메뉴 건너뛰기




Volumn 2, Issue , 2013, Pages

Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water

Author keywords

[No Author keywords available]

Indexed keywords

ANION; INTEGRAL MEMBRANE PROTEIN; INTRINSICALLY INSOLUBLE PROTEIN; MAJOR SPERM PROTEIN; MEMBRANE PROTEIN; PROTEIN; PROTEIN SH3; SODIUM CHLORIDE; UNCLASSIFIED DRUG; VESICLE ASSOCIATED MEMBRANE PROTEIN B; VESICLE ASSOCIATED MEMBRANE PROTEIN B3; WATER;

EID: 84905451354     PISSN: 20461402     EISSN: 1759796X     Source Type: Journal    
DOI: 10.12688/f1000research.2-94.v1     Document Type: Article
Times cited : (35)

References (126)
  • 1
    • 0004146634 scopus 로고
    • What is Life?
    • Reference Source, Cambridge University Press
    • Schrödinger E: What is Life?Cambridge University Press,1944. Reference Source
    • (1944)
    • Schrödinger, E.1
  • 2
    • 85040139145 scopus 로고
    • GAIA - A New Look at Life on Earth
    • Reference Source, Oxford University Press
    • Lovelock J: GAIA - A New Look at Life on Earth; Oxford University Press,1979. Reference Source
    • (1979)
    • Lovelock, J.1
  • 3
  • 4
    • 57649114778 scopus 로고    scopus 로고
    • Why did life emerge?
    • Annila A Annila E: Why did life emerge? Int J Astrobiol. 2008;7(3-4):293-300. 10.1017/S1473550408004308
    • (2008) Int J Astrobiol , vol.7 , Issue.3-4 , pp. 293-300
    • Annila, A.1    Annila, E.2
  • 5
    • 33847219928 scopus 로고    scopus 로고
    • Natural process-Natural selection
    • 17289252, xxxx
    • Sharma V Annila A: Natural process-Natural selection. Biophys Chem. 2007;127(1-2):123-128. 17289252 10.1016/j.bpc.2007.01.005 xxxx
    • (2007) Biophys Chem , vol.127 , Issue.1-2 , pp. 123-128
    • Sharma, V.1    Annila, A.2
  • 6
    • 46749093044 scopus 로고    scopus 로고
    • Chirality and life
    • Barron LD: Chirality and life. Space Sci Rev. 2008;135(1-4):187-201. 10.1007/s11214-007-9254-7
    • (2008) Space Sci Rev , vol.135 , Issue.1-4 , pp. 187-201
    • Barron, L.D.1
  • 7
    • 84865619571 scopus 로고    scopus 로고
    • Chiroptical signatures of life and fundamental physics
    • 22730157
    • MacDermott AJ: Chiroptical signatures of life and fundamental physics. Chirality. 2012;24(9):764-769. 22730157 10.1002/chir.22076
    • (2012) Chirality , vol.24 , Issue.9 , pp. 764-769
    • MacDermott, A.J.1
  • 8
    • 84865812140 scopus 로고    scopus 로고
    • Genomics. ENCODE Project Writes Eulogy For Junk DNA
    • 22955811
    • Pennisi E: Genomics. ENCODE Project Writes Eulogy For Junk DNA. Science. 2012;337(6099):1159-1161. 22955811 10.1126/science.337.6099.1159
    • (2012) Science , vol.337 , Issue.6099 , pp. 1159-1161
    • Pennisi, E.1
  • 9
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • 4124164
    • Anfinsen CB: Principles that govern the folding of protein chains. Science. 1973;181(4096):223-230. 4124164 10.1126/science.181.4096.223
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 10
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Reference Source
    • Levinthal C: Are there pathways for protein folding? J Chim Phys. 1968;65(xx):44-45. Reference Source
    • (1968) J Chim Phys , vol.65 , Issue.20 , pp. 44-45
    • Levinthal, C.1
  • 11
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • 6287919
    • Kim PS Baldwin RL: Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem. 1982;51:459-489. 6287919 10.1146/annurev.bi.51.070182.002331
    • (1982) Annu Rev Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 12
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • 8989315
    • Dill KA Chan HS: From Levinthal to pathways to funnels. Nat Struct Biol. 1997;4(1):10-9. 8989315 10.1038/nsb0197-10
    • (1997) Nat Struct Biol , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 13
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • 14404936
    • Kauzmann W: Some factors in the interpretation of protein denaturation. Adv Protein Chem. 1959;14:1-63. 14404936 10.1016/s0065-3233(08)60608-7
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 14
    • 0017884417 scopus 로고
    • The hydrophobic effect and the organization of living matter
    • 653353, xxxx
    • Tanford C: The hydrophobic effect and the organization of living matter. Science. 1978;200(4345):1012-1018. 653353 10.1126/science.653353 xxxx
    • (1978) Science , vol.200 , Issue.4345 , pp. 1012-1018
    • Tanford, C.1
  • 15
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • 2207096
    • Dill KA: Dominant forces in protein folding. Biochemistry. 1990;29(31):7133-7155. 2207096 10.1021/bi00483a001
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 16
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • 16193038
    • Chandler D: Interfaces and the driving force of hydrophobic assembly. Nature. 2005;437(7059):640-647. 16193038 10.1038/nature04162
    • (2005) Nature , vol.437 , Issue.7059 , pp. 640-647
    • Chandler, D.1
  • 17
    • 0032479326 scopus 로고    scopus 로고
    • Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule
    • 9653039
    • Song J Bai P Luo L: Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule. J Mol Biol. 1998;280(1):167-74. 9653039 10.1006/jmbi.1998.1826
    • (1998) J Mol Biol , vol.280 , Issue.1 , pp. 167-174
    • Song, J.1    Bai, P.2    Luo, L.3
  • 18
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • 15738986
    • Dyson HJ Wright PE: Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol. 2005;6(3):197-208. 15738986 10.1038/nrm1589
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • 15943980
    • Tompa P: The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005;579(15):3346-3354. 15943980 10.1016/j.febslet.2005.03.072
