0041677606 scopus 로고    scopus 로고
    • Principles of interleukin (IL)-6-type cytokine signalling and its regulation
    • Heinrich PC, Behrmann I, Haan S, et al. Principles of interleukin (IL)-6-type cytokine signalling and its regulation. Biochem J. 2003 ; 374: 1-20
    • (2003) Biochem J , vol.374 , pp. 1-20
    • Heinrich, P.C.1    Behrmann, I.2    Haan, S.3
  • 13
    • 0037064539 scopus 로고    scopus 로고
    • Molecular basis of the cell specificity of cytokine action
    • Ishihara K, Hirano T. Molecular basis of the cell specificity of cytokine action. Biochim Biophys Acta. 2002 ; 1592: 281-296
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 281-296
    • Ishihara, K.1    Hirano, T.2
  • 15
    • 76749109317 scopus 로고    scopus 로고
    • Immunologic messenger molecules: Cytokines, interferons, and chemokines
    • Commins SP, Borish L, Steinke JW. Immunologic messenger molecules: cytokines, interferons, and chemokines. J Allergy Clin Immunol. 2010 ; 125: S53 - S72
    • (2010) J Allergy Clin Immunol , vol.125
    • Commins, S.P.1    Borish, L.2    Steinke, J.W.3
  • 17
    • 78649746427 scopus 로고    scopus 로고
    • IL-10 family of cytokines
    • Sabat R. IL-10 family of cytokines. Cytokine Growth Factor Rev. 2010 ; 21: 315-324
    • (2010) Cytokine Growth Factor Rev , vol.21 , pp. 315-324
    • Sabat, R.1
  • 18
    • 19444365121 scopus 로고    scopus 로고
    • Evolution of the Class 2 cytokines and receptors, and discovery of new friends and relatives
    • Krause CD, Pestka S. Evolution of the Class 2 cytokines and receptors, and discovery of new friends and relatives. Pharmacol Ther. 2005 ; 106: 299-346
    • (2005) Pharmacol Ther , vol.106 , pp. 299-346
    • Krause, C.D.1    Pestka, S.2
  • 19
    • 0034029101 scopus 로고    scopus 로고
    • Cytokine receptor signaling pathways
    • Leonard WJ, Lin JX. Cytokine receptor signaling pathways. J Clin Immunol. 2000 ; 105: 877-888
    • (2000) J Clin Immunol , vol.105 , pp. 877-888
    • Leonard, W.J.1    Lin, J.X.2
  • 21
    • 67449110978 scopus 로고    scopus 로고
    • Parasites represent a major selective force for interleukins genes and shape the genetic predisposition to autoimmune conditions
    • Fumagalli M, Pozzoli U, Cagliani R, et al. Parasites represent a major selective force for interleukins genes and shape the genetic predisposition to autoimmune conditions. J Exp Med. 2009 ; 206: 1395-1408
    • (2009) J Exp Med , vol.206 , pp. 1395-1408
    • Fumagalli, M.1    Pozzoli, U.2    Cagliani, R.3
  • 22
    • 42749087384 scopus 로고    scopus 로고
    • The extended IL-10 superfamily: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, IL-28, and IL-29
    • Commins S, Steinke JW, Borish L. The extended IL-10 superfamily: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, IL-28, and IL-29. J Allergy Clin Immunol. 2008 ; 121: 1108-1111
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 1108-1111
    • Commins, S.1    Steinke, J.W.2    Borish, L.3
  • 23
    • 0001929693 scopus 로고    scopus 로고
    • Cytokines in acute and chronic inflammation
    • Feghali CA, Wright TM. Cytokines in acute and chronic inflammation. Front Biosci. 1997 ; 2: d12 - d26
    • (1997) Front Biosci , vol.2
    • Feghali, C.A.1    Wright, T.M.2
  • 24
    • 0036029247 scopus 로고    scopus 로고
    • Cytokines and related receptor-mediated signaling pathways
    • Haddad JJ. Cytokines and related receptor-mediated signaling pathways. Biochem Biophys Res Commun. 2002 ; 297: 700-713
    • (2002) Biochem Biophys Res Commun , vol.297 , pp. 700-713
