메뉴 건너뛰기




Volumn 113, Issue 11, 2016, Pages E1470-E1478

Biophysical principles predict fitness landscapes of drug resistance

Author keywords

DHFR; Drug resistance; Fitness landscapes; Molten globule; Protein stability

Indexed keywords

ANTIBIOTIC AGENT; CELL PROTEIN; DIHYDROFOLATE REDUCTASE; TRIMETHOPRIM; ESCHERICHIA COLI PROTEIN;

EID: 84961838974     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1601441113     Document Type: Article
Times cited : (110)

References (36)
  • 1
    • 84555171441 scopus 로고    scopus 로고
    • Evolutionary paths to antibiotic resistance under dynamically sustained drug selection
    • Toprak E, et al. (2012) Evolutionary paths to antibiotic resistance under dynamically sustained drug selection. Nat Genet 44(1):101-105.
    • (2012) Nat Genet , vol.44 , Issue.1 , pp. 101-105
    • Toprak, E.1
  • 2
    • 84931274969 scopus 로고    scopus 로고
    • Delayed commitment to evolutionary fate in antibiotic resistance fitness landscapes
    • Palmer AC, et al. (2015) Delayed commitment to evolutionary fate in antibiotic resistance fitness landscapes. Nat Commun 6:7385.
    • (2015) Nat Commun , vol.6 , pp. 7385
    • Palmer, A.C.1
  • 3
    • 67749098058 scopus 로고    scopus 로고
    • Stepwise acquisition of pyrimethamine resistance in the malaria parasite
    • Lozovsky ER, et al. (2009) Stepwise acquisition of pyrimethamine resistance in the malaria parasite. Proc Natl Acad Sci USA 106(29):12025-12030.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.29 , pp. 12025-12030
    • Lozovsky, E.R.1
  • 4
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich DM, Delaney NF, Depristo MA, Hartl DL (2006) Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312(5770):111-114.
    • (2006) Science , vol.312 , Issue.5770 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4
  • 5
    • 84906751681 scopus 로고    scopus 로고
    • Strength of selection pressure is an important parameter contributing to the complexity of antibiotic resistance evolution
    • Oz T, et al. (2014) Strength of selection pressure is an important parameter contributing to the complexity of antibiotic resistance evolution. Mol Biol Evol 31(9): 2387-2401.
    • (2014) Mol Biol Evol , vol.31 , Issue.9 , pp. 2387-2401
    • Oz, T.1
  • 6
    • 84885671999 scopus 로고    scopus 로고
    • Accessible mutational trajectories for the evolution of pyrimethamine resistance in the malaria parasite Plasmodium vivax
    • Jiang PP, Corbett-Detig RB, Hartl DL, Lozovsky ER (2013) Accessible mutational trajectories for the evolution of pyrimethamine resistance in the malaria parasite Plasmodium vivax. J Mol Evol 77(3):81-91.
    • (2013) J Mol Evol , vol.77 , Issue.3 , pp. 81-91
    • Jiang, P.P.1    Corbett-Detig, R.B.2    Hartl, D.L.3    Lozovsky, E.R.4
  • 7
    • 84925859323 scopus 로고    scopus 로고
    • Predicting evolution from the shape of genealogical trees
    • Neher RA, Russell CA, Shraiman BI (2014) Predicting evolution from the shape of genealogical trees. eLife 3:3.
    • (2014) ELife , vol.3 , pp. 3
    • Neher, R.A.1    Russell, C.A.2    Shraiman, B.I.3
  • 8
    • 84855296907 scopus 로고    scopus 로고
    • Predictability of evolutionary trajectories in fitness landscapes
    • Lobkovsky AE, Wolf YI, Koonin EV (2011) Predictability of evolutionary trajectories in fitness landscapes. PLOS Comput Biol 7(12):e1002302.
    • (2011) PLOS Comput Biol , vol.7 , Issue.12
    • Lobkovsky, A.E.1    Wolf, Y.I.2    Koonin, E.V.3
  • 9
    • 75649111192 scopus 로고    scopus 로고
    • The genetic landscape of a cell
    • Costanzo M, et al. (2010) The genetic landscape of a cell. Science 327(5964):425-431.
    • (2010) Science , vol.327 , Issue.5964 , pp. 425-431
    • Costanzo, M.1
  • 10
    • 82955229552 scopus 로고    scopus 로고
    • Impact of epistasis and pleiotropy on evolutionary adaptation
    • Ostman B, Hintze A, Adami C (2012) Impact of epistasis and pleiotropy on evolutionary adaptation. Proc Biol Sci 279(1727):247-256.