    • (2005) FEBS Lett , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 20
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • 11025552
    • Uversky VN Gillespie JR Fink AL: Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins. 2000;41(3):415-427. 11025552 10.1002/1097-0134(20001115)41:3&<415::AID-PROT130&>3.0.CO;2-7
    • (2000) Proteins , vol.41 , Issue.3 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 21
    • 34249876378 scopus 로고    scopus 로고
    • The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications
    • 17397058
    • Li M Song J: The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. Proteins. 2007;68(1):100-108. 17397058 10.1002/prot.21385
    • (2007) Proteins , vol.68 , Issue.1 , pp. 100-108
    • Li, M.1    Song, J.2
  • 22
    • 37449005942 scopus 로고    scopus 로고
    • A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active
    • 18078811
    • Liu J Song J: A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. Biochem Biophys Res Commun. 2008;366(2):585-591. 18078811 10.1016/j.bbrc.2007.12.022
    • (2008) Biochem Biophys Res Commun , vol.366 , Issue.2 , pp. 585-591
    • Liu, J.1    Song, J.2
  • 23
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life
    • 22702725
    • Xue B Dunker AK Uversky VN: Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn. 2012;30(2):137-49. 22702725 10.1080/07391102.2012.675145
    • (2012) J Biomol Struct Dyn , vol.30 , Issue.2 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 24
    • 41149150251 scopus 로고    scopus 로고
    • Water: water - an enduring mystery
    • 18354466
    • Ball P: Water: water - an enduring mystery. Nature. 2008;452(7185):291-292. 18354466 10.1038/452291a
    • (2008) Nature , vol.452 , Issue.7185 , pp. 291-292
    • Ball, P.1
  • 25
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • 18095715
    • Ball P: Water as an active constituent in cell biology. Chem Rev. 2008;108(1):74-108. 18095715 10.1021/cr068037a
    • (2008) Chem Rev , vol.108 , Issue.1 , pp. 74-108
    • Ball, P.1
  • 26
    • 61749096920 scopus 로고    scopus 로고
    • Insight into "insoluble proteins" with pure water
    • 19233178
    • Song J: Insight into "insoluble proteins" with pure water. FEBS Letts. 2009;583(6):953-959. 19233178 10.1016/j.febslet.2009.02.022
    • (2009) FEBS Letts , vol.583 , Issue.6 , pp. 953-959
    • Song, J.1
  • 27
    • 0037058913 scopus 로고    scopus 로고
    • Slaving: solvent fluctuations dominate protein dynamics and functions
    • 12444262, 138562
    • Fenimore PW Frauenfelder H McMahon BH: Slaving: solvent fluctuations dominate protein dynamics and functions. Proc Natl Acad Sci U S A. 2002;99(25):16047-16051. 12444262 10.1073/pnas.212637899 138562
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.25 , pp. 16047-16051
    • Fenimore, P.W.1    Frauenfelder, H.2    McMahon, B.H.3
  • 28
    • 33745032291 scopus 로고    scopus 로고
    • Water mediation in protein folding and molecular recognition
    • 16689642
    • Levy Y Onuchic JN: Water mediation in protein folding and molecular recognition. Annu Rev Biophys Biomol Struct. 2006;35:389-415. 16689642 10.1146/annurev.biophys.35.040405.102134
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 389-415
    • Levy, Y.1    Onuchic, J.N.2
  • 29
    • 84871188659 scopus 로고    scopus 로고
    • Is Water the Universal Solvent for Life?
    • 23065397
    • Pohorille A Pratt LR: Is Water the Universal Solvent for Life? Orig Life Evol Biosph. 2012;42(5):405-409. 23065397 10.1007/s11084-012-9301-6
    • (2012) Orig Life Evol Biosph , vol.42 , Issue.5 , pp. 405-409
    • Pohorille, A.1    Pratt, L.R.2
  • 30
    • 4344669431 scopus 로고    scopus 로고
    • Protein structure, stability and solubility in water and other solvents
    • 15306378, 1693406
    • Pace CN Trevino S Prabhakaran E: Protein structure, stability and solubility in water and other solvents. Philos Trans R Soc Lond B Biol Sci. 2004;359(1448):1225-1234. 15306378 10.1098/rstb.2004.1500 1693406
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , Issue.1448 , pp. 1225-1234
    • Pace, C.N.1    Trevino, S.2    Prabhakaran, E.3
  • 31
    • 79961226780 scopus 로고    scopus 로고
    • An introduction to membrane proteins
    • 21815691
    • Hedin LE Illergård K Elofsson A: An introduction to membrane proteins. J Proteome Res. 2011;10(8):3324-31. 21815691 10.1021/pr200145a
    • (2011) J Proteome Res , vol.10 , Issue.8 , pp. 3324-3331
    • Hedin, L.E.1    Illergård, K.2    Elofsson, A.3
  • 32
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • 1547331, 1260259
    • Wiener MC White SH: Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys J. 1992;61(2):434-447. 1547331 10.1016/S0006-3495(92)81849-0 1260259
    • (1992) Biophys J , vol.61 , Issue.2 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 33
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • 9568909, 2143985
    • Wallin E von Heijne G: Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998;7(4):1029-1038. 9568909 10.1002/pro.5560070420 2143985
    • (1998) Protein Sci , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 34
    • 84864679413 scopus 로고    scopus 로고
    • Solution NMR studies of peptide-lipid interactions in model membranes
    • 22583052
    • Mäler L: Solution NMR studies of peptide-lipid interactions in model membranes. Mol Membr Biol. 2012;29(5):155-76. 22583052 10.3109/09687688.2012.683456
    • (2012) Mol Membr Biol , vol.29 , Issue.5 , pp. 155-176
    • Mäler, L.1
  • 35
    • 34249739711 scopus 로고    scopus 로고
    • The membrane protein universe: What's out there and why bother?
