메뉴 건너뛰기




Volumn 11, Issue 6, 2004, Pages 865-874

Evolutionary optimization of a nonbiological ATP binding protein for improved folding stability

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEIN; THROMBIN;

EID: 3042693137     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.04.006     Document Type: Article
Times cited : (34)

References (45)
  • 4
    • 0032545151 scopus 로고    scopus 로고
    • Estimating the number of protein folds
    • Zhang C., DeLisi C. Estimating the number of protein folds. J. Mol. Biol. 284:1998;1301-1305
    • (1998) J. Mol. Biol. , vol.284 , pp. 1301-1305
    • Zhang, C.1    Delisi, C.2
  • 5
    • 0027122748 scopus 로고
    • One thousand families for the molecular biologist
    • Chothia C. One thousand families for the molecular biologist. Nature. 357:1992;543-544
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 6
    • 0028593509 scopus 로고
    • Protein superfamilies and domain structures
    • Orengo C.A., Jones D.T., Thornton J.M. Protein superfamilies and domain structures. Nature. 372:1994;631-634
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 7
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert W. Why genes in pieces? Nature. 271:1978;501
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 8
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle R.F. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:1995;287-314
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 9
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function
    • Gerlt J.A., Babbitt P.C. Divergent evolution of enzymatic function. Annu. Rev. Biochem. 70:2001;209-246
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 10
  • 11
    • 0035471132 scopus 로고    scopus 로고
    • De novo proteins from combinatorial libraries
    • Moffet D.A., Hecht M.H. De novo proteins from combinatorial libraries. Chem. Rev. 101:2001;3191-3203
    • (2001) Chem. Rev. , vol.101 , pp. 3191-3203
    • Moffet, D.A.1    Hecht, M.H.2
  • 14
    • 0344392714 scopus 로고    scopus 로고
    • Solution structure of a de novo protein from a designed combinatorial library
    • Wei Y., Kim S., Fela D., Baum J., Hecht M.H. Solution structure of a de novo protein from a designed combinatorial library. Proc. Natl. Acad. Sci. USA. 100:2003;13270-13273
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13270-13273
    • Wei, Y.1    Kim, S.2    Fela, D.3    Baum, J.4    Hecht, M.H.5
  • 15
    • 0028218304 scopus 로고
    • Folded proteins occur frequently in libraries of random amino acid sequences
    • Davidson A.R., Sauer R.T. Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl. Acad. Sci. USA. 91:1994;2146-2150
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 16
    • 0029120253 scopus 로고
    • Cooperatively folded proteins in random sequence libraries
    • Davidson A.R., Lumb K.J., Sauer R.T. Cooperatively folded proteins in random sequence libraries. Nat. Struct. Biol. 2:1995;856-864
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 856-864
    • Davidson, A.R.1    Lumb, K.J.2    Sauer, R.T.3
  • 17
    • 0028858499 scopus 로고
    • De-novo design of the hydrophobic core of proteins
    • Desjarlais J.R., Handel T.M. De-novo design of the hydrophobic core of proteins. Protein Sci. 4:1995;2006-2018
    • (1995) Protein Sci. , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 18
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat B.I., Mayo S.L. De novo protein design. fully automated sequence selection Science. 278:1997;82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 19
    • 0035957360 scopus 로고    scopus 로고
    • Computational method to reduce the search space for directed protein evolution
    • Voigt C.A., Mayo S.L., Arnold F.H., Wang Z.-G. Computational method to reduce the search space for directed protein evolution. Proc. Natl. Acad. Sci. USA. 98:2001;3778-3783
