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Volumn 9, Issue 3, 1999, Pages 363-367

From protein sequence to function

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0033150942     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80049-9     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 85030360232 scopus 로고    scopus 로고
    • The EMBL nucleotide sequence database on the World Wide Web at URL: http://www.ebi.ac.uk_docs/embl_db/ebi/topembl.html
  • 2
    • 85030363917 scopus 로고    scopus 로고
    • DNA Data Bank of Japan on the World Wide Web at URL: http://www.ddbj.nig.ac.jp/
  • 3
    • 85030363886 scopus 로고    scopus 로고
    • Entrez genomes on the World Wide Web at URL: http://www.ncbi.nlm.nih.gov/Entrez/Genome/org.html
  • 4
    • 85030366014 scopus 로고    scopus 로고
    • GenomeNet WWW server on the World Wide Web at URL: http://www.genome.ad.jp/
  • 5
    • 85030366917 scopus 로고    scopus 로고
    • The Sanger Centre Projects on the World Wide Web at URL: http://www.sanger.ac.uk/Projects/
  • 6
    • 85030363630 scopus 로고    scopus 로고
    • The Institute for Genomic Research on the World Wide Web at URL: http://www.tigr.org/
  • 7
    • 85030370116 scopus 로고    scopus 로고
    • The University of Oklahoma's Advanced Center for Genome Technology on the World Wide Web at URL: http://www.genome.ou.edu/
  • 8
    • 85030369608 scopus 로고    scopus 로고
    • Completed and ongoing genome projects monitor on the World Wide Web at URL: http://geta.life.uiuc.edu/-nikos/genomes.html
  • 9
    • 85030364441 scopus 로고    scopus 로고
    • Genomic databases on the Internet on the World Wide Web at URL: http://bmbsgi12.leeds.ac.uk/bmbknd/DNA/genomic.html
  • 10
    • 85030370128 scopus 로고    scopus 로고
    • Annotated links to Biochemistry and Molecular Biology Internet resources on the World Wide Web at URL: http://www.sgi.bls.umkc.edu/biolinks/
  • 11
    • 85030365931 scopus 로고    scopus 로고
    • The SwissProt data library is the best annotated protein sequence library that is used to predict protein functions. Please note that it is not infallible!
    • ExPASy Molecular Biology Server on the World Wide Web at URL: http://expasy.hcuge.ch/www/expasy-top.html The SwissProt data library is the best annotated protein sequence library that is used to predict protein functions. Please note that it is not infallible!
  • 12
    • 85030366334 scopus 로고    scopus 로고
    • The Brookhaven National Laboratory Protein Data Bank on the World Wide Web at URL: http://www.pdb.bnl.gov/pdb-docs/index.html
  • 13
    • 0031853060 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • Kay LE: Protein dynamics from NMR. Nat Struct Biol 1998, 5(suppl):513-517.
    • (1998) Nat Struct Biol , vol.5 , Issue.SUPPL. , pp. 513-517
    • Kay, L.E.1
  • 14
    • 0031856084 scopus 로고    scopus 로고
    • Kinetic studies of protein folding using NMR spectroscopy
    • Dobson CM, Hore PJ: Kinetic studies of protein folding using NMR spectroscopy. Nat Struct Biol 1998, 5(suppl):504-507.
    • (1998) Nat Struct Biol , vol.5 , Issue.SUPPL. , pp. 504-507
    • Dobson, C.M.1    Hore, P.J.2
  • 15
    • 0031595590 scopus 로고    scopus 로고
    • The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
    • NMR spectroscopy techniques are developing rapidly. The protein structures that are resolved using this technique are getting bigger and bigger, thanks to the use of heteronuclear coupling, as described in this paper
    • Gardner KH, Kay LE: The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu Rev Biophys Biomol Struct 1998, 27:357-406. NMR spectroscopy techniques are developing rapidly. The protein structures that are resolved using this technique are getting bigger and bigger, thanks to the use of heteronuclear coupling, as described in this paper.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 16
    • 0030949159 scopus 로고    scopus 로고
    • Electron crystallography of macromolecular periodic arrays on phospholipid monolayers
    • Chiu W, Avila-Sakar AJ, Schmid MF: Electron crystallography of macromolecular periodic arrays on phospholipid monolayers. Adv Biophys 1997, 34:161-172.