    • (2012) Proc Biol Sci , vol.279 , Issue.1727 , pp. 247-256
    • Ostman, B.1    Hintze, A.2    Adami, C.3
  • 11
    • 84903957269 scopus 로고    scopus 로고
    • Genome-wide analysis captures the determinants of the antibiotic cross-resistance interaction network
    • Lázár V, et al. (2014) Genome-wide analysis captures the determinants of the antibiotic cross-resistance interaction network. Nat Commun 5:4352.
    • (2014) Nat Commun , vol.5 , pp. 4352
    • Lázár, V.1
  • 12
    • 84859476261 scopus 로고    scopus 로고
    • Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations
    • Bershtein S, Mu W, Shakhnovich EI (2012) Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations. Proc Natl Acad Sci USA 109(13): 4857-4862.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.13 , pp. 4857-4862
    • Bershtein, S.1    Mu, W.2    Shakhnovich, E.I.3
  • 13
    • 84872272432 scopus 로고    scopus 로고
    • Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness
    • Bershtein S, Mu W, Serohijos AW, Zhou J, Shakhnovich EI (2013) Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness. Mol Cell 49(1):133-144.
    • (2013) Mol Cell , vol.49 , Issue.1 , pp. 133-144
    • Bershtein, S.1    Mu, W.2    Serohijos, A.W.3    Zhou, J.4    Shakhnovich, E.I.5
  • 14
    • 0019869334 scopus 로고
    • The molecular basis of dominance
    • Kacser H, Burns JA (1981) The molecular basis of dominance. Genetics 97(3-4): 639-666.
    • (1981) Genetics , vol.97 , Issue.3-4 , pp. 639-666
    • Kacser, H.1    Burns, J.A.2
  • 16
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 17
    • 0025216077 scopus 로고
    • An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'
    • Goldberg ME, et al. (1990) An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. FEBS Lett 263(1):51-56.
    • (1990) FEBS Lett , vol.263 , Issue.1 , pp. 51-56
    • Goldberg, M.E.1
  • 18
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke CA, Johnson KA, Benkovic SJ (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26(13):4085-4092.
    • (1987) Biochemistry , vol.26 , Issue.13 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 20
    • 84946600829 scopus 로고    scopus 로고
    • Protein homeostasis imposes a barrier on functional integration of horizontally transferred genes in bacteria
    • Bershtein S, et al. (2015) Protein homeostasis imposes a barrier on functional integration of horizontally transferred genes in bacteria. PLoS Genet 11(10):e1005612.
    • (2015) PLoS Genet , vol.11 , Issue.10
    • Bershtein, S.1
  • 21
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett BD, et al. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5(8):593-599.
    • (2009) Nat Chem Biol , vol.5 , Issue.8 , pp. 593-599
    • Bennett, B.D.1
  • 22
    • 0021152232 scopus 로고
    • Trimethoprim, failure to penetrate into Pseudomonasaeruginosa cells
    • Werner RG, Goeth H (1984) Trimethoprim, failure to penetrate into Pseudomonasaeruginosa cells. FEMS Microbiol Lett 23(2-3):201-204.
    • (1984) FEMS Microbiol Lett , vol.23 , Issue.2-3 , pp. 201-204
    • Werner, R.G.1    Goeth, H.2
  • 23
    • 70350769418 scopus 로고    scopus 로고
    • Nonoptimal microbial response to antibiotics underlies suppressive drug interactions
    • Bollenbach T, Quan S, Chait R, Kishony R (2009) Nonoptimal microbial response to antibiotics underlies suppressive drug interactions. Cell 139(4):707-718.
    • (2009) Cell , vol.139 , Issue.4 , pp. 707-718
    • Bollenbach, T.1    Quan, S.2    Chait, R.3    Kishony, R.4
  • 24
    • 84928581611 scopus 로고    scopus 로고
    • Systems-level response to point mutations in a core metabolic enzyme modulates genotype-phenotype relationship
    • Bershtein S, Choi JM, Bhattacharyya S, Budnik B, Shakhnovich E (2015) Systems-level response to point mutations in a core metabolic enzyme modulates genotype-phenotype relationship. Cell Reports 11(4):645-656.
    • (2015) Cell Reports , vol.11 , Issue.4 , pp. 645-656
    • Bershtein, S.1    Choi, J.M.2    Bhattacharyya, S.3    Budnik, B.4    Shakhnovich, E.5