    • 17547710
    • Von Heijne G: The membrane protein universe: What's out there and why bother? J Intern Med. 2007;261(6):543-557. 17547710 10.1111/j.1365-2796.2007.01792.x
    • (2007) J Intern Med , vol.261 , Issue.6 , pp. 543-557
    • Von Heijne, G.1
  • 36
    • 0027080146 scopus 로고
    • Forces involved in the assembly and stabilization of membrane proteins
    • 1464373
    • Cramer WA Engelman DM Von Heijne G: Forces involved in the assembly and stabilization of membrane proteins. FASEB J. 1992;6(15):3397-3402. 1464373
    • (1992) FASEB J , vol.6 , Issue.15 , pp. 3397-3402
    • Cramer, W.A.1    Engelman, D.M.2    Von Heijne, G.3
  • 37
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • 7919780
    • Von Heijne G: Membrane proteins: From sequence to structure. Annu Rev Biophys Biomol Struct. 1994;23:167-192. 7919780 10.1146/annurev.bb.23.060194.001123
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 38
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • 10410805
    • White SH Wimley WC: Membrane protein folding and stability: Physical principles. Annu Rev Biophys Biomol Struct. 1999;28:319-365. 10410805 10.1146/annurev.biophys.28.1.319
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 39
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
    • 21606332, 3121867
    • Moon CP Fleming KG: Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers. Proc Natl Acad Sci U S A. 2011;108(25):10174-10177. 21606332 10.1073/pnas.1103979108 3121867
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.25 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 40
    • 84872775991 scopus 로고    scopus 로고
    • Structural biology. Membrane protein twists and turns
    • 23349275
    • Bowie JU: Structural biology. Membrane protein twists and turns. Science. 2013;339(6118):398-9. 23349275 10.1126/science.1228655
    • (2013) Science , vol.339 , Issue.6118 , pp. 398-399
    • Bowie, J.U.1
  • 41
    • 82355173188 scopus 로고    scopus 로고
    • Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions
    • 21930386
    • MacCallum JL Tieleman DP: Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions. Trends Biochem Sci. 2011;36(12):653-662. 21930386 10.1016/j.tibs.2011.08.003
    • (2011) Trends Biochem Sci , vol.36 , Issue.12 , pp. 653-662
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 42
    • 84869595622 scopus 로고    scopus 로고
    • Assembly and stability of α-helical membrane proteins
    • 23166562, 3500387
    • Heyden M Freites JA Ulmschneider MB: Assembly and stability of α-helical membrane proteins. Soft Matter. 2012;8(30):7742-7752. 23166562 10.1039/C2SM25402F 3500387
    • (2012) Soft Matter , vol.8 , Issue.30 , pp. 7742-7752
    • Heyden, M.1    Freites, J.A.2    Ulmschneider, M.B.3
  • 43
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • 16167052
    • Ross CA Poirier MA: Opinion: What is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol. 2005;6(11):891-8. 16167052 10.1038/nrm1742
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.11 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 44
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • 15272267
    • Ross CA Poirier MA: Protein aggregation and neurodegenerative disease. Nat Med. 2004;10:S10-7. 15272267 10.1038/nm1066
    • (2004) Nat Med , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 45
    • 68649110959 scopus 로고    scopus 로고
    • Bridging the gap: from protein misfolding to protein misfolding diseases
    • 19545568
    • Luheshi LM Dobson CM: Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett. 2009;583(16):2581-2586. 19545568 10.1016/j.febslet.2009.06.030
    • (2009) FEBS Lett , vol.583 , Issue.16 , pp. 2581-2586
    • Luheshi, L.M.1    Dobson, C.M.2
  • 46
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • 16756495
    • Chiti F Dobson CM: Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006;75:333-366. 16756495 10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 47
    • 84863479475 scopus 로고    scopus 로고
    • Protein aggregation: Mechanisms and functional consequences
    • 22713792
    • Invernizzi G Papaleo E Sabate R: Protein aggregation: Mechanisms and functional consequences. Int J Biochem Cell Biol. 2012;44(9):1541-1554. 22713792 10.1016/j.biocel.2012.05.023
    • (2012) Int J Biochem Cell Biol , vol.44 , Issue.9 , pp. 1541-1554
    • Invernizzi, G.1    Papaleo, E.2    Sabate, R.3
  • 48
    • 84863117217 scopus 로고    scopus 로고
    • Protein aggregation in neurodegenerative diseases: Insights from computational analyses
    • Sarkar A Kumar S Grover A: Protein aggregation in neurodegenerative diseases: Insights from computational analyses. Curr Bioinformatics. 2012;7(1):87-95. 10.2174/157489312799304495
    • (2012) Curr Bioinformatics , vol.7 , Issue.1 , pp. 87-95
    • Sarkar, A.1    Kumar, S.2    Grover, A.3
  • 49
    • 84857033477 scopus 로고    scopus 로고
    • The two faces of Janus: Functional interactions and protein aggregation
    • 22155180
    • Pastore A Temussi PA: The two faces of Janus: Functional interactions and protein aggregation. Curr Opin Struct Biol. 2012;22(1):30-37. 22155180 10.1016/j.sbi.2011.11.007
    • (2012) Curr Opin Struct Biol , vol.22 , Issue.1 , pp. 30-37
    • Pastore, A.1    Temussi, P.A.2
  • 50
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • 17051203
    • Lansbury PT Lashuel HA: A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature. 2006;443(7113):774-779. 17051203 10.1038/nature05290
    • (2006) Nature , vol.443 , Issue.7113 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 51
    • 48349090111 scopus 로고    scopus 로고
    • Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival
    • 18666828, 2486295
    • Wang Q Johnson JL Agar N: Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival. PLoS Biol. 2008;6(7):e170. 18666828 10.1371/journal.pbio.0060170 2486295
    • (2008) PLoS Biol , vol.6 , Issue.7 , pp. e170
    • Wang, Q.1    Johnson, J.L.2    Agar, N.3
  • 52
    • 63449129653 scopus 로고    scopus 로고