    • (1997) Adv Biophys , vol.34 , pp. 161-172
    • Chiu, W.1    Avila-Sakar, A.J.2    Schmid, M.F.3
  • 17
    • 0031784044 scopus 로고    scopus 로고
    • A genome-based approach for the identification of essential bacterial genes
    • A comprehensive view of the potential of in silico prediction of gene function, illustrated with specific examples
    • Arigoni F, Talabot F, Peitsch M, Edgerton MD, Meldrum E, Allet E, Fish R, Jamotte T, Curchod ML, Loferer H: A genome-based approach for the identification of essential bacterial genes. Nat Biotechnol 1998, 16:851-856. A comprehensive view of the potential of in silico prediction of gene function, illustrated with specific examples.
    • (1998) Nat Biotechnol , vol.16 , pp. 851-856
    • Arigoni, F.1    Talabot, F.2    Peitsch, M.3    Edgerton, M.D.4    Meldrum, E.5    Allet, E.6    Fish, R.7    Jamotte, T.8    Curchod, M.L.9    Loferer, H.10
  • 18
    • 0029828166 scopus 로고    scopus 로고
    • Fully automated genome analysis that reflects user needs and preferences. A detailed introduction to the MAGPIE system architecture
    • Gaasterland T, Sensen CW: Fully automated genome analysis that reflects user needs and preferences. A detailed introduction to the MAGPIE system architecture. Biochimie 1996, 78:302-310.
    • (1996) Biochimie , vol.78 , pp. 302-310
    • Gaasterland, T.1    Sensen, C.W.2
  • 19
    • 0030881249 scopus 로고    scopus 로고
    • Genotator: A workbench for sequence annotation
    • Harris NL: Genotator: A workbench for sequence annotation. Genome Res 1997, 7:754-762.
    • (1997) Genome Res , vol.7 , pp. 754-762
    • Harris, N.L.1
  • 20
    • 0031694515 scopus 로고    scopus 로고
    • EUCLID: Automatic classification of proteins in functional classes by their database annotations
    • Tamames J, Ouzounis C, Casari G, Sander C, Valencia A: EUCLID: Automatic classification of proteins in functional classes by their database annotations. Bioinformatics 1998, 14:542-543.
    • (1998) Bioinformatics , vol.14 , pp. 542-543
    • Tamames, J.1    Ouzounis, C.2    Casari, G.3    Sander, C.4    Valencia, A.5
  • 21
    • 0032535567 scopus 로고    scopus 로고
    • Structures of Escherichia coli CMP kinase alone and in complex with CDP: A new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity
    • Briozo P, Golinelli-Pimpaneau B, Gilles A-M, Gaucher J-F, Burlacu-Miron S, Sakamoto H, Janin J, Barzu O: Structures of Escherichia coli CMP kinase alone and in complex with CDP: A new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity. Structure 1998, 6:1517-1527.
    • (1998) Structure , vol.6 , pp. 1517-1527
    • Briozo, P.1    Golinelli-Pimpaneau, B.2    Gilles, A.-M.3    Gaucher, J.-F.4    Burlacu-Miron, S.5    Sakamoto, H.6    Janin, J.7    Barzu, O.8
  • 22
    • 0032169440 scopus 로고    scopus 로고
    • Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: Archaeon specificity and catalytic mechanism of adenylate formation
    • Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D: Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: Archaeon specificity and catalytic mechanism of adenylate formation. EMBO J 1998, 17:5227-5237.
    • (1998) EMBO J , vol.17 , pp. 5227-5237
    • Schmitt, E.1    Moulinier, L.2    Fujiwara, S.3    Imanaka, T.4    Thierry, J.C.5    Moras, D.6
  • 23
    • 0030752655 scopus 로고    scopus 로고
    • Rotation of the gamma subunit in F1 -ATPase; evidence that ATP synthase is a rotary motor enzyme
    • Yasuda R, Noji H, Kinosita K Jr, Motojima F, Yoshida M: Rotation of the gamma subunit in F1 -ATPase; evidence that ATP synthase is a rotary motor enzyme. J Bioenerg Biomembr 1997, 29:207-209.
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 207-209
    • Yasuda, R.1    Noji, H.2    Kinosita K., Jr.3    Motojima, F.4    Yoshida, M.5
  • 24
    • 0032568695 scopus 로고    scopus 로고
    • F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps
    • This beautiful experimental work demonstrates that ATP synthase is the smallest engine in the world
    • Yasuda R, Noji H, Kinosita K Jr, Yoshida M: F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps. Cell 1998, 93:1117-1124. This beautiful experimental work demonstrates that ATP synthase is the smallest engine in the world.
