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Volumn 2, Issue 4, 2011, Pages 671-688

Functional capabilities of the earliest peptides and the emergence of life

Author keywords

Catgrips; Emergence of life; Hydrothermal mound; Nests; Niches; Peptides

Indexed keywords

AMYLOID; ANION; CATION; FERROUS SULFIDE; PEPTIDE; PHOSPHATE; POTASSIUM CHANNEL;

EID: 84055190859     PISSN: None     EISSN: 20734425     Source Type: Journal    
DOI: 10.3390/genes2040671     Document Type: Article
Times cited : (42)

References (83)
  • 2
    • 0023497732 scopus 로고
    • Selection by differential molecular survival: A possible mechanism of early chemical evolution
    • De Duve, C. Selection by differential molecular survival: A possible mechanism of early chemical evolution. Proc. Natl. Acad. Sci. USA 1987, 84, 8253-8256.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8253-8256
    • De, D.1
  • 4
    • 34347347191 scopus 로고    scopus 로고
    • On the origin of the translation system and the genetic code in the RNA world by means of natural selection, exaptation and subfunctionalization
    • doi:10.1186/1745-6150-2-14
    • Wolf, Y.I.; Koonin, E.V. On the origin of the translation system and the genetic code in the RNA world by means of natural selection, exaptation and subfunctionalization. Biol. Direct 2007, doi:10.1186/1745-6150-2-14.
    • (2007) Biol. Direct
    • Wolf, Y.I.1    Koonin, E.V.2
  • 5
    • 66149108671 scopus 로고    scopus 로고
    • Synthesis of activated pyrimidine ribonucleotides in prebiotically plausible conditions
    • Powner, M.W.; Gerland, B.; Sutherland, J.D. Synthesis of activated pyrimidine ribonucleotides in prebiotically plausible conditions. Nature 2009, 459, 239-242.
    • (2009) Nature , vol.459 , pp. 239-242
    • Powner, M.W.1    Gerland, B.2    Sutherland, J.D.3
  • 6
    • 0026742154 scopus 로고
    • Abiotic synthesis of amino acids under hydrothermal conditions and the origin of life: A perpetual phenomenon?
    • Hennet, R.J.-C.; Holm, N.G.; Engel, M.H. Abiotic synthesis of amino acids under hydrothermal conditions and the origin of life: A perpetual phenomenon? Naturwissenschaft 1992, 79, 361-365.
    • (1992) Naturwissenschaft , vol.79 , pp. 361-365
    • Hennet, R.J.-C.1    Holm, N.G.2    Engel, M.H.3
  • 7
    • 0030875872 scopus 로고    scopus 로고
    • The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front
    • Russell, M.J.; Hall, A.J. The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front. J. Geol. Soc. Lond. 1997, 154, 377-402.
    • (1997) J. Geol. Soc. Lond , vol.154 , pp. 377-402
    • Russell, M.J.1    Hall, A.J.2
  • 8
    • 36549019578 scopus 로고    scopus 로고
    • Evolution of Early Earth's Atmosphere, Hydrosphere, and Biosphere-Constraints from Ore Deposits; Kesler, S.E., Ohmoto, H., Eds.; Geological Society of America: Boulder, CO, USA
    • Russell, M.J.; Hall, A.J. The Onset and Early Evolution of Life. In Evolution of Early Earth's Atmosphere, Hydrosphere, and Biosphere-Constraints from Ore Deposits; Kesler, S.E., Ohmoto, H., Eds.; Geological Society of America: Boulder, CO, USA, 2006; Volume 198, pp. 1-32.
    • (2006) The Onset and Early Evolution of Life , vol.198 , pp. 1-32
    • Russell, M.J.1    Hall, A.J.2
  • 9
    • 0642285283 scopus 로고    scopus 로고
    • Exponential DNA replication by laminar convection
    • Braun, D.; Goddard, N.L.; Libchaber, A. Exponential DNA replication by laminar convection. Phys. Rev. Lett. 2003, 91, 158103.
    • (2003) Phys. Rev. Lett , vol.91 , pp. 158103
    • Braun, D.1    Goddard, N.L.2    Libchaber, A.3
  • 10
    • 27744591844 scopus 로고    scopus 로고
    • On the origin of genomes and cells within inorganic compartments
    • Koonin, E.; Martin, W. On the origin of genomes and cells within inorganic compartments. Trends Biochem. Sci. 2005, 21, 647-654.