    • Molecular pathology of lewy body diseases
    • 19399218, 2671999
    • Beyer K Domingo-Sàbat M Ariza A: Molecular pathology of lewy body diseases. Int J Mol Sci. 2009;10(3):724-745. 19399218 10.3390/ijms10030724 2671999
    • (2009) Int J Mol Sci , vol.10 , Issue.3 , pp. 724-745
    • Beyer, K.1    Domingo-Sàbat, M.2    Ariza, A.3
  • 53
    • 69949084211 scopus 로고    scopus 로고
    • Protein aggregation as a paradigm of aging
    • 19527771
    • Lindner AB Demarez A: Protein aggregation as a paradigm of aging. Biochim Biophys Acta. 2009;1790(10):980-996. 19527771 10.1016/j.bbagen.2009.06.005
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.10 , pp. 980-996
    • Lindner, A.B.1    Demarez, A.2
  • 54
    • 79960046164 scopus 로고    scopus 로고
    • Cellular stress response pathways and ageing: Intricate molecular relationships
    • 21587205, 3155297
    • Kourtis N Tavernarakis N: Cellular stress response pathways and ageing: Intricate molecular relationships. EMBO J. 2011;30(13):2520-2531. 21587205 10.1038/emboj.2011.162 3155297
    • (2011) EMBO J , vol.30 , Issue.13 , pp. 2520-2531
    • Kourtis, N.1    Tavernarakis, N.2
  • 55
    • 47749105267 scopus 로고    scopus 로고
    • Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy
    • 18541737, 2601596
    • Tannous P Zhu H Nemchenko A: Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy. Circulation. 2008;117(24):3070-3078. 18541737 10.1161/CIRCULATIONAHA.107.763870 2601596
    • (2008) Circulation , vol.117 , Issue.24 , pp. 3070-3078
    • Tannous, P.1    Zhu, H.2    Nemchenko, A.3
  • 56
    • 78049281798 scopus 로고    scopus 로고
    • Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth
    • 20724178, 2967602
    • Liu M Hodish I Haataja L: Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth. Trends Endocrinol Metab. 2010;21(11):652-659. 20724178 10.1016/j.tem.2010.07.001 2967602
    • (2010) Trends Endocrinol Metab , vol.21 , Issue.11 , pp. 652-659
    • Liu, M.1    Hodish, I.2    Haataja, L.3
  • 57
    • 84861357149 scopus 로고    scopus 로고
    • Protein aggregation and misfolding: Good or evil?
    • 22595337
    • Pastore A Temussi P: Protein aggregation and misfolding: Good or evil? J Phys Condens Matter. 2012;24(24):244101. 22595337 10.1088/0953-8984/24/24/244101
    • (2012) J Phys Condens Matter , vol.24 , Issue.24 , pp. 244101
    • Pastore, A.1    Temussi, P.2
  • 58
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • 10783891
    • Schubert U Anton LC Gibbs J: Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 2000;404(6779):770-774. 10783891 10.1038/35008096
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3
  • 59
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • 17928587
    • Hebert DN Molinari M: In and out of the ER: Protein folding, quality control, degradation, and related human diseases. Physiol Rev. 2007;87(4):1377-1408. 17928587 10.1152/physrev.00050.2006
    • (2007) Physiol Rev , vol.87 , Issue.4 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 60
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • 17051204
    • Rubinsztein DC: The roles of intracellular protein-degradation pathways in neurodegeneration. Nature. 2006;443(7113):780-786. 17051204 10.1038/nature05291
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 61
    • 79957947433 scopus 로고    scopus 로고
    • Removing protein aggregates: The role of proteolysis in neurodegeneration
    • 21568912
    • Nijholt DA De Kimpe L Elfrink HL: Removing protein aggregates: The role of proteolysis in neurodegeneration. Curr Med Chem. 2011;18(16):2459-2476. 21568912 10.2174/092986711795843236
    • (2011) Curr Med Chem , vol.18 , Issue.16 , pp. 2459-2476
    • Nijholt, D.A.1    De Kimpe, L.2    Elfrink, H.L.3
  • 62
    • 84857648264 scopus 로고    scopus 로고
    • Mechanisms for quality control of misfolded transmembrane proteins
    • 22100602, 3288195
    • Houck SA Cyr DM: Mechanisms for quality control of misfolded transmembrane proteins. Biochim Biophys Acta. 2012;1818(4):1108-1114. 22100602 10.1016/j.bbamem.2011.11.007 3288195
    • (2012) Biochim Biophys Acta , vol.1818 , Issue.4 , pp. 1108-1114
    • Houck, S.A.1    Cyr, D.M.2
  • 63
    • 59649114573 scopus 로고    scopus 로고
    • Autophagic Clearance of Aggregate-Prone Proteins Associated with Neurodegeneration
    • 19216903
    • Sarkar S Ravikumar B Rubinsztein DC: Autophagic Clearance of Aggregate-Prone Proteins Associated with Neurodegeneration. Methods Enzymol. 2009;453:83-110. 19216903 10.1016/S0076-6879(08)04005-6
    • (2009) Methods Enzymol , vol.453 , pp. 83-110
    • Sarkar, S.1    Ravikumar, B.2    Rubinsztein, D.C.3
  • 64
    • 39049148153 scopus 로고    scopus 로고
    • Aggresome formation and neurodegenerative diseases: Therapeutic implications
    • 18220762
    • Olzmann JA Li L Chin LS: Aggresome formation and neurodegenerative diseases: Therapeutic implications. Curr Med Chem. 2008;15(1):47-60. 18220762 10.2174/092986708783330692
    • (2008) Curr Med Chem , vol.15 , Issue.1 , pp. 47-60
    • Olzmann, J.A.1    Li, L.2    Chin, L.S.3
  • 65
    • 59649096550 scopus 로고    scopus 로고
    • Abnormal proteins can form aggresome in yeast: Aggresome-targeting signals and components of the machinery
    • 18854435, 2630789
    • Wang Y Meriin AB Zaarur N: Abnormal proteins can form aggresome in yeast: Aggresome-targeting signals and components of the machinery. FASEB J. 2009;23(2):451-463. 18854435 10.1096/fj.08-117614 2630789
    • (2009) FASEB J , vol.23 , Issue.2 , pp. 451-463
    • Wang, Y.1    Meriin, A.B.2    Zaarur, N.3
  • 66
    • 0033739529 scopus 로고    scopus 로고
    • Structural proteomics: prospects for high throughput sample preparation
    • 11063779, xxxx
    • Christendat D Yee A Dharamsi A: Structural proteomics: prospects for high throughput sample preparation. Prog Biophys Mol Biol. 2000;73(5):339-345. 11063779 10.1016/S0079-6107(00)00010-9 xxxx
    • (2000) Prog Biophys Mol Biol , vol.73 , Issue.5 , pp. 339-345
    • Christendat, D.1    Yee, A.2    Dharamsi, A.3