    • Haddad, J.J.1
  • 25
    • 72849122933 scopus 로고    scopus 로고
    • From evolutionary genetics to human immunology: How selection shapes host defence genes
    • Barreiro LB, Quintana-Murci L. From evolutionary genetics to human immunology: how selection shapes host defence genes. Nat Rev Genet. 2010 ; 11: 17-30
    • (2010) Nat Rev Genet , vol.11 , pp. 17-30
    • Barreiro, L.B.1    Quintana-Murci, L.2
  • 26
    • 77954798091 scopus 로고    scopus 로고
    • Diversifying selection and functional analysis of interleukin-4 suggests antagonism-driven evolution at receptor-binding interfaces
    • Koyanagi M, Kerns JA, Chung L, et al. Diversifying selection and functional analysis of interleukin-4 suggests antagonism-driven evolution at receptor-binding interfaces. BMC Evol Biol. 2010 ; 10: 223-223
    • (2010) BMC Evol Biol , vol.10 , pp. 223-223
    • Koyanagi, M.1    Kerns, J.A.2    Chung, L.3
  • 27
    • 0031856647 scopus 로고    scopus 로고
    • Synonymous and nonsynonymous substitution distances are correlated in mouse and rat genes
    • Makalowski W, Boguski MS. Synonymous and nonsynonymous substitution distances are correlated in mouse and rat genes. J Mol Evol. 1998 ; 47: 119-121
    • (1998) J Mol Evol , vol.47 , pp. 119-121
    • Makalowski, W.1    Boguski, M.S.2
  • 28
    • 79960346953 scopus 로고    scopus 로고
    • Evolution of IL4 and pathogen antagonism
    • PIL-lai MR, Bix M. Evolution of IL4 and pathogen antagonism. Growth Factors. 2011 ; 29: 153-160
    • (2011) Growth Factors , vol.29 , pp. 153-160
    • Pil-Lai, M.R.1    Bix, M.2
  • 29
    • 84855484381 scopus 로고    scopus 로고
    • Evolutionary genetic dissection of human interferons
    • Manry J, Laval G, Patin E, et al. Evolutionary genetic dissection of human interferons. J Exp Med. 2011 ; 208: 2747-2759
    • (2011) J Exp Med , vol.208 , pp. 2747-2759
    • Manry, J.1    Laval, G.2    Patin, E.3
  • 30
    • 77951126544 scopus 로고    scopus 로고
    • Comprehensive sequence analysis of the human IL23A gene defines new variation content and high rate of evolutionary conservation
    • Tindall EA, Hayes VM. Comprehensive sequence analysis of the human IL23A gene defines new variation content and high rate of evolutionary conservation. DNA Res. 2010 ; 17: 117-122
    • (2010) DNA Res , vol.17 , pp. 117-122
    • Tindall, E.A.1    Hayes, V.M.2
  • 31
    • 10744225855 scopus 로고    scopus 로고
    • Haplotype structure and evidence for positive selection at the human IL13 locus
    • Zhou G, Zhai Y, Dong X, et al. Haplotype structure and evidence for positive selection at the human IL13 locus. Mol Biol Evol. 2004 ; 21: 29-35
    • (2004) Mol Biol Evol , vol.21 , pp. 29-35
    • Zhou, G.1    Zhai, Y.2    Dong, X.3
  • 32
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl Acids Symp Ser. 1999 ; 41: 95-98
    • (1999) Nucl Acids Symp ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 33
    • 0037468544 scopus 로고    scopus 로고
    • Amino acid substitutions in the human genome: Evolutionary implications of single nucleotide polymorphisms
    • Majewski J, Ott J. Amino acid substitutions in the human genome: evolutionary implications of single nucleotide polymorphisms. Gene. 2003 ; 305: 167-173
    • (2003) Gene , vol.305 , pp. 167-173
    • Majewski, J.1    Ott, J.2
  • 34
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z. PAML: a program package for phylogenetic analysis by maximum likelihood. Comput Appl Biosci. 1997 ; 13: 555-556
    • (1997) Comput Appl Biosci , vol.13 , pp. 555-556