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita K., Jr.3    Yoshida, M.4
  • 25
    • 0032547899 scopus 로고    scopus 로고
    • Energy transduction in the F1 motor of ATP synthase
    • Wang H, Oster G: Energy transduction in the F1 motor of ATP synthase. Nature 1998, 396:279-282.
    • (1998) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 26
    • 0032531926 scopus 로고    scopus 로고
    • Voltage-generated torque drives the motor of the ATP synthase
    • Kaim G, Dimroth P: Voltage-generated torque drives the motor of the ATP synthase. EMBO J 1998, 17:5887-5895.
    • (1998) EMBO J , vol.17 , pp. 5887-5895
    • Kaim, G.1    Dimroth, P.2
  • 27
    • 0032311089 scopus 로고    scopus 로고
    • Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase
    • WilkenS S, Capaldi RA: Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase. Biochim Biophys Acta 1998, 1365:93-97.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 93-97
    • Wilkens, S.1    Capaldi, R.A.2
  • 28
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F0F1-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • Arnold I, Pfeiffer K, Neupert W, Stuart RA, Schägger H: Yeast mitochondrial F0F1-ATP synthase exists as a dimer: Identification of three dimer-specific subunits. EMBO J 1998, 17:7170-7178.
    • (1998) EMBO J , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schägger, H.5
  • 29
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan Y, Kollman PA: Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science 1998, 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 30
    • 0031758128 scopus 로고    scopus 로고
    • Reduced protein models and their application to the protein folding problem
    • Skolnick J, Kolinski A, Ortiz AR: Reduced protein models and their application to the protein folding problem. J Biomol Struct Dyn 1998, 16:381-396.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 381-396
    • Skolnick, J.1    Kolinski, A.2    Ortiz, A.R.3
  • 31
    • 0031604141 scopus 로고    scopus 로고
    • Genetic algorithms for protein threading
    • Yadgari J, Amir A, Unger R: Genetic algorithms for protein threading. ISMB 1998, 6:193-202.
    • (1998) ISMB , vol.6 , pp. 193-202
    • Yadgari, J.1    Amir, A.2    Unger, R.3
  • 32
    • 0031616029 scopus 로고    scopus 로고
    • A protein conformational search space defined by secondary structure contacts
    • Parisien M, Major F, Peitsch M: A protein conformational search space defined by secondary structure contacts. Pac Symp Biocomput 1998:425-436.
    • (1998) Pac Symp Biocomput , pp. 425-436
    • Parisien, M.1    Major, F.2    Peitsch, M.3
  • 33
    • 0032189646 scopus 로고    scopus 로고
    • Dictionary of recurrent domains in protein structures
    • Holm L, Sander C: Dictionary of recurrent domains in protein structures. Proteins 1998, 33:88-96.
    • (1998) Proteins , vol.33 , pp. 88-96
    • Holm, L.1    Sander, C.2
  • 34
    • 0032919371 scopus 로고    scopus 로고
    • Protein folds and families: Sequence and structure alignments
    • This article, together with [33], provides a dictionary of folds and enables them to be connected with sequence multi-alignments
    • Holm L, Sander C: Protein folds and families: Sequence and structure alignments. Nucleic Acids Res 1999, 27:244-247. This article, together with [33], provides a dictionary of folds and enables them to be connected with sequence multi-alignments.
    • (1999) Nucleic Acids Res , vol.27 , pp. 244-247
    • Holm, L.1    Sander, C.2
  • 35
    • 0031626948 scopus 로고    scopus 로고
    • The GAIA software framework for genome annotation
    • The GAIA software illustrates a recent case of the general tendency to develop multipurpose engines for semi-automatic genome annotation (e.g. Imagene), in contrast to automatic annotation (e.g. Genotator, Genequiz and so on)
    • Overton GC, Bailey C, Crabtree J, Gibson M, Fischer S, Schug J: The GAIA software framework for genome annotation. Pac Symp Biocomput 1998:291-302. The GAIA software illustrates a recent case of the general tendency to develop multipurpose engines for semi-automatic genome annotation (e.g. Imagene), in contrast to automatic annotation (e.g. Genotator, Genequiz and so on).
