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Volumn 106, Issue 9, 2009, Pages 3107-3112

Scaling and self-organized criticality in proteins I

Author keywords

Hydrophobicity; Repeat; Scaling

Indexed keywords

AMINO ACID; LEUCINE; PROTEIN SUBUNIT; SCAFFOLD PROTEIN; SYNAPSIN I;

EID: 62549145387     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811262106     Document Type: Article
Times cited : (34)

References (33)
  • 1
    • 5844290410 scopus 로고
    • Self-organized criticality: An explanation of the 1/f noise
    • Bak P, Tang C, Wiesenfeld K (1987) Self-organized criticality: An explanation of the 1/f noise. Phys Rev Lett 59:381-384.
    • (1987) Phys Rev Lett , vol.59 , pp. 381-384
    • Bak, P.1    Tang, C.2    Wiesenfeld, K.3
  • 2
    • 0000160958 scopus 로고
    • Sweeping of an instability: An alternative to self-organized criticality to get power laws without parameter tuning
    • Sornette D (1994) Sweeping of an instability: An alternative to self-organized criticality to get power laws without parameter tuning. J Phys I [French] 4:209-221.
    • (1994) J Phys I [French] , vol.4 , pp. 209-221
    • Sornette, D.1
  • 4
    • 43149124630 scopus 로고    scopus 로고
    • Abrupt boundaries of intermediate phases and space filling in oxide glasses
    • Rompicharla K, et al. (2008) Abrupt boundaries of intermediate phases and space filling in oxide glasses. J Phys Condens Matter 20:202101.
    • (2008) J Phys Condens Matter , vol.20 , pp. 202101
    • Rompicharla, K.1
  • 5
    • 33751217712 scopus 로고    scopus 로고
    • Self-organization vs. self-ordering events in life-origin models
    • Abel DL, Trevors JT (2006) Self-organization vs. self-ordering events in life-origin models. Phys Life Rev 3:211-228.
    • (2006) Phys Life Rev , vol.3 , pp. 211-228
    • Abel, D.L.1    Trevors, J.T.2
  • 6
    • 15544372313 scopus 로고    scopus 로고
    • The architecture of the protein domain universe
    • Dokholyan NV (2005) The architecture of the protein domain universe. Gene 347:199-206.
    • (2005) Gene , vol.347 , pp. 199-206
    • Dokholyan, N.V.1
  • 7
    • 33846546999 scopus 로고    scopus 로고
    • Amino acid hydrophobicity and accessible surface area
    • Moret MA, Zebende GF (2007) Amino acid hydrophobicity and accessible surface area. Phys Rev E 75:011920.
    • (2007) Phys Rev E , vol.75 , pp. 011920
    • Moret, M.A.1    Zebende, G.F.2
  • 8
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 9
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler D (2005) Interfaces and the driving force of hydrophobic assembly. Nature 437:640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 11
    • 17644446703 scopus 로고    scopus 로고
    • Effective interactions cannot replace solvent effects in a lattice model of proteins
    • Salvi G, De Los Rios P (2003) Effective interactions cannot replace solvent effects in a lattice model of proteins. Phys Rev Lett 91:258102.
    • (2003) Phys Rev Lett , vol.91 , pp. 258102
    • Salvi, G.1    De Los Rios, P.2
  • 12
    • 40849116814 scopus 로고    scopus 로고
    • Maximum entropy approach for deducing amino acid interactions in proteins
    • Seno F, Trovato A, Banavar JR, Maritan A (2008) Maximum entropy approach for deducing amino acid interactions in proteins. Phys Rev Lett 100:078102.
    • (2008) Phys Rev Lett , vol.100 , pp. 078102
    • Seno, F.1    Trovato, A.2    Banavar, J.R.3    Maritan, A.4
  • 13
    • 0034306119 scopus 로고    scopus 로고
    • When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
    • Kobe B, Kajava AV (2000) When protein folding is simplified to protein coiling: The continuum of solenoid protein structures. Trends Biochem Sci 25:509-515.
    • (2000) Trends Biochem Sci , vol.25 , pp. 509-515
    • Kobe, B.1    Kajava, A.V.2
  • 14
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar AP, DuBay KF, Zurdo J, Vendruscolo M, Dobson CM (2005) Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J Mol Biol 350:379-392.
    • (2005) J Mol Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 15
    • 0035946941 scopus 로고    scopus 로고
    • Comparison of ARM and HEAT protein repeats
    • Andrade M, Petosa C, O'Donoghue S (2001) Comparison of ARM and HEAT protein repeats. J Mol Biol 309:1-18.
    • (2001) J Mol Biol , vol.309 , pp. 1-18
    • Andrade, M.1    Petosa, C.2    O'Donoghue, S.3
  • 16
    • 33750011953 scopus 로고    scopus 로고
    • The evolution of biased codon and amino acid usage in nematode genomes
    • Cutter AD, Wasmuth JD, Blaxter ML (2006) The evolution of biased codon and amino acid usage in nematode genomes. Mol Biol Evol 23:2303-2315.
    • (2006) Mol Biol Evol , vol.23 , pp. 2303-2315
    • Cutter, A.D.1    Wasmuth, J.D.2    Blaxter, M.L.3
  • 17