  • 67
    • 77951902249 scopus 로고    scopus 로고
    • Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis
    • 20377183
    • Shi J Lua S Tong JS: Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. Biochemistry. 2010;49(18):3887-3897. 20377183 10.1021/bi902057a
    • (2010) Biochemistry , vol.49 , Issue.18 , pp. 3887-3897
    • Shi, J.1    Lua, S.2    Tong, J.S.3
  • 68
    • 33845370672 scopus 로고    scopus 로고
    • Resurrecting abandoned proteins with pure water: CD and NMR studies of protein fragments solubilized in salt-free water
    • 16980357, 1635667
    • Li M Liu J Ran X: Resurrecting abandoned proteins with pure water: CD and NMR studies of protein fragments solubilized in salt-free water. Biophys J. 2006;91(11):4201-4209. 16980357 10.1529/biophysj.106.093187 1635667
    • (2006) Biophys J , vol.91 , Issue.11 , pp. 4201-4209
    • Li, M.1    Liu, J.2    Ran, X.3
  • 69
    • 33746528014 scopus 로고    scopus 로고
    • Nogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration
    • 16877707, 2242580
    • Li M Liu J Song J: Nogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration. Protein Sci. 2006;15(8):1835-41. 16877707 10.1110/ps.062306906 2242580
    • (2006) Protein Sci , vol.15 , Issue.8 , pp. 1835-1841
    • Li, M.1    Liu, J.2    Song, J.3
  • 70
    • 64349115533 scopus 로고    scopus 로고
    • The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form
    • 19236004, 2748245
    • Delak K Harcup C Lakshminarayanan R: The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. Biochemistry. 2009;48(10):2272-2281. 19236004 10.1021/bi802175a 2748245
    • (2009) Biochemistry , vol.48 , Issue.10 , pp. 2272-2281
    • Delak, K.1    Harcup, C.2    Lakshminarayanan, R.3
  • 71
    • 64349106349 scopus 로고    scopus 로고
    • AP7, a partially disordered pseudo C-RING protein, is capable of forming stabilized aragonite in vitro
    • 19159266
    • Amos FF Evans JS: AP7, a partially disordered pseudo C-RING protein, is capable of forming stabilized aragonite in vitro. Biochemistry. 2009;48(6):1332-1339. 19159266 10.1021/bi802148r
    • (2009) Biochemistry , vol.48 , Issue.6 , pp. 1332-1339
    • Amos, F.F.1    Evans, J.S.2
  • 72
    • 65449165696 scopus 로고    scopus 로고
    • Polyelectrolyte domains and intrinsic disorder within the prismatic asprich protein family
    • 19344178
    • Delak K Collino S Evans JS: Polyelectrolyte domains and intrinsic disorder within the prismatic asprich protein family. Biochemistry. 2009;48(16):3669-3677. 19344178 10.1021/bi900113v
    • (2009) Biochemistry , vol.48 , Issue.16 , pp. 3669-3677
    • Delak, K.1    Collino, S.2    Evans, J.S.3
  • 73
    • 77749322192 scopus 로고    scopus 로고
    • The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a "fuzzy" complex upon DNA binding
    • 20102160
    • Aguado-Llera D Goormaghtigh E De Geest N: The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a "fuzzy" complex upon DNA binding. Biochemistry. 2010;49(8):1577-1589. 20102160 10.1021/bi901616z
    • (2010) Biochemistry , vol.49 , Issue.8 , pp. 1577-1589
    • Aguado-Llera, D.1    Goormaghtigh, E.2    De Geest, N.3
  • 74
    • 77954638580 scopus 로고    scopus 로고
    • beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles
    • 20301214
    • Nielsen SB Franzmann M Basaiawmoit RV: beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles. Biopolymers. 2010;93(8):678-689. 20301214 10.1002/bip.21434
    • (2010) Biopolymers , vol.93 , Issue.8 , pp. 678-689
    • Nielsen, S.B.1    Franzmann, M.2    Basaiawmoit, R.V.3
  • 75
    • 80054753936 scopus 로고    scopus 로고
    • A C-RING-like domain participates in protein self-assembly and mineral nucleation
    • 21928802
    • Amos FF Ndao M Ponce CB: A C-RING-like domain participates in protein self-assembly and mineral nucleation. Biochemistry. 2011;50(41):8880-8887. 21928802 10.1021/bi201346d
    • (2011) Biochemistry , vol.50 , Issue.41 , pp. 8880-8887
    • Amos, F.F.1    Ndao, M.2    Ponce, C.B.3
  • 76
    • 79953172914 scopus 로고    scopus 로고
    • Probing the self-association, intermolecular contacts, and folding propensity of amelogenin
    • 21351181, 3081550
    • Ndao M Dutta K Bromley KM: Probing the self-association, intermolecular contacts, and folding propensity of amelogenin. Protein Sci. 2011;20(4):724-734. 21351181 10.1002/pro.603 3081550
    • (2011) Protein Sci , vol.20 , Issue.4 , pp. 724-734
    • Ndao, M.1    Dutta, K.2    Bromley, K.M.3
  • 77
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • 18054235
    • Tompa P Fuxreiter M: Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci. 2008;33(1):2-8. 18054235 10.1016/j.tibs.2007.10.003
    • (2008) Trends Biochem Sci , vol.33 , Issue.1 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 78
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • 21927770
    • Fuxreiter M: Fuzziness: linking regulation to protein dynamics. Mol Biosyst. 2012;8(1):168-177. 21927770 10.1039/c1mb05234a
    • (2012) Mol Biosyst , vol.8 , Issue.1 , pp. 168-177
    • Fuxreiter, M.1
  • 79
    • 84862227635 scopus 로고    scopus 로고
    • Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations
    • 22720086, 3374797
    • Gupta G Qin H Song J: Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations. PLoS One. 2012;7(6):e39261. 22720086 10.1371/journal.pone.0039261 3374797
    • (2012) PLoS One , vol.7 , Issue.6 , pp. e39261
    • Gupta, G.1    Qin, H.2    Song, J.3
  • 80
    • 84864012621 scopus 로고    scopus 로고
    • VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B
    • 22815741, 3398895
    • Goyal S Gupta G Qin H: VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B. PLoS One. 2012;7(7):e40341. 22815741 10.1371/journal.pone.0040341 3398895
    • (2012) PLoS One , vol.7 , Issue.7 , pp. e40341
    • Goyal, S.1    Gupta, G.2    Qin, H.3
  • 81
    • 84865146912 scopus 로고    scopus 로고
    • Intrinsically Disordered Proteins in Biomineralization
    • Advanced Topics in Biomineralization, Dr. Jong Seto (Ed.)