    • (2005) Trends Biochem. Sci , vol.21 , pp. 647-654
    • Koonin, E.1    Martin, W.2
  • 13
    • 72449155029 scopus 로고    scopus 로고
    • Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge
    • Nitschke, W.; Russell, M.J. Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge. J. Mol. Evol. 2009, 69, 481-496.
    • (2009) J. Mol. Evol , vol.69 , pp. 481-496
    • Nitschke, W.1    Russell, M.J.2
  • 14
    • 35148861695 scopus 로고    scopus 로고
    • On the origin of biochemistry at an alkaline hydrothermal vent
    • Martin, W.; Russell, M.J. On the origin of biochemistry at an alkaline hydrothermal vent. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2007, 362, 1887-1925.
    • (2007) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.362 , pp. 1887-1925
    • Martin, W.1    Russell, M.J.2
  • 15
    • 84055209681 scopus 로고    scopus 로고
    • Precipitation Patterns of Iron Minerals in a Chemical Gradient: A Laboratory Analog to Hydrothermal Environments on the Early Earth
    • Woodlands, TX, USA, March 2011; LPI Contribution No. 1608
    • Barge, L.M.; Russell, M.J.; Kanik, I. Precipitation Patterns of Iron Minerals in a Chemical Gradient: A Laboratory Analog to Hydrothermal Environments on the Early Earth. In Proceedings of 42nd Lunar and Planetary Science Conference, Woodlands, TX, USA, 7-11 March 2011; LPI Contribution No. 1608, p.1099.
    • Proceedings of 42nd Lunar and Planetary Science Conference , pp. 7-11
    • Barge, L.M.1    Russell, M.J.2    Kanik, I.3
  • 18
    • 0024250242 scopus 로고
    • Condensation of oligoglycines with trimeta- and tetrametaphosphate in aqueous solutions
    • Yamanaka, J.; Inomata, K.; Yamagata, Y. Condensation of oligoglycines with trimeta- and tetrametaphosphate in aqueous solutions. Orig. Life Evol. Biosph. 1988, 18, 165-178.
    • (1988) Orig. Life Evol. Biosph , vol.18 , pp. 165-178
    • Yamanaka, J.1    Inomata, K.2    Yamagata, Y.3
  • 19
    • 0031196319 scopus 로고    scopus 로고
    • Condensation of glycylglycine to oligoglycines with trimetaphosphate in aqueous solution
    • Yamagata, Y.; Inomata, K. Condensation of glycylglycine to oligoglycines with trimetaphosphate in aqueous solution. Orig. Life Evol. Biosph. 1997, 27, 339-344.
    • (1997) Orig. Life Evol. Biosph , vol.27 , pp. 339-344
    • Yamagata, Y.1    Inomata, K.2
  • 20
    • 3242755111 scopus 로고    scopus 로고
    • The rocky roots of the acetyl coenzyme-A pathway
    • Russell, M.J.; Martin, W. The rocky roots of the acetyl coenzyme-A pathway. Trends Biochem. Sci. 2004, 24, 358-363.
    • (2004) Trends Biochem. Sci , vol.24 , pp. 358-363
    • Russell, M.J.1    Martin, W.2
  • 21
    • 78349267379 scopus 로고    scopus 로고
    • Why does life start, what does It do, where will it be, and how might we find it
    • Russell, M.J.; Kanik, I. Why does life start, what does It do, where will it be, and how might we find it? J. Cosmol. 2010, 5, 1008-1039.
    • (2010) J. Cosmol , vol.5 , pp. 1008-1039
    • Russell, M.J.1    Kanik, I.2
  • 22
    • 5044231005 scopus 로고    scopus 로고
    • Biomimetic phosphoryl transfer catalysed by iron(II)- mineral precipitates
    • de Zwart, I.I.; Meade, S.J.; Pratt, A.J. Biomimetic phosphoryl transfer catalysed by iron(II)- mineral precipitates. Geochim. Cosmochim. Acta 2004, 68, 4093-4098.
    • (2004) Geochim. Cosmochim. Acta , vol.68 , pp. 4093-4098
    • de Zwart, I.I.1    Meade, S.J.2    Pratt, A.J.3
  • 23
    • 0001202417 scopus 로고
    • Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences
    • Eck, R.V.; Dayhoff, M.O. Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences. Science 1966, 152, 363-366.