    • (1998) Pac Symp Biocomput , pp. 291-302
    • Overton, G.C.1    Bailey, C.2    Crabtree, J.3    Gibson, M.4    Fischer, S.5    Schug, J.6
  • 36
    • 0031610846 scopus 로고    scopus 로고
    • Constructing multigenome views of whole microbial genomes
    • A further reflection after MAGPIE, which set the stage for an integrated view of genome annotation. MAGPIE was an important step forward that permitted the community of genome annotators to discover the impossibility, in the absence of entirely new concepts, of managing the huge amount of data generated by genome comparisons
    • Gaasterland T, Ragan MA: Constructing multigenome views of whole microbial genomes. Microb Comp Genomics 1998, 3:177-192. A further reflection after MAGPIE, which set the stage for an integrated view of genome annotation. MAGPIE was an important step forward that permitted the community of genome annotators to discover the impossibility, in the absence of entirely new concepts, of managing the huge amount of data generated by genome comparisons.
    • (1998) Microb Comp Genomics , vol.3 , pp. 177-192
    • Gaasterland, T.1    Ragan, M.A.2
  • 37
    • 0032919372 scopus 로고    scopus 로고
    • Recent improvements of the prodom database of protein domain families
    • A standard, but useful, automatic construction of the multi-alignment of protein domains
    • Corpet F, Gouzy J, Kahn D: Recent improvements of the ProDom database of protein domain families. Nucleic Acids Res 1999, 27:263-267. A standard, but useful, automatic construction of the multi-alignment of protein domains.
    • (1999) Nucleic Acids Res , vol.27 , pp. 263-267
    • Corpet, F.1    Gouzy, J.2    Kahn, D.3
  • 39
    • 0032213054 scopus 로고    scopus 로고
    • Chemical basis for alkali cation selectivity in potassium-channel proteins
    • Moczydlowski E: Chemical basis for alkali cation selectivity in potassium-channel proteins. Chem Biol 1998, 5:R291-R301.
    • (1998) Chem Biol , vol.5
    • Moczydlowski, E.1
  • 40
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong N, Sun Y, Chen GQ, Gouaux E: Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 1998, 395:913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 41
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC: Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 1998, 282:2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 42
    • 0032480889 scopus 로고    scopus 로고
    • Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2
    • Himanen JP, Henkemeyer M, Nikolov DB: Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2. Nature 1998, 396:486-491.
    • (1998) Nature , vol.396 , pp. 486-491
    • Himanen, J.P.1    Henkemeyer, M.2    Nikolov, D.B.3
  • 43
    • 0032190991 scopus 로고    scopus 로고
    • Evolution of the androgen receptor: Structure-function implications
    • Thornton JW, Kelley DB: Evolution of the androgen receptor: Structure-function implications. Bioessays 1998, 20:860-869.
    • (1998) Bioessays , vol.20 , pp. 860-869
    • Thornton, J.W.1    Kelley, D.B.2
  • 44
    • 0031867073 scopus 로고    scopus 로고
    • Nuclear receptors, nuclear-receptor factors, and nuclear-receptor-like orphans form a large paralog cluster in Homo sapiens
    • An interesting illustration of the combination of phylogenetic, biochemical and sequence data in order to understand the formation of multidomain proteins
    • Garcia-Vallve S, Palau J: Nuclear receptors, nuclear-receptor factors, and nuclear-receptor-like orphans form a large paralog cluster in Homo sapiens. Mol Biol Evol 1998, 15:665-682. An interesting illustration of the combination of phylogenetic, biochemical and sequence data in order to understand the formation of multidomain proteins.
    • (1998) Mol Biol Evol , vol.15 , pp. 665-682
    • Garcia-Vallve, S.1    Palau, J.2
  • 45
    • 0032545324 scopus 로고    scopus 로고
    • A remarkable synthesis of a cork-in-a-bottleneck pore structure. FhuA is located in the outer membrane of E. coli and one might have expected a static structure, like that of the porins. This work illustrates how a signal from the inside of the cell, mediated by TonB through the periplasm, might induce an allosteric transition moving the cork and allowing the iron-carrying siderophore to pass through FhuA
    • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W: Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide. Science 1998, 282:2215-2226. A remarkable synthesis of a cork-in-a-bottleneck pore structure. FhuA is located in the outer membrane of E. coli and one might have expected a static structure, like that of the porins. This work illustrates how a signal from the inside of the cell, mediated by TonB through the periplasm, might induce an allosteric transition moving the cork and allowing the iron-carrying siderophore to pass through FhuA.