    • Wojtas M Dobryszycki P Ozyhar A: Intrinsically Disordered Proteins in Biomineralization.Advanced Topics in Biomineralization, Dr. Jong Seto (Ed.),2012. 10.5772/31121
    • (2012)
    • Wojtas, M.1    Dobryszycki, P.2    Ozyhar, A.3
  • 82
    • 84864762380 scopus 로고    scopus 로고
    • Structural disorder in proteins brings order to crystal growth in biomineralization
    • 22634174
    • Kalmar L Homola D Varga G: Structural disorder in proteins brings order to crystal growth in biomineralization. Bone. 2012;51(3):528-534. 22634174 10.1016/j.bone.2012.05.009
    • (2012) Bone , vol.51 , Issue.3 , pp. 528-534
    • Kalmar, L.1    Homola, D.2    Varga, G.3
  • 83
    • 77950618150 scopus 로고    scopus 로고
    • Molecular simulations of protein disorder
    • 20453929
    • Rauscher S Pomès R: Molecular simulations of protein disorder. Biochem Cell Biol. 2010;88(2):269-90. 20453929 10.1139/o09-169
    • (2010) Biochem Cell Biol , vol.88 , Issue.2 , pp. 269-290
    • Rauscher, S.1    Pomès, R.2
  • 84
    • 84873704015 scopus 로고    scopus 로고
    • ALS-causing P56S Mutation and Splicing Variation on the hVAPB MSP Domain Transform its β-sandwich Fold into Lipid-interacting Helical Conformations
    • 23333387
    • Qin H Wang W Song J: ALS-causing P56S Mutation and Splicing Variation on the hVAPB MSP Domain Transform its β-sandwich Fold into Lipid-interacting Helical Conformations. Biochem Biophys Res Commun. 2013;431(3):398-403. 23333387 10.1016/j.bbrc.2013.01.039
    • (2013) Biochem Biophys Res Commun , vol.431 , Issue.3 , pp. 398-403
    • Qin, H.1    Wang, W.2    Song, J.3
  • 85
    • 77950516260 scopus 로고    scopus 로고
    • Novel splice variants of the amyotrophic lateral sclerosis-associated gene VAPB expressed in human tissues
    • 20227395
    • Nachreiner T Esser M Tenten V: Novel splice variants of the amyotrophic lateral sclerosis-associated gene VAPB expressed in human tissues. Biochem Biophys Res Commun. 2010;394(3):703-708. 20227395 10.1016/j.bbrc.2010.03.055
    • (2010) Biochem Biophys Res Commun , vol.394 , Issue.3 , pp. 703-708
    • Nachreiner, T.1    Esser, M.2    Tenten, V.3
  • 87
    • 0027692037 scopus 로고
    • Complexity of protein folding
    • 8281132
    • Fraenkel AS: Complexity of protein folding. Bull Math Biol. 1993;55(6):1199-1210. 8281132 10.1007/BF02460704
    • (1993) Bull Math Biol , vol.55 , Issue.6 , pp. 1199-1210
    • Fraenkel, A.S.1
  • 88
    • 38749151911 scopus 로고    scopus 로고
    • Structural basis for the function and inhibition of an influenza virus proton channel
    • 18235504
    • Stouffer AL Acharya R Salom D: Structural basis for the function and inhibition of an influenza virus proton channel. Nature. 2008;451(7178):596-599. 18235504 10.1038/nature06528
    • (2008) Nature , vol.451 , Issue.7178 , pp. 596-599
    • Stouffer, A.L.1    Acharya, R.2    Salom, D.3
  • 89
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • 18235503, 3108054
    • Schnell JR Chou JJ: Structure and mechanism of the M2 proton channel of influenza A virus. Nature. 2008;451(7178):591-595. 18235503 10.1038/nature06531 3108054
    • (2008) Nature , vol.451 , Issue.7178 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 90
    • 58149345493 scopus 로고    scopus 로고
    • Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantadine binding
    • 19061899
    • Cady SD Mishanina TV Hong M: Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantadine binding. J Mol Biol. 2009;385(4):1127-41. 19061899 10.1016/j.jmb.2008.11.022
    • (2009) J Mol Biol , vol.385 , Issue.4 , pp. 1127-1141
    • Cady, S.D.1    Mishanina, T.V.2    Hong, M.3
  • 91
    • 84914815858 scopus 로고    scopus 로고
    • Solubilization of M2 Transmembrane Peptide of Influenza A in Pure Water: Implications for Emergence of Proteins and Protein-embedded Primeval Membranes in Unsalted Oceans
    • Reference Source
    • Song J Miao L: Solubilization of M2 Transmembrane Peptide of Influenza A in Pure Water: Implications for Emergence of Proteins and Protein-embedded Primeval Membranes in Unsalted Oceans. Nature Precedings. 2012. Reference Source
    • (2012) Nature Precedings
    • Song, J.1    Miao, L.2
  • 92
    • 0002801327 scopus 로고
    • Existence and nature of dark matter in the universe
    • Trimble V: Existence and nature of dark matter in the universe. Annu Rev Astron Astrophys. 1987;25:425-472. 10.1146/annurev.aa.25.090187.002233
    • (1987) Annu Rev Astron Astrophys , vol.25 , pp. 425-472
    • Trimble, V.1
  • 93
    • 71049135717 scopus 로고    scopus 로고
    • Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water
    • 19956763, 2776303
    • Liu J Song J: Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water. PLoS One. 2009;4(11):e7805. 19956763 10.1371/journal.pone.0007805 2776303
    • (2009) PLoS One , vol.4 , Issue.11 , pp. e7805
    • Liu, J.1    Song, J.2
  • 94