    • (1966) Science , vol.152 , pp. 363-366
    • Eck, R.V.1    Dayhoff, M.O.2
  • 24
    • 0015218669 scopus 로고
    • Role for ferredoxins in the origin of life and biological evolution
    • Hall, D.O.; Cammack, R.; Rao, K.K. Role for ferredoxins in the origin of life and biological evolution. Nature 1971, 233, 136-138.
    • (1971) Nature , vol.233 , pp. 136-138
    • Hall, D.O.1    Cammack, R.2    Rao, K.K.3
  • 25
    • 0035783055 scopus 로고    scopus 로고
    • On the evolution of protein folds: Are similar motifs the result of convergence, insertion or relics of an ancient peptide world
    • Lupas, A.N.; Ponting, C.P.; Russell, R.B. On the evolution of protein folds: Are similar motifs the result of convergence, insertion or relics of an ancient peptide world? J. Struct. Biol. 2001, 134, 191-203.
    • (2001) J. Struct. Biol , vol.134 , pp. 191-203
    • Lupas, A.N.1    Ponting, C.P.2    Russell, R.B.3
  • 26
    • 3042809615 scopus 로고    scopus 로고
    • Towards a structural classification of phosphate binding sites in protein-nucleotide complexes
    • Brakoulias, A.; Jackson, R.M. Towards a structural classification of phosphate binding sites in protein-nucleotide complexes. Proteins 2004, 56, 250-260.
    • (2004) Proteins , vol.56 , pp. 250-260
    • Brakoulias, A.1    Jackson, R.M.2
  • 28
    • 84055205317 scopus 로고    scopus 로고
    • An ancient protein fold links metal-based gas reactions with the RNA world
    • Volbeda, A.; Nicolet, Y.; Fontecilla-Camps, J. An ancient protein fold links metal-based gas reactions with the RNA world. J. Cosmol. 2010, 10, 3243-3257.
    • (2010) J. Cosmol , vol.10 , pp. 3243-3257
    • Volbeda, A.1    Nicolet, Y.2    Fontecilla-Camps, J.3
  • 29
    • 0028023065 scopus 로고
    • A hydrothermally precipitated catalytic iron sulphide membrane as a first step toward life
    • Russell, M.J.; Daniel, R.M.; Hall, A.J.; Sherringham, J. A hydrothermally precipitated catalytic iron sulphide membrane as a first step toward life. J. Mol. Evol. 1994, 39, 231-243.
    • (1994) J. Mol. Evol , vol.39 , pp. 231-243
    • Russell, M.J.1    Daniel, R.M.2    Hall, A.J.3    Sherringham, J.4
  • 30
    • 18644380729 scopus 로고    scopus 로고
    • Sites for phosphates and iron-sulfur thiolates in the first membranes: 3 to 6 residue anion binding motifs (nests)
    • Milner-White, E.J.; Russell, M.J. Sites for phosphates and iron-sulfur thiolates in the first membranes: 3 to 6 residue anion binding motifs (nests). Orig. Life Evol. Biosph. 2005, 35, 19-27.
    • (2005) Orig. Life Evol. Biosph , vol.35 , pp. 19-27
    • Milner-White, E.J.1    Russell, M.J.2
  • 32
    • 84055170486 scopus 로고    scopus 로고
    • Woolfson, A. Life without Genes; Flamingo: London, UK, 2000; ISBN:978-0006548744.
    • Woolfson, A.1
  • 33
    • 21044454225 scopus 로고    scopus 로고
    • Possible steps to the emergence of life: The [GADV]-protein world hypothesis
    • Ikehara, K. Possible steps to the emergence of life: The [GADV]-protein world hypothesis. Chem. Rec. 2005, 5, 107-118.
    • (2005) Chem. Rec , vol.5 , pp. 107-118
    • Ikehara, K.1
  • 34
    • 0017232521 scopus 로고
    • Coenzymes as fossils of an earlier metabolic state
    • White, H.B. Coenzymes as fossils of an earlier metabolic state. J. Mol. Evol. 1976, 7, 101-104.