    • Yang, Z.1
  • 35
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: Phylogenetic analysis by maximum likelihood
    • Yang Z. PAML 4: phylogenetic analysis by maximum likelihood. Mol Biol Evol. 2007 ; 24: 1586-1591
    • (2007) Mol Biol Evol , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 36
    • 17744396121 scopus 로고    scopus 로고
    • Not so different after all: A comparison of methods for detecting amino acid sites under selection
    • Kosakovsky Pond SL, Frost SD. Not so different after all: a comparison of methods for detecting amino acid sites under selection. Mol Biol Evol. 2005 ; 22: 1208-1222
    • (2005) Mol Biol Evol , vol.22 , pp. 1208-1222
    • Kosakovsky Pond, S.L.1    Frost, S.D.2
  • 37
    • 17744395033 scopus 로고    scopus 로고
    • Datamonkey: Rapid detection of selective pressure on individual sites of codon alignments
    • Pond SL, Frost SD. Datamonkey: rapid detection of selective pressure on individual sites of codon alignments. Bioinformatics. 2005 ; 21: 2531-2533
    • (2005) Bioinformatics , vol.21 , pp. 2531-2533
    • Pond, S.L.1    Frost, S.D.2
  • 38
    • 68049135942 scopus 로고    scopus 로고
    • Detecting signatures of selection from DNA sequences using Datamonkey
    • Poon AF, Frost SD, Pond SL. Detecting signatures of selection from DNA sequences using Datamonkey. Methods Mol Biol. 2009 ; 537: 163-183
    • (2009) Methods Mol Biol , vol.537 , pp. 163-183
    • Poon, A.F.1    Frost, S.D.2    Pond, S.L.3
  • 39
    • 0037270595 scopus 로고    scopus 로고
    • Maximum likelihood methods for detecting adaptive evolution after gene duplication
    • Bielawski JP, Yang Z. Maximum likelihood methods for detecting adaptive evolution after gene duplication. J Struct Funct Genomics. 2003 ; 3: 201-212
    • (2003) J Struct Funct Genomics , vol.3 , pp. 201-212
    • Bielawski, J.P.1    Yang, Z.2
  • 40
    • 0036889183 scopus 로고    scopus 로고
    • Inference of selection from multiple species alignments
    • Yang Z. Inference of selection from multiple species alignments. Curr Opin Genet Dev. 2002 ; 12: 688-694
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 688-694
    • Yang, Z.1
  • 41
    • 0034097381 scopus 로고    scopus 로고
    • Codon-substitution models for heterogeneous selection pressure at amino acid sites
    • Yang Z, Nielsen R, Goldman N, Pedersen AM. Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics. 2000 ; 155: 431-449
    • (2000) Genetics , vol.155 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.M.4
  • 42
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, et al. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol. 2011 ; 28: 2731-2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3
  • 43
    • 83655181433 scopus 로고    scopus 로고
    • Signatures of positive selection in Toll-like receptor (TLR) genes in mammals
    • Areal H, Abrantes J, Esteves PJ. Signatures of positive selection in Toll-like receptor (TLR) genes in mammals. BMC Evol Biol. 2011 ; 11: 368-368
    • (2011) BMC Evol Biol , vol.11 , pp. 368-368
    • Areal, H.1    Abrantes, J.2    Esteves, P.J.3
  • 44
    • 77955975911 scopus 로고    scopus 로고
    • Adaptation and constraint at Toll-like receptors in primates
    • Wlasiuk G, Nachman MW. Adaptation and constraint at Toll-like receptors in primates. Mol Biol Evol. 2010 ; 27: 2172-2186
    • (2010) Mol Biol Evol , vol.27 , pp. 2172-2186
    • Wlasiuk, G.1    Nachman, M.W.2
  • 45
    • 50849122974 scopus 로고    scopus 로고
    • Patterns of positive selection in six Mammalian genomes