  • 25
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. Coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa M, et al. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research. DNA Res 12(5):291-299.
    • (2005) DNA Res , vol.12 , Issue.5 , pp. 291-299
    • Kitagawa, M.1
  • 26
    • 0023158041 scopus 로고
    • Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim
    • Flensburg J, Sköld O (1987) Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim. Eur J Biochem 162(3):473-476.
    • (1987) Eur J Biochem , vol.162 , Issue.3 , pp. 473-476
    • Flensburg, J.1    Sköld, O.2
  • 27
    • 84890127117 scopus 로고    scopus 로고
    • Lon protease inactivation, or translocation of the lon gene, potentiate bacterial evolution to antibiotic resistance
    • Nicoloff H, Andersson DI (2013) Lon protease inactivation, or translocation of the lon gene, potentiate bacterial evolution to antibiotic resistance. Mol Microbiol 90(6): 1233-1248.
    • (2013) Mol Microbiol , vol.90 , Issue.6 , pp. 1233-1248
    • Nicoloff, H.1    Andersson, D.I.2
  • 28
    • 84902775598 scopus 로고    scopus 로고
    • Empirical fitness landscapes and the predictability of evolution
    • de Visser JA, Krug J (2014) Empirical fitness landscapes and the predictability of evolution. Nat Rev Genet 15(7):480-490.
    • (2014) Nat Rev Genet , vol.15 , Issue.7 , pp. 480-490
    • De Visser, J.A.1    Krug, J.2
  • 29
    • 84901742626 scopus 로고    scopus 로고
    • Mapping the fitness landscape of gene expression uncovers the cause of antagonism and sign epistasis between adaptive mutations
    • Chou HH, Delaney NF, Draghi JA, Marx CJ (2014) Mapping the fitness landscape of gene expression uncovers the cause of antagonism and sign epistasis between adaptive mutations. PLoS Genet 10(2):e1004149.
    • (2014) PLoS Genet , vol.10 , Issue.2
    • Chou, H.H.1    Delaney, N.F.2    Draghi, J.A.3    Marx, C.J.4
  • 30
    • 84881408157 scopus 로고    scopus 로고
    • Capturing the mutational landscape of the beta-lactamase TEM-1
    • Jacquier H, et al. (2013) Capturing the mutational landscape of the beta-lactamase TEM-1. Proc Natl Acad Sci USA 110(32):13067-13072.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.32 , pp. 13067-13072
    • Jacquier, H.1
  • 31
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N, Tawfik DS (2009) Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459(7247):668-673.
    • (2009) Nature , vol.459 , Issue.7247 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 32
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C, Sangster TA, Lindquist S (2002) Hsp90 as a capacitor of phenotypic variation. Nature 417(6889):618-624.
    • (2002) Nature , vol.417 , Issue.6889 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 34
    • 84929497890 scopus 로고    scopus 로고
    • Thermal stabilization of dihydrofolate reductase using monte carlo unfolding simulations and its functional consequences
    • Tian J, Woodard JC, Whitney A, Shakhnovich EI (2015) Thermal stabilization of dihydrofolate reductase using monte carlo unfolding simulations and its functional consequences. PLOS Comput Biol 11(4):e1004207.
    • (2015) PLOS Comput Biol , vol.11 , Issue.4
    • Tian, J.1    Woodard, J.C.2    Whitney, A.3    Shakhnovich, E.I.4
  • 35
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson KA, Simpson ZB, Blom T (2009) FitSpace explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data. Anal Biochem 387(1):30-41.
    • (2009) Anal Biochem , vol.387 , Issue.1 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 36
    • 0347224283 scopus 로고    scopus 로고
    • Interpreting enzyme and receptor kinetics: Keeping it simple, but not too simple
    • Krohn KA, Link JM (2003) Interpreting enzyme and receptor kinetics: Keeping it simple, but not too simple. Nucl Med Biol 30(8):819-826.
    • (2003) Nucl Med Biol , vol.30 , Issue.8 , pp. 819-826
    • Krohn, K.A.1    Link, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.