    • (1976) J. Mol. Evol , vol.7 , pp. 101-104
    • White, H.B.1
  • 35
    • 79961096926 scopus 로고    scopus 로고
    • Getting past the RNA world: The initial Darwinian ancestor
    • doi:10.1101/cshperspect.a003590
    • Yarus, M. Getting past the RNA world: The initial Darwinian ancestor. Cold Spring Harb. Perspect. Biol. 2010, doi:10.1101/cshperspect.a003590.
    • (2010) Cold Spring Harb. Perspect. Biol
    • Yarus, M.1
  • 36
    • 0037450456 scopus 로고    scopus 로고
    • Primordial reductive amination revisited
    • Huber, C.; Wächtershäuser, G. Primordial reductive amination revisited. Tetrahedron Lett. 2003, 44, 1695-1697.
    • (2003) Tetrahedron Lett , vol.44 , pp. 1695-1697
    • Huber, C.1    Wächtershäuser, G.2
  • 37
    • 33744822163 scopus 로고    scopus 로고
    • The link between sequence and conformation in protein structures appears to be stereochemically established
    • Ramakrishnan, V.; Ranbhor, R.; Kumar, A.; Durani, S. The link between sequence and conformation in protein structures appears to be stereochemically established. J. Phys. Chem. B 2006, 110, 9314-9326.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 9314-9326
    • Ramakrishnan, V.1    Ranbhor, R.2    Kumar, A.3    Durani, S.4
  • 38
    • 62149127051 scopus 로고    scopus 로고
    • Motivated Proteins: A web application for studying small threedimensional protein motifs
    • Leader, D.P.; Milner-White, E.J. Motivated Proteins: A web application for studying small threedimensional protein motifs. BMC Bioinforma. 2009, 10, 60-64.
    • (2009) BMC Bioinforma , vol.10 , pp. 60-64
    • Leader, D.P.1    Milner-White, E.J.2
  • 39
    • 0036293842 scopus 로고    scopus 로고
    • A novel main-chain anion-binding site in proteins: The nest. A combination of f{cyrillic}, ψ values in successive residues gives rise to anion-binding sites that occur commonly and are found at functionally important regions
    • Watson, J.D.; Milner-White, E.J. A novel main-chain anion-binding site in proteins: The nest. A combination of Φ, ψ values in successive residues gives rise to anion-binding sites that occur commonly and are found at functionally important regions. J. Mol. Biol. 2002, 315, 171-182.
    • (2002) J. Mol. Biol , vol.315 , pp. 171-182
    • Watson, J.D.1    Milner-White, E.J.2
  • 40
    • 0036289154 scopus 로고    scopus 로고
    • The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins
    • Watson, J.D.; Milner-White, E.J. The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins. J. Mol. Biol. 2002, 315, 183-191.
    • (2002) J. Mol. Biol , vol.315 , pp. 183-191
    • Watson, J.D.1    Milner-White, E.J.2
  • 42
    • 0346035924 scopus 로고    scopus 로고
    • New principles of protein structure: Nests, eggs and what next?
    • Pal, D.; Suehnel, J.; Weiss, M. New principles of protein structure: Nests, eggs and what next? Angew. Chem. Int. Ed. 2002, 41, 4663-4665.
    • (2002) Angew. Chem. Int. Ed , vol.41 , pp. 4663-4665
    • Pal, D.1    Suehnel, J.2    Weiss, M.3
  • 43
    • 62449223308 scopus 로고    scopus 로고
    • Amino acid containing anion receptors
    • Kubik, S. Amino acid containing anion receptors. Chem. Soc. Rev. 2009, 38, 585-605.
    • (2009) Chem. Soc. Rev , vol.38 , pp. 585-605
    • Kubik, S.1
  • 44
    • 84855839895 scopus 로고    scopus 로고
    • De novo design of α,β-didehydrophenylalanine containing peptides
    • Gupta, M.; Chauhan, V.S. De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications. Biopolymers 2010, 6, 1-11.
    • (2010) From Models to Applications. Biopolymers , vol.6 , pp. 1-11
    • Gupta, M.1    Chauhan, V.S.2
  • 45
    • 1542708065 scopus 로고    scopus 로고
    • De novo design and characterization of a helical hairpin eicosapeptide: Emergence of an anion receptor in the linker region
    • Rudresh, A.; Ramakumar, S.; Ramagopal, U.A.; Inai, Y.; Goel, S.; Sahal, D.; Chauhan, V.S. De novo design and characterization of a helical hairpin eicosapeptide: emergence of an anion receptor in the linker region. Struct. Fold. Des. 2004, 12, 389-396.