    • 33745016248 scopus 로고    scopus 로고
    • Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins
    • 16752908
    • Liu J Li M Ran X: Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins. Biochemistry. 2006;45(23):7171-84. 16752908 10.1021/bi060091y
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7171-7184
    • Liu, J.1    Li, M.2    Ran, X.3
  • 95
    • 58149168271 scopus 로고    scopus 로고
    • NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain
    • 18599634, 2576364
    • Liu J Song J: NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain. Biophys J. 2008;95(10):4803-12. 18599634 10.1529/biophysj.107.125641 2576364
    • (2008) Biophys J , vol.95 , Issue.10 , pp. 4803-4812
    • Liu, J.1    Song, J.2
  • 96
    • 80053273216 scopus 로고    scopus 로고
    • Selective and specific ion binding on proteins at physiologically-relevant concentrations
    • 21907714
    • Miao L Qin H Koehl P: Selective and specific ion binding on proteins at physiologically-relevant concentrations. FEBS Lett. 2011;585(19):3126-32. 21907714 10.1016/j.febslet.2011.08.048
    • (2011) FEBS Lett , vol.585 , Issue.19 , pp. 3126-3132
    • Miao, L.1    Qin, H.2    Koehl, P.3
  • 97
    • 0036712112 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin B2, a cell-surface ligand with bidirectional signaling properties
    • 12206665
    • Song J Vranken W Xu P: Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin B2, a cell-surface ligand with bidirectional signaling properties. Biochemistry. 2002;41(36):10942-9. 12206665 10.1021/bi025815u
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 10942-10949
    • Song, J.1    Vranken, W.2    Xu, P.3
  • 98
    • 0042591409 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties
    • 12606549
    • Song J: Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties. J Biol Chem. 2003;278(27):24714-20. 12606549 10.1074/jbc.M210625200
    • (2003) J Biol Chem , vol.278 , Issue.27 , pp. 24714-24720
    • Song, J.1
  • 99
    • 84914811312 scopus 로고    scopus 로고
    • "Dark Mediators" of Proteins as Revealed by NMR in Water: Residue-selective Anion Bindings that are Masked by Pre-existing Buffer
    • Reference Source
    • Miao L Qin H Song J: "Dark Mediators" of Proteins as Revealed by NMR in Water: Residue-selective Anion Bindings that are Masked by Pre-existing Buffer. Nature Precedings. 2012. Reference Source
    • (2012) Nature Precedings
    • Miao, L.1    Qin, H.2    Song, J.3
  • 100
    • 58149166734 scopus 로고    scopus 로고
    • Identification and structural mechanism for a novel interaction between a ubiquitin ligase WWP1 and Nogo-A, a key inhibitor for central nervous system regeneration
    • 19035836
    • Qin H Pu HX Li M: Identification and structural mechanism for a novel interaction between a ubiquitin ligase WWP1 and Nogo-A, a key inhibitor for central nervous system regeneration. Biochemistry. 2008;47(51):13647-58. 19035836 10.1021/bi8017976
    • (2008) Biochemistry , vol.47 , Issue.51 , pp. 13647-13658
    • Qin, H.1    Pu, H.X.2    Li, M.3
  • 101
    • 33846387917 scopus 로고    scopus 로고
    • Influence of the Hofmeister anions on protein stability as studied by thermal denaturation and chemical shift perturbation
    • 17223714
    • Tadeo X Pons M Millet O: Influence of the Hofmeister anions on protein stability as studied by thermal denaturation and chemical shift perturbation. Biochemistry. 2007;46(3):917-923. 17223714 10.1021/bi0613426
    • (2007) Biochemistry , vol.46 , Issue.3 , pp. 917-923
    • Tadeo, X.1    Pons, M.2    Millet, O.3
  • 102
    • 80055113691 scopus 로고    scopus 로고
    • Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations
    • 22069488, 3206076
    • Lua S Qin H Lim L: Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations. PLoS One. 2011;6(11):e27072. 22069488 10.1371/journal.pone.0027072 3206076
    • (2011) PLoS One , vol.6 , Issue.11 , pp. e27072
    • Lua, S.1    Qin, H.2    Lim, L.3
  • 103
    • 79955698252 scopus 로고    scopus 로고
    • Protein crowding tunes protein stability
    • 21506571
    • Miklos AC Sarkar M Wang Y: Protein crowding tunes protein stability. J Am Chem Soc. 2011;133(18):7116-7120. 21506571 10.1021/ja200067p
    • (2011) J Am Chem Soc , vol.133 , Issue.18 , pp. 7116-7120
    • Miklos, A.C.1    Sarkar, M.2    Wang, Y.3
  • 104
    • 77952308995 scopus 로고    scopus 로고
    • A VAP B mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum
    • 20008544
    • Fasana E Fossati M Ruggiano A: A VAP B mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum. FASEB J. 2010;24(5):1419-1430. 20008544 10.1096/fj.09-147850
    • (2010) FASEB J , vol.24 , Issue.5 , pp. 1419-1430
    • Fasana, E.1    Fossati, M.2    Ruggiano, A.3
  • 105
    • 84869122198 scopus 로고    scopus 로고
    • Restructured endoplasmic reticulum generated by mutant amyotrophic lateral sclerosis-linked VAPB is cleared by the proteasome