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV (2001) The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 11:725-732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 19
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D (1999) The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell 96:99-110.
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 20
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho US, Xu WQ (2007) Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445:53-57.
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.Q.2
  • 21
    • 34447106751 scopus 로고    scopus 로고
    • PP2A: Unveiling a reluctant tumor suppressor
    • Mumby M (2007) PP2A: Unveiling a reluctant tumor suppressor. Cell 130:21-24.
    • (2007) Cell , vol.130 , pp. 21-24
    • Mumby, M.1
  • 22
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • Michaely P, Tomchick DR, Machius M, Anderson RGW (2002) Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J 21:6387-6396.
    • (2002) EMBO J , vol.21 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.W.4
  • 24
    • 33846611978 scopus 로고    scopus 로고
    • TPRpred:Atool for prediction of TPR-, PPR- and SELI-like repeats from protein sequences
    • Karpenahalli MR, Lupas AN, Soding J (2007) TPRpred:Atool for prediction of TPR-, PPR- and SELI-like repeats from protein sequences. BMC Bioinform 8:2.
    • (2007) BMC Bioinform , vol.8 , pp. 2
    • Karpenahalli, M.R.1    Lupas, A.N.2    Soding, J.3
  • 25
    • 49449111983 scopus 로고    scopus 로고
    • Competing interactions create functionality through frustration
    • Lubchenko V (2008) Competing interactions create functionality through frustration. Proc Natl Acad Sci USA 105:10635-10636.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10635-10636
    • Lubchenko, V.1
  • 26
    • 33646931471 scopus 로고    scopus 로고
    • Protein folding thermodynamics and dynamics: Where physics, chemistry, and biology meet
    • Shakhnovich E (2006) Protein folding thermodynamics and dynamics: Where physics, chemistry, and biology meet. Chem Rev 106:1559-1588.
    • (2006) Chem Rev , vol.106 , pp. 1559-1588
    • Shakhnovich, E.1
  • 27
    • 0020491423 scopus 로고
    • The hydrophobic interaction is long-range, decaying exponentially with distance
    • Israelachvili JN, Pashley RM (1982) The hydrophobic interaction is long-range, decaying exponentially with distance. Nature 300:341-342.
    • (1982) Nature , vol.300 , pp. 341-342
    • Israelachvili, J.N.1    Pashley, R.M.2
  • 28
    • 48849107165 scopus 로고    scopus 로고
    • Determination of ligand-binding sites on proteins using long-range hydrophobic potential
    • Yamaotsu N, Oda A, Hirono S (2008) Determination of ligand-binding sites on proteins using long-range hydrophobic potential. Biol Pharm Bull 31:1552-1558.
    • (2008) Biol Pharm Bull , vol.31 , pp. 1552-1558
    • Yamaotsu, N.1    Oda, A.2    Hirono, S.3
  • 29
    • 43949086047 scopus 로고    scopus 로고
    • Thermoreversible lysozyme hydrogels: Properties and an insight into the gelation pathway
    • Yan H, et al. (2008) Thermoreversible lysozyme hydrogels: Properties and an insight into the gelation pathway. Soft Matter 4:1313-1325.
    • (2008) Soft Matter , vol.4 , pp. 1313-1325
    • Yan, H.1
  • 30
    • 39149098445 scopus 로고    scopus 로고
    • Designed armadillo repeat proteins as general peptide-binding scaffolds: Consensus design and computational optimization of the hydrophobic core
    • Parmeggiani F, et al. (2008) Designed armadillo repeat proteins as general peptide-binding scaffolds: Consensus design and computational optimization of the hydrophobic core. J Mol Biol 376:1282-1304.
    • (2008) J Mol Biol , vol.376 , pp. 1282-1304
    • Parmeggiani, F.1
  • 31
    • 55549101623 scopus 로고    scopus 로고
    • DNA sequencing of a cytogenetically normal acute myeloid leukemia genome
    • Ley TJ, et al. (2008) DNA sequencing of a cytogenetically normal acute myeloid leukemia genome. Nature 456:66-72.
    • (2008) Nature , vol.456 , pp. 66-72
    • Ley, T.J.1
  • 32
    • 0026650732 scopus 로고
    • PROFILEGRAPH: An interactive graphical tool for protein sequence analysis
    • Hofmann K, Stoffel W (1992) PROFILEGRAPH: An interactive graphical tool for protein sequence analysis. Bioinformatics 8:331-337.
    • (1992) Bioinformatics , vol.8 , pp. 331-337
    • Hofmann, K.1    Stoffel, W.2
  • 33
    • 62549113538 scopus 로고    scopus 로고
    • Scaling and self-organized criticality in proteins II
    • 10.1073/pnas.0811308106
    • Phillips JC (2009) Scaling and self-organized criticality in proteins II. Proc Natl Acad Sci USA 10.1073/pnas.0811308106.
    • (2009) Proc Natl Acad Sci USA
    • Phillips, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.