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3778-3783
    • Voigt, C.A.1    Mayo, S.L.2    Arnold, F.H.3    Wang, Z.-G.4
  • 20
  • 21
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe A.D., Szostak J.W. Functional proteins from a random-sequence library. Nature. 410:2001;715-718
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 22
    • 0027180473 scopus 로고
    • An RNA motif that binds ATP
    • Sassanfar M., Szostak J.W. An RNA motif that binds ATP. Nature. 364:1993;550-553
    • (1993) Nature , vol.364 , pp. 550-553
    • Sassanfar, M.1    Szostak, J.W.2
  • 24
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • Jung S., Honegger A., Pluckthun A. Selection for improved protein stability by phage display. J. Mol. Biol. 294:1999;163-180
    • (1999) J. Mol. Biol. , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Pluckthun, A.3
  • 25
    • 0037468662 scopus 로고    scopus 로고
    • Selection based on the folding properties of proteins with ribosome display
    • Matsuura T., Pluckthun A. Selection based on the folding properties of proteins with ribosome display. FEBS Lett. 539:2003;24-28
    • (2003) FEBS Lett. , vol.539 , pp. 24-28
    • Matsuura, T.1    Pluckthun, A.2
  • 26
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusion for the in vitro selection of peptides and proteins
    • Roberts R., Szostak J.W. RNA-peptide fusion for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA. 94:1997;12297-12302
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12297-12302
    • Roberts, R.1    Szostak, J.W.2
  • 27
    • 0037348840 scopus 로고    scopus 로고
    • A novel strategy for in vitro selection of peptide-drug conjugates
    • Li S., Roberts R.W. A novel strategy for in vitro selection of peptide-drug conjugates. Chem. Biol. 10:2003;233-239
    • (2003) Chem. Biol. , vol.10 , pp. 233-239
    • Li, S.1    Roberts, R.W.2
  • 28
    • 0035986682 scopus 로고    scopus 로고
    • Drug receptor identification from multiple tissues using cellular-derived mRNA display libraries
    • McPherson M., Yang Y., Hammond P.W., Kreider B.L. Drug receptor identification from multiple tissues using cellular-derived mRNA display libraries. Chem. Biol. 9:2002;691-698
    • (2002) Chem. Biol. , vol.9 , pp. 691-698
    • McPherson, M.1    Yang, Y.2    Hammond, P.W.3    Kreider, B.L.4
  • 29
    • 0035957374 scopus 로고    scopus 로고
    • The use of mRNA display to select high-affinity protein-binding peptides
    • Wilson D.S., Keefe A.D., Szostak J.W. The use of mRNA display to select high-affinity protein-binding peptides. Proc. Natl. Acad. Sci. USA. 98:2001;3750-3755
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3750-3755
    • Wilson, D.S.1    Keefe, A.D.2    Szostak, J.W.3
  • 30
    • 0035877791 scopus 로고    scopus 로고
    • In vitro selection and characterization of Bcl-XL-binding proteins from a mix of tissue-specific mRNA display libraries
    • Mammond P.W., Alpin J., Rise C.E., Wright M., Kreider B.L. In vitro selection and characterization of Bcl-XL-binding proteins from a mix of tissue-specific mRNA display libraries. J. Biol. Chem. 276:2001;20898-20906
    • (2001) J. Biol. Chem. , vol.276 , pp. 20898-20906
    • Mammond, P.W.1    Alpin, J.2    Rise, C.E.3    Wright, M.4    Kreider, B.L.5
  • 31
    • 0036008852 scopus 로고    scopus 로고
    • Selection of v-AbI tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display
    • Cujec T.P., Medeiros P.F., Hammond P.W., Rise C.E., Kreider B.L. Selection of v-AbI tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display. Chem. Biol. 9:2002;253-264
    • (2002) Chem. Biol. , vol.9 , pp. 253-264
    • Cujec, T.P.1    Medeiros, P.F.2    Hammond, P.W.3    Rise, C.E.4    Kreider, B.L.5