    • (2004) Struct. Fold. Des , vol.12 , pp. 389-396
    • Rudresh, A.1    Ramakumar, S.2    Ramagopal, U.A.3    Inai, Y.4    Goel, S.5    Sahal, D.6    Chauhan, V.S.7
  • 46
    • 33644598465 scopus 로고    scopus 로고
    • Asymmetric enone epoxidation by short solid-phase bound peptides: Further evidence for catalyst helicity and catalytic activity of individual peptide strands
    • Berkessel, A.; Koch, B.; Toniolo, C.; Rainaldi, M.; Broxterman, Q.B.; Kaptein, B. Asymmetric enone epoxidation by short solid-phase bound peptides: Further evidence for catalyst helicity and catalytic activity of individual peptide strands. Biopolymers 2006, 84, 90-96.
    • (2006) Biopolymers , vol.84 , pp. 90-96
    • Berkessel, A.1    Koch, B.2    Toniolo, C.3    Rainaldi, M.4    Broxterman, Q.B.5    Kaptein, B.6
  • 47
    • 29944442301 scopus 로고    scopus 로고
    • Cation dependence of chloride ion complexation by open-chained receptor molecules in chloroform solution
    • Pajewski, R.; Ferdani, R.; Pajewska, J.; Li, R.; Gokel, G.W. Cation dependence of chloride ion complexation by open-chained receptor molecules in chloroform solution. J. Am. Chem. Soc. 2005, 127, 18281-18295.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 18281-18295
    • Pajewski, R.1    Ferdani, R.2    Pajewska, J.3    Li, R.4    Gokel, G.W.5
  • 48
    • 3042592410 scopus 로고    scopus 로고
    • The use of in vitro peptide library screens in the analysis of phosphoserine/phosphothreonine binding domain structure and function
    • Yaffe, M.B.; Smerdon, S.J. The use of in vitro peptide library screens in the analysis of phosphoserine/phosphothreonine binding domain structure and function. Annu. Rev. Biophys. Biomol. Struct. 2004, 33, 225-244.
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 225-244
    • Yaffe, M.B.1    Smerdon, S.J.2
  • 49
    • 33845377125 scopus 로고
    • Assembly of FenSn (SR)2- (n=2,4) in aqueous media from iron salts, thiols and sulfur, sulfide, thiosulfide plus rhodanese
    • Bonomi, F.; Werth, M.T.; Kurtz, D.M. Assembly of FenSn (SR)2- (n=2,4) in aqueous media from iron salts, thiols and sulfur, sulfide, thiosulfide plus rhodanese. Inorg. Chem. 1985, 24, 4331-4335.
    • (1985) Inorg. Chem , vol.24 , pp. 4331-4335
    • Bonomi, F.1    Werth, M.T.2    Kurtz, D.M.3
  • 50
    • 39349107507 scopus 로고    scopus 로고
    • Predicting the conformations of peptides and proteins in early evolution
    • doi:10.1186/1745-6150-3-3
    • Milner-White, E.J.; Russell, M.J. Predicting the conformations of peptides and proteins in early evolution. Biol. Direct. 2008, doi:10.1186/1745-6150-3-3.
    • (2008) Biol. Direct
    • Milner-White, E.J.1    Russell, M.J.2
  • 51
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K1 channel-Fab complex at 2.0Å resolution
    • Zhou, Y.F.; Morais-Cabral, J.H.; Kaufman, A.; MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K1 channel-Fab complex at 2.0Å resolution. Nature 2001, 414, 43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.F.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 52
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui, H.; Han, B-G.; Lee, J.K.; Wallan, P.; Jap, B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature 2001, 414, 872-878.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Wallan, P.4    Jap, B.K.5
  • 53
    • 76549238253 scopus 로고
    • The pleated sheet, a new layer configuration of polypeptide chains
    • Pauling, L.; Corey, R.B. The pleated sheet, a new layer configuration of polypeptide chains. Proc. Natl. Acad. Sci. USA 1951, 37, 251-256.