    • Kosiol C, Vinar T, da Fonseca RR, et al. Patterns of positive selection in six Mammalian genomes. PLoS Genet. 2008 ; 4: e1000144 - e1000144
    • (2008) PLoS Genet , vol.4
    • Kosiol, C.1    Vinar, T.2    Da Fonseca, R.R.3
  • 46
    • 49049119143 scopus 로고    scopus 로고
    • Balancing selection is the main force shaping the evolution of innate immunity genes
    • Ferrer-Admetlla A, Bosch E, Sikora M, et al. Balancing selection is the main force shaping the evolution of innate immunity genes. J Immunol. 2008 ; 181: 1315-1322
    • (2008) J Immunol , vol.181 , pp. 1315-1322
    • Ferrer-Admetlla, A.1    Bosch, E.2    Sikora, M.3
  • 47
    • 33748500819 scopus 로고    scopus 로고
    • The structure of IL2 bound to the three chains of the IL2 receptor and how signaling occurs
    • Smith KA. The structure of IL2 bound to the three chains of the IL2 receptor and how signaling occurs. Med Immunol. 2006 ; 5: 3-3
    • (2006) Med Immunol , vol.5 , pp. 3-3
    • Smith, K.A.1
  • 48
    • 0033574713 scopus 로고    scopus 로고
    • Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface
    • Hage T, Sebald W, Reinemer P. Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface. Cell. 1999 ; 97: 271-281
    • (1999) Cell , vol.97 , pp. 271-281
    • Hage, T.1    Sebald, W.2    Reinemer, P.3
  • 49
    • 38649137731 scopus 로고    scopus 로고
    • Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system
    • LaPorte SL, Juo ZS, Vaclavikova J, et al. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Cell. 2008 ; 132: 259-272
    • (2008) Cell , vol.132 , pp. 259-272
    • Laporte, S.L.1    Juo, Z.S.2    Vaclavikova, J.3
  • 50
    • 4444288545 scopus 로고    scopus 로고
    • Molecular cloning of the swine IL-4 receptor alpha and IL-13 receptor 1-chains: Effects of experimental Toxoplasma gondii, Ascaris suum and Trichuris suis infections on tissue mRNA levels
    • Zarlenga DS, Dawson H, Kringel H, et al. Molecular cloning of the swine IL-4 receptor alpha and IL-13 receptor 1-chains: effects of experimental Toxoplasma gondii, Ascaris suum and Trichuris suis infections on tissue mRNA levels. Vet Immunol Immunopathol. 2004 ; 101: 223-234
    • (2004) Vet Immunol Immunopathol , vol.101 , pp. 223-234
    • Zarlenga, D.S.1    Dawson, H.2    Kringel, H.3
  • 51
    • 0036300916 scopus 로고    scopus 로고
    • The high-affinity interaction of human IL-4 and the receptor alpha chain is constituted by two independent binding clusters
    • Zhang JL, Simeonowa I, Wang Y, Sebald W. The high-affinity interaction of human IL-4 and the receptor alpha chain is constituted by two independent binding clusters. J Mol Biol. 2002 ; 315: 399-407
    • (2002) J Mol Biol , vol.315 , pp. 399-407
    • Zhang, J.L.1    Simeonowa, I.2    Wang, Y.3    Sebald, W.4
  • 52
    • 0037064548 scopus 로고    scopus 로고
    • Structure, binding, and antagonists in the IL-4/IL-13 receptor system
    • Mueller TD, Zhang JL, Sebald W, Duschl A. Structure, binding, and antagonists in the IL-4/IL-13 receptor system. Biochim Biophys Acta. 2002 ; 1592: 237-250
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 237-250
    • Mueller, T.D.1    Zhang, J.L.2    Sebald, W.3    Duschl, A.4
  • 53
    • 0033758410 scopus 로고    scopus 로고
    • Targeting interleukin 18 with interleukin 18 binding protein
    • Dinarello CA. Targeting interleukin 18 with interleukin 18 binding protein. Ann Rheum Dis. 2000 ; 59: i17 - i20
    • (2000) Ann Rheum Dis , vol.59
    • Dinarello, C.A.1
  • 54