    • 22611258
    • Papiani G Ruggiano A Fossati M: Restructured endoplasmic reticulum generated by mutant amyotrophic lateral sclerosis-linked VAPB is cleared by the proteasome. J Cell Sci. 2012;125(Pt 15):3601-3611. 22611258
    • (2012) J Cell Sci , vol.125 , pp. 3601-3611
    • Papiani, G.1    Ruggiano, A.2    Fossati, M.3
  • 106
    • 80052225992 scopus 로고    scopus 로고
    • Downregulation of VAPB expression in motor neurons derived from induced pluripotent stem cells of ALS8 patients
    • 21685205, 3159551
    • Mitne-Neto M Machado-Costa M Marchetto MC: Downregulation of VAPB expression in motor neurons derived from induced pluripotent stem cells of ALS8 patients. Hum Mol Genet. 2011;20(18):3642-3652. 21685205 10.1093/hmg/ddr284 3159551
    • (2011) Hum Mol Genet , vol.20 , Issue.18 , pp. 3642-3652
    • Mitne-Neto, M.1    Machado-Costa, M.2    Marchetto, M.C.3
  • 107
    • 63549086214 scopus 로고    scopus 로고
    • Co-evolution of primordial membranes and membrane proteins
    • 19303305, 2752816
    • Mulkidjanian AY Galperin MY Koonin EV: Co-evolution of primordial membranes and membrane proteins. Trends Biochem Sci. 2009;34(4):206-215. 19303305 10.1016/j.tibs.2009.01.005 2752816
    • (2009) Trends Biochem Sci , vol.34 , Issue.4 , pp. 206-215
    • Mulkidjanian, A.Y.1    Galperin, M.Y.2    Koonin, E.V.3
  • 108
    • 43049130286 scopus 로고    scopus 로고
    • The origin and evolution of the oceans
    • In Lectures in Astrobiology (Gargaud, M. et al., eds), Springer-Verlag
    • Pinti DL: The origin and evolution of the oceans.In Lectures in Astrobiology (Gargaud, M. et al., eds), Springer-Verlag.2005;pp 83-112. 10.1007/10913406_4
    • (2005) , pp. 83-112
    • Pinti, D.L.1
  • 109
    • 69849105908 scopus 로고    scopus 로고
    • Probing the "dark matter" of protein fold space
    • 19748345
    • Taylor WR Chelliah V Hollup SM: Probing the "dark matter" of protein fold space. Structure. 2009;17(9):1244-1252. 19748345 10.1016/j.str.2009.07.012
    • (2009) Structure , vol.17 , Issue.9 , pp. 1244-1252
    • Taylor, W.R.1    Chelliah, V.2    Hollup, S.M.3
  • 110
    • 27744591844 scopus 로고    scopus 로고
    • On the origin of genomes and cells within inorganic compartments
    • 16223546
    • Koonin EV Martin W: On the origin of genomes and cells within inorganic compartments. Trends Genet. 2005;21(12):647-654. 16223546 10.1016/j.tig.2005.09.006
    • (2005) Trends Genet , vol.21 , Issue.12 , pp. 647-654
    • Koonin, E.V.1    Martin, W.2
  • 111
    • 34250795054 scopus 로고    scopus 로고
    • Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain
    • 17585875
    • Li M Song J: Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. Biochem Biophys Res Commun. 2007;360(1):128-134. 17585875 10.1016/j.bbrc.2007.06.031
    • (2007) Biochem Biophys Res Commun , vol.360 , Issue.1 , pp. 128-134
    • Li, M.1    Song, J.2
  • 112
    • 47349103543 scopus 로고    scopus 로고
    • NMR structure and dynamics of human ephrin-B2 ectodomain: the functionally critical C-D and G-H loops are highly dynamic in solution
    • 18300229
    • Ran X Qin H Liu J: NMR structure and dynamics of human ephrin-B2 ectodomain: the functionally critical C-D and G-H loops are highly dynamic in solution. Proteins. 2008;72(3):1019-1029. 18300229 10.1002/prot.21999
    • (2008) Proteins , vol.72 , Issue.3 , pp. 1019-1029
    • Ran, X.1    Qin, H.2    Liu, J.3
  • 113
    • 73949157872 scopus 로고    scopus 로고
    • Structural characterization reveals that viperin is a radical S-adenosyl-L-methionine (SAM) enzyme
    • 20026307
    • Shaveta G Shi J Chow VT: Structural characterization reveals that viperin is a radical S-adenosyl-L-methionine (SAM) enzyme. Biochem Bio phys Res Commun. 2010;391(3):1390-1395. 20026307 10.1016/j.bbrc.2009.12.070
    • (2010) Biochem Bio phys Res Commun , vol.391 , Issue.3 , pp. 1390-1395
    • Shaveta, G.1    Shi, J.2    Chow, V.T.3
  • 114
    • 0036617018 scopus 로고    scopus 로고
    • Influence of ionic inorganic solutes on self-assembly and polymerization processes related to early forms of life: implications for a prebiotic aqueous medium
    • 12469365
    • Monnard PA Apel CL Kanavarioti A: Influence of ionic inorganic solutes on self-assembly and polymerization processes related to early forms of life: implications for a prebiotic aqueous medium. Astrobiology. 2002;2(2):139-52. 12469365 10.1089/15311070260192237
    • (2002) Astrobiology , vol.2 , Issue.2 , pp. 139-152
    • Monnard, P.A.1    Apel, C.L.2    Kanavarioti, A.3
  • 115
    • 84868328903 scopus 로고    scopus 로고
    • Editorial: Proteostenosis: cancer's Achilles heel?
    • 23118441, 3476236
    • Yewdell JW David A: Editorial: Proteostenosis: cancer's Achilles heel? J Leukoc Biol. 2012;92(5):913-915. 23118441 10.1189/jlb.0612272 3476236
    • (2012) J Leukoc Biol , vol.92 , Issue.5 , pp. 913-915
    