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 251-256
    • Pauling, L.1    Corey, R.B.2
  • 54
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • Armen, R.S.; DeMarco, M.L.; Alonso, D.O.V.; Daggett, V. Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc. Natl. Acad. Sci. USA 2004, 101, 11622-11627.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11622-11627
    • Armen, R.S.1    Demarco, M.L.2    Alonso, D.O.V.3    Daggett, V.4
  • 55
    • 33749857843 scopus 로고    scopus 로고
    • α-sheet: The toxic conformer in amyloid diseases
    • Daggett, V. α-sheet: The toxic conformer in amyloid diseases? Acc. Chem. Res. 2006, 39, 594-602.
    • (2006) Acc. Chem. Res , vol.39 , pp. 594-602
    • Daggett, V.1
  • 56
    • 33748447891 scopus 로고    scopus 로고
    • Amyloid formation may involve α- to β-sheet interconversion via peptide plane flipping
    • Milner-White, E.J.; Watson, J.D.; Qi, G.; Hayward, S. Amyloid formation may involve α- to β-sheet interconversion via peptide plane flipping. Structure 2006, 14, 1369-1376.
    • (2006) Structure , vol.14 , pp. 1369-1376
    • Milner-White, E.J.1    Watson, J.D.2    Qi, G.3    Hayward, S.4
  • 57
    • 40549126970 scopus 로고    scopus 로고
    • The geometry of α-sheet: Implications for its possible function as amyloid precursor in proteins
    • Hayward, S.; Milner-White, E.J. The geometry of α-sheet: Implications for its possible function as amyloid precursor in proteins. Proteins 2008, 71, 415-425.
    • (2008) Proteins , vol.71 , pp. 415-425
    • Hayward, S.1    Milner-White, E.J.2
  • 58
    • 84855828550 scopus 로고    scopus 로고
    • Simulation of the α- to β-sheet transition results in a twisted sheet for antiparallel and an α-nanotube for parallel strands
    • In Press
    • Hayward, S.; Milner-White, E.J. Simulation of the α- to β-sheet transition results in a twisted sheet for antiparallel and an α-nanotube for parallel strands. Implications for amyloid formation. Proteins 2011, In Press.
    • (2011) Implications For Amyloid Formation. Proteins
    • Hayward, S.1    Milner-White, E.J.2
  • 60
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin-even an ordinary globular protein can assume a rogue guise if conditions are right
    • Fandrich, M.; Fletcher, M.A.; Dobson, C.M. Amyloid fibrils from muscle myoglobin-even an ordinary globular protein can assume a rogue guise if conditions are right. Nature 2001, 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 61
    • 68049114613 scopus 로고    scopus 로고
    • Self-propagating β-sheet polypeptide structures as prebiotic informational molecular entities: The amyloid world
    • Maury, C.P.J. Self-propagating β-sheet polypeptide structures as prebiotic informational molecular entities: The amyloid world. Orig. Life Evol. Biosph. 2009, 39, 141-150.
    • (2009) Orig. Life Evol. Biosph , vol.39 , pp. 141-150
    • Maury, C.P.J.1
  • 62
    • 79955761085 scopus 로고    scopus 로고
    • Structural insights into functional and pathological amyloid
    • Shewmaker, F.; McGlinchey, R.P.; Wickner, R.B. Structural insights into functional and pathological amyloid. J. Biol. Chem. 2011, 286, 16533-16540.
    • (2011) J. Biol. Chem , vol.286 , pp. 16533-16540
    • Shewmaker, F.1    McGlinchey, R.P.2    Wickner, R.B.3
  • 63
    • 0000406389 scopus 로고    scopus 로고
    • Amino terminal Cu(II) and Ni(II) binding ATCUN motif of proteins and peptides
    • Harford, C.; Sarkar, B. Amino terminal Cu(II) and Ni(II) binding ATCUN motif of proteins and peptides. Acc. Chem. Res. 1999, 30, 123-130.
    • (1999) Acc. Chem. Res , vol.30 , pp. 123-130
    • Harford, C.1    Sarkar, B.2
  • 64
    • 0000602652 scopus 로고
    • The association of nickel(II) ion with peptides
    • Martin, R.B.; Chamberlin, M.; Edsal, J.T. The association of nickel(II) ion with peptides. J. Am. Chem. Soc. 1960, 82, 495-498.
    • (1960) J. Am. Chem. Soc , vol.82 , pp. 495-498
    • Martin, R.B.1    Chamberlin, M.2    Edsal, J.T.3
  • 65
    • 33947336002 scopus 로고
    • Metal ion exchange of square-planar nickel(II) tetraglycine with polydentate amines
    • Ma, N.W.H.; White, D.A.; Martin, R.B. Metal ion exchange of square-planar nickel(II) tetraglycine with polydentate amines. Inorg. Chem. 1967, 6, 1632-1636.