  • 32
    • 17544399298 scopus 로고    scopus 로고
    • Psoralen photo-crosslinked mRNA-puromycin conjugates: A novel template for the rapid and facile preparation of MRA-protein fusions
    • Kurz M., Gu K., Lohse P.A. Psoralen photo-crosslinked mRNA-puromycin conjugates. a novel template for the rapid and facile preparation of MRA-protein fusions Nucleic Acids Res. 28:2000;e83
    • (2000) Nucleic Acids Res. , vol.28 , pp. 83
    • Kurz, M.1    Gu, K.2    Lohse, P.A.3
  • 33
    • 0028224199 scopus 로고
    • High resolution molecular discrimination by RNA
    • Jenison R.D., Gill S.C., Pardi A., Polisky B. High resolution molecular discrimination by RNA. Science. 263:1994;1425-1429
    • (1994) Science , vol.263 , pp. 1425-1429
    • Jenison, R.D.1    Gill, S.C.2    Pardi, A.3    Polisky, B.4
  • 34
    • 0029379551 scopus 로고
    • Let's get specific: The relationship between specificity and affinity
    • Eaton B.E., Gold L., Zichi D.A. Let's get specific. the relationship between specificity and affinity Chem. Biol. 2:1995;633-638
    • (1995) Chem. Biol. , vol.2 , pp. 633-638
    • Eaton, B.E.1    Gold, L.2    Zichi, D.A.3
  • 35
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 36
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride determination of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • Greene R.F., Pace N.C. Urea and guanidine hydrochloride determination of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J. Biol. Chem. 249:1974;5388-5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, N.C.2
  • 37
    • 0020479709 scopus 로고
    • Estimation of the free energy of stabilization of ribonuclease A, lysozyme, α-lactalbumin, and myoglobin
    • Ahmad F., Bigelow C.C. Estimation of the free energy of stabilization of ribonuclease A, lysozyme, α-lactalbumin, and myoglobin. J. Biol. Chem. 257:1982;12935-12938
    • (1982) J. Biol. Chem. , vol.257 , pp. 12935-12938
    • Ahmad, F.1    Bigelow, C.C.2
  • 38
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody R.W. Circular dichroism. Methods Enzymol. 246:1995;34-70
    • (1995) Methods Enzymol. , vol.246 , pp. 34-70
    • Woody, R.W.1
  • 39
    • 0033643217 scopus 로고    scopus 로고
    • Optimized synthesis of RNA-protein fusions for in vitro protein selection
    • Liu R., Barrick J.E., Szostak J.W., Roberts R.W. Optimized synthesis of RNA-protein fusions for in vitro protein selection. Methods Enzymol. 318:2000;268-293
    • (2000) Methods Enzymol. , vol.318 , pp. 268-293
    • Liu, R.1    Barrick, J.E.2    Szostak, J.W.3    Roberts, R.W.4
  • 40
    • 0034708337 scopus 로고    scopus 로고
    • Construction of high complexity synthetic libraries of long ORFs using in vitro selection
    • Cho G., Keefe A.D., Wilson D.S., Liu R., Szostak J.W. Construction of high complexity synthetic libraries of long ORFs using in vitro selection. J. Mol. Biol. 297:2000;309-319
    • (2000) J. Mol. Biol. , vol.297 , pp. 309-319
    • Cho, G.1    Keefe, A.D.2    Wilson, D.S.3    Liu, R.4    Szostak, J.W.5
  • 42
    • 0030779872 scopus 로고    scopus 로고
    • Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX
    • McCafferty D.G., Lessard I.A.D., Walsh C.T. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry. 36:1997;10498-10505
    • (1997) Biochemistry , vol.36 , pp. 10498-10505
    • McCafferty, D.G.1    Lessard, I.A.D.2    Walsh, C.T.3
  • 44
    • 3042591971 scopus 로고    scopus 로고
    • Oestereich, S., and Szostak, J.W. (2004).
    • Oestereich, S., and Szostak, J.W. (2004).
  • 45
    • 0015438810 scopus 로고
    • The preparation of guanidine hydrochloride
    • Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol. 26:1972;43-50
    • (1972) Methods Enzymol. , vol.26 , pp. 43-50
    • Nozaki, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.