    • 57349136769 scopus 로고    scopus 로고
    • Interleukin-18 binding protein transgenic mice are protected against ischemic acute kidney injury
    • He Z, Lu L, Altmann C, et al. Interleukin-18 binding protein transgenic mice are protected against ischemic acute kidney injury. Am J Physiol Renal Physiol. 2008 ; 295: F1414 - F1421
    • (2008) Am J Physiol Renal Physiol , vol.295
    • He, Z.1    Lu, L.2    Altmann, C.3
  • 55
    • 2942551762 scopus 로고    scopus 로고
    • Interleukin-18/interleukin-18 binding protein signaling modulates atherosclerotic lesion development and stability
    • Mallat Z, Corbaz A, Scoazec A, et al. Interleukin-18/interleukin-18 binding protein signaling modulates atherosclerotic lesion development and stability. Circ Res. 2001 ; 89: E41 - E45
    • (2001) Circ Res , vol.89
    • Mallat, Z.1    Corbaz, A.2    Scoazec, A.3
  • 56
    • 33644854500 scopus 로고    scopus 로고
    • Interleukin 1 and interleukin 18 as mediators of inflammation and the aging process
    • Dinarello CA. Interleukin 1 and interleukin 18 as mediators of inflammation and the aging process. Am J Clin Nutr. 2006 ; 83: 447S - 455S
    • (2006) Am J Clin Nutr , vol.83
    • Dinarello, C.A.1
  • 57
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: A close look at thermodynamic stabilization
    • Shental-Bechor D, Levy Y. Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc Natl Acad Sci USA. 2008 ; 105: 8256-8261
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 58
    • 70350011931 scopus 로고    scopus 로고
    • Critical role of glycosylation in determining the length and structure of T cell epitopes
    • Szabo TG, Palotai R, Antal P, et al. Critical role of glycosylation in determining the length and structure of T cell epitopes. Immunome Res. 2009 ; 5: 4-4
    • (2009) Immunome Res , vol.5 , pp. 4-4
    • Szabo, T.G.1    Palotai, R.2    Antal, P.3
  • 59
    • 76249113764 scopus 로고    scopus 로고
    • N-linked glycosylation is essential for the stability but not the signaling function of the interleukin-6 signal transducer glycoprotein 130
    • Waetzig GH, Chalaris A, Rosenstiel P, et al. N-linked glycosylation is essential for the stability but not the signaling function of the interleukin-6 signal transducer glycoprotein 130. J Biol Chem. 2010 ; 285: 1781-1789
    • (2010) J Biol Chem , vol.285 , pp. 1781-1789
    • Waetzig, G.H.1    Chalaris, A.2    Rosenstiel, P.3
  • 60
    • 0035991506 scopus 로고    scopus 로고
    • Impact of glycosylation on the effect of cytokines. A special focus on oncology
    • Chamorey AL, Magne N, Pivot X, MIL-ano G. Impact of glycosylation on the effect of cytokines. A special focus on oncology. Eur Cytokine Netw. 2002 ; 13: 154-160
    • (2002) Eur Cytokine Netw , vol.13 , pp. 154-160
    • Chamorey, A.L.1    Magne, N.2    Pivot, X.3    Mil-Ano, G.4
  • 61
    • 79954494180 scopus 로고    scopus 로고
    • Selective loss of cysteine residues and disulphide bonds in a potato proteinase inhibitor II family
    • Li XQ, Zhang T, Donnelly D. Selective loss of cysteine residues and disulphide bonds in a potato proteinase inhibitor II family. PLoS One. 2011 ; 6: e18615 - e18615
    • (2011) PLoS One , vol.6
    • Li, X.Q.1    Zhang, T.2    Donnelly, D.3
  • 62
    • 84861389565 scopus 로고    scopus 로고
    • Disulfide bonding in protein biophysics
    • Fass D. Disulfide bonding in protein biophysics. Annu Rev Biophys. 2012 ; 41: 63-79
    • (2012) Annu Rev Biophys , vol.41 , pp. 63-79
    • Fass, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.