    • (1967) Inorg. Chem , vol.6 , pp. 1632-1636
    • Ma, N.W.H.1    White, D.A.2    Martin, R.B.3
  • 66
    • 0742321266 scopus 로고    scopus 로고
    • Sulfite induced autoxidation of Ni(II) and Co(II) tetraglycine complexes. Spectrophotometric and rotating ring-disc voltammetric studies
    • Alipázaga, M.V.; Lowinsohn, D.; Bertotti, M.; Coichev, N. Sulfite induced autoxidation of Ni(II) and Co(II) tetraglycine complexes. Spectrophotometric and rotating ring-disc voltammetric studies. Dalton Trans. 2004, 267-272.
    • (2004) Dalton Trans , pp. 267-272
    • Alipázaga, M.V.1    Lowinsohn, D.2    Bertotti, M.3    Coichev, N.4
  • 67
    • 58149356979 scopus 로고    scopus 로고
    • A novel main chain motif in proteins bridged by cationic groups: The niche
    • Torrance, G.M.; Leader, D.P.; Gilbert, D.R.; Milner-White, E.J. A novel main chain motif in proteins bridged by cationic groups: The niche. J. Mol. Biol. 2009, 385, 1076-1086.
    • (2009) J. Mol. Biol , vol.385 , pp. 1076-1086
    • Torrance, G.M.1    Leader, D.P.2    Gilbert, D.R.3    Milner-White, E.J.4
  • 68
    • 0029171446 scopus 로고
    • Abiotic synthesis of organic compounds under the conditions of submarine hydrothermal systems: A perspective
    • Holm, N.G.; Anderson, E.M. Abiotic synthesis of organic compounds under the conditions of submarine hydrothermal systems: A perspective. Planet. Space Sci. 1995, 43, I53-159.
    • (1995) Planet. Space Sci , vol.43 , pp. 153-159
    • Holm, N.G.1    Anderson, E.M.2
  • 69
    • 34447130835 scopus 로고    scopus 로고
    • Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs
    • Gifford, J.L.; Walsh, M.P.; Vogel, H.J. Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem. J. 2007, 405, 199-221.
    • (2007) Biochem. J , vol.405 , pp. 199-221
    • Gifford, J.L.1    Walsh, M.P.2    Vogel, H.J.3
  • 70
    • 78649747986 scopus 로고    scopus 로고
    • Closed headpiece of integrin aIIbb3 and its complex with an antagonist that does not induce opening
    • Zhu, J.; Zhu, J.; Negri, A.; Provasi, D.; Filizola, M.; Coller, B.S.; Springer, T. Closed headpiece of integrin aIIbb3 and its complex with an antagonist that does not induce opening. Blood 2011, 116, 5050-5061.
    • (2011) Blood , vol.116 , pp. 5050-5061
    • Zhu, J.1    Zhu, J.2    Negri, A.3    Provasi, D.4    Filizola, M.5    Coller, B.S.6    Springer, T.7
  • 71
    • 70350567248 scopus 로고    scopus 로고
    • The first peptides: The evolutionary transition between prebiotic amino acids and early proteins
    • Van der Gulik, P.; Massar, S.; Gilis, D.; Buhrman, H.; Rooman, M. The first peptides: The evolutionary transition between prebiotic amino acids and early proteins. J. Theor. Biol. 2009, 261, 531-539.
    • (2009) J. Theor. Biol , vol.261 , pp. 531-539
    • van der Gulik, P.1    Massar, S.2    Gilis, D.3    Buhrman, H.4    Rooman, M.5
  • 72
    • 0037791613 scopus 로고    scopus 로고
    • Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases
    • Iyer, L.M.; Koonin, E.V.; Aravind, L. Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases. BMC Struct. Biol. 2003, 3:1.
    • (2003) BMC Struct. Biol , vol.3 , pp. 1
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 74
    • 1642452663 scopus 로고    scopus 로고
    • Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa
    • Regni, C.; Naught, L.; Tipton, P.A.; Beamer, L.J. Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure 2004, 12, 55-63.