    • (1998) Science , vol.282 , pp. 2215-2226
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 47
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • The long-awaited structure of the ATP-binding subunit of an ABC transporter, raising many new questions
    • Hung L-W, Wang IX, Nikaido K, Liu P-Q, Ames GF-L, Kim S-H: Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 1998, 396:703-707. The long-awaited structure of the ATP-binding subunit of an ABC transporter, raising many new questions.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.-W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.-Q.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 48
    • 0031796062 scopus 로고    scopus 로고
    • In vivo characterization of the drug resistance profile of the major ABC transporters and other components of the yeast pleiotropic drug resistance network
    • Kolaczkowski M, Kolaczowska A, Luczynski J, Witek S, Goffeau A: In vivo characterization of the drug resistance profile of the major ABC transporters and other components of the yeast pleiotropic drug resistance network. Microb Drug Resist 1998, 4:143-158.
    • (1998) Microb Drug Resist , vol.4 , pp. 143-158
    • Kolaczkowski, M.1    Kolaczowska, A.2    Luczynski, J.3    Witek, S.4    Goffeau, A.5
  • 49
    • 0024893581 scopus 로고
    • Homeotopic transformation and the origin of translation
    • Danchin A: Homeotopic transformation and the origin of translation. Prog Biophys Mol Biol 1989, 54:81-86.
    • (1989) Prog Biophys Mol Biol , vol.54 , pp. 81-86
    • Danchin, A.1
  • 50
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes. More than meets the eye
    • An illustration of the recruitment of new functions by existing structures
    • Piatigorsky J: Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann N Y Acad Sci 1998, 842:7-15. An illustration of the recruitment of new functions by existing structures.
    • (1998) Ann N Y Acad Sci , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 51
    • 0031792001 scopus 로고    scopus 로고
    • At the interface: Crystal structures of phospholipases A2
    • Ward RJ, de Azevedo WF Jr, Arni RK: At the interface: Crystal structures of phospholipases A2. Toxicon 1998, 36:1623-1633.
    • (1998) Toxicon , vol.36 , pp. 1623-1633
    • Ward, R.J.1    De Azevedo W.F., Jr.2    Arni, R.K.3
  • 52
    • 0032537722 scopus 로고    scopus 로고
    • Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
    • Carpenter EP, Hawkins AR, Frost JW, Brown KA: Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 1998, 394:299-302.
    • (1998) Nature , vol.394 , pp. 299-302
    • Carpenter, E.P.1    Hawkins, A.R.2    Frost, J.W.3    Brown, K.A.4
  • 53
    • 0032476667 scopus 로고    scopus 로고
    • The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases
    • Resolving the ribosome protein L25 structure illustrates the power of the new NMR techniques. It also raises major questions about the origin and fate of RNA-binding proteins. What are the similarities among sequences with a structure in common and do they display common functions?
    • Stoldt M, Wohnert J, Gorlach M, Brown LR: The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases. EMBO J 1998, 17:6377-6384. Resolving the ribosome protein L25 structure illustrates the power of the new NMR techniques. It also raises major questions about the origin and fate of RNA-binding proteins. What are the similarities among sequences with a structure in common and do they display common functions?
    • (1998) EMBO J , vol.17 , pp. 6377-6384
    • Stoldt, M.1    Wohnert, J.2    Gorlach, M.3    Brown, L.R.4
  • 54
    • 0031794743 scopus 로고    scopus 로고
    • Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
    • A very controversial view on the first cells found at the origin of life. Using sequence data correlated to the corresponding functions, Gupta reverts to the prokaryote/eukaryote dichotomy, proposing that Gram-positive eubacteria and archaebacteria form the original class (monoderms) and that Gram-negative eubacteria (diderms) engulfed an archaebacterial type to form the eukaryotic lineage
    • Gupta RS: Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes. Microbiol Mol Biol Rev 1998, 62:1435-1491. A very controversial view on the first cells found at the origin of life. Using sequence data correlated to the corresponding functions, Gupta reverts to the prokaryote/eukaryote dichotomy, proposing that Gram-positive eubacteria and archaebacteria form the original class (monoderms) and that Gram-negative eubacteria (diderms) engulfed an archaebacterial type to form the eukaryotic lineage.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1435-1491
    • Gupta, R.S.1
  • 55
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin H, Marahiel MA, Heinemann U: Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 1993, 364:164-168.
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 56
    • 0032167995 scopus 로고    scopus 로고
    • Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 å resolution
    • An important protein containing hypusine, an unusual amino acid, is described (see, also, [57])
    • Kim KK, Hung LW, Yokota H, Kim R, Kim SH: Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 å resolution. Proc Natl Acad Sci USA 1998, 95:10419-10424. An important protein containing hypusine, an unusual amino acid, is described (see, also, [57]).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10419-10424
    • Kim, K.K.1    Hung, L.W.2    Yokota, H.3    Kim, R.4    Kim, S.H.5
  • 57
    • 0032530708 scopus 로고    scopus 로고
    • Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 å resolution
    • Peat TS, Newman J, Waldo GS, Berendzen J, Terwilliger TC: Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 å resolution. Structure 1998, 6:1207-1214.
    • (1998) Structure , vol.6 , pp. 1207-1214
    • Peat, T.S.1    Newman, J.2    Waldo, G.S.3    Berendzen, J.4    Terwilliger, T.C.5
  • 58
    • 0033556127 scopus 로고    scopus 로고
    • RNA binding strategies of ribosomal proteins
    • Draper DE, Reynaldo LP: RNA binding strategies of ribosomal proteins. Nucleic Acids Res 1999, 27:381-388.
    • (1999) Nucleic Acids Res , vol.27 , pp. 381-388
    • Draper, D.E.1    Reynaldo, L.P.2
  • 59
    • 0028317640 scopus 로고
    • Adenylyl cyclases: A heterogeneous class of ATP-utilizing enzymes
    • Barzu O, Danchin A: Adenylyl cyclases: A heterogeneous class of ATP-utilizing enzymes. Prog Nucleic Acid Res Mol Biol 1994, 49:241-283.
    • (1994) Prog Nucleic Acid Res Mol Biol , vol.49 , pp. 241-283
    • Barzu, O.1    Danchin, A.2
  • 60
    • 0030901637 scopus 로고    scopus 로고
    • Structure of the adenylyl cyclase catalytic core
    • [Published erratum appears in Nature 1997, 388:204.]
    • Zhang G, Liu Y, Ruoho AE, Hurley JH: Structure of the adenylyl cyclase catalytic core. Nature 1997, 386:247-253. [Published erratum appears in Nature 1997, 388:204.]
    • (1997) Nature , vol.386 , pp. 247-253
    • Zhang, G.1    Liu, Y.2    Ruoho, A.E.3    Hurley, J.H.4
  • 61
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with GsαGTPγS
    • Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR: Crystal structure of the catalytic domains of adenylyl cyclase in a complex with GsαGTPγS. Science 1997, 278:1907-1916.
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 62
    • 0032584606 scopus 로고    scopus 로고
    • Mutations uncover a role for two magnesium ions in the catalytic mechanism of adenylyl cyclase
    • Zimmermann G, Zhou D, Taussig R: Mutations uncover a role for two magnesium ions in the catalytic mechanism of adenylyl cyclase. J Biol Chem 1998, 273:19650-19655.
    • (1998) J Biol Chem , vol.273 , pp. 19650-19655
    • Zimmermann, G.1    Zhou, D.2    Taussig, R.3
  • 63
    • 0031764044 scopus 로고    scopus 로고
    • Indigo: A world-wide-web review of genomes and gene functions
    • The concept of 'neighborhood' is illustrated in this review, showing how to use an inductive approach to understand, knowing its sequence, the function of a protein
    • Nitschké P, Guerdoux-Jamet P, Chiapello H, Faroux G, Hénaut C, Hénaut A, Danchin A: Indigo: A world-wide-web review of genomes and gene functions. FEMS Microbiol Rev 1998, 22:207-227. The concept of 'neighborhood' is illustrated in this review, showing how to use an inductive approach to understand, knowing its sequence, the function of a protein.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 207-227
    • Nitschké, P.1    Guerdoux-Jamet, P.2    Chiapello, H.3    Faroux, G.4    Hénaut, C.5    Hénaut, A.6    Danchin, A.7
  • 64
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • This paper looks towards the future of protein design
    • Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS: High-resolution protein design with backbone freedom. Science 1998, 282:1462-1467. This paper looks towards the future of protein design.
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber, T.4    Kim, P.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.