    • (2004) Structure , vol.12 , pp. 55-63
    • Regni, C.1    Naught, L.2    Tipton, P.A.3    Beamer, L.J.4
  • 75
    • 78349253629 scopus 로고    scopus 로고
    • Polyphosphate-peptide synergy and the organic takeover at the emergence of life
    • Milner-White, E.J.; Russell, M.J. Polyphosphate-peptide synergy and the organic takeover at the emergence of life. J. Cosmol. 2010, 10, 3217-3229.
    • (2010) J. Cosmol , vol.10 , pp. 3217-3229
    • Milner-White, E.J.1    Russell, M.J.2
  • 76
    • 77956825055 scopus 로고
    • Inorganic pyrophosphate and inorganic pyrophosphatases
    • Baltscheffsky, M.; Baltscheffsky, H. Inorganic pyrophosphate and inorganic pyrophosphatases. Mol. Mechan. Bioenerg. 1992, 23, 331-348.
    • (1992) Mol. Mechan. Bioenerg , vol.23 , pp. 331-348
    • Baltscheffsky, M.1    Baltscheffsky, H.2
  • 77
    • 57649134961 scopus 로고    scopus 로고
    • Mutual effect of cationic ligands and substrate on activity of the Na+-transporting pyrophosphatase of Methanosarcina mazei
    • Malinen, A.M.; Baykov, A.A.; Lahti, R. Mutual effect of cationic ligands and substrate on activity of the Na+-transporting pyrophosphatase of Methanosarcina mazei. Biochemistry 2008, 47, 13447-13454.
    • (2008) Biochemistry , vol.47 , pp. 13447-13454
    • Malinen, A.M.1    Baykov, A.A.2    Lahti, R.3
  • 78
    • 80052961156 scopus 로고    scopus 로고
    • Links between hydrothermal environments, pyrophosphate, Na+ and early evolution
    • doi:10.1007/s11084-011-9235-4
    • Holm, N.G.; Baltscheffsky, H. Links between hydrothermal environments, pyrophosphate, Na+ and early evolution. Orig. Life Evol. Biosph. 2011, 41, doi:10.1007/s11084-011-9235-4.
    • (2011) Orig. Life Evol. Biosph , vol.41
    • Holm, N.G.1    Baltscheffsky, H.2
  • 79
    • 33750539554 scopus 로고    scopus 로고
    • Analysis of ancient sequence motifs in the H+-PPase family
    • Hedlund, J.; Cantoni, R.; Baltscheffsky, M.; Baltscheffsky, H. Analysis of ancient sequence motifs in the H+-PPase family. FEBS J. 2006, 273, 5183-5193.
    • (2006) FEBS J , vol.273 , pp. 5183-5193
    • Hedlund, J.1    Cantoni, R.2    Baltscheffsky, M.3    Baltscheffsky, H.4
  • 80
    • 0028184159 scopus 로고
    • Hydrothermal and oceanic pH conditions at 4Ga relevant to the origin of life
    • Macleod, G.; Mckeown, C.; Hall, A.J.; Russell, M.J. Hydrothermal and oceanic pH conditions at 4Ga relevant to the origin of life. Orig. Life Evol. Biosph. 1994, 24, 19-41.
    • (1994) Orig. Life Evol. Biosph , vol.24 , pp. 19-41
    • Macleod, G.1    McKeown, C.2    Hall, A.J.3    Russell, M.J.4
  • 82
    • 0014688015 scopus 로고
    • Peptide formation in the presence of linear or cyclic polyphosphates
    • Rabinowitz, J.; Flores, R.; Krebsback, R.; Rogers, G. Peptide formation in the presence of linear or cyclic polyphosphates. Nature 1969, 224, 795-796.
    • (1969) Nature , vol.224 , pp. 795-796
    • Rabinowitz, J.1    Flores, R.2    Krebsback, R.3    Rogers, G.4
  • 83
    • 38349066158 scopus 로고    scopus 로고
    • α-amino acid behaves differently from β- and γ- amino acids as treated by metaphosphate
    • Gao, X, Liu, Y, Cai, Y.M. Zhao, Y.F. α-amino acid behaves differently from β- and γ- amino acids as treated by metaphosphate. Amino Acids 2008, 34, 47-53.
    • (2008) Amino Acids , vol.34 , pp. 47-53
    • Gao, X.1    Liu, Y.2    Cai, Y.M.3    Zhao, Y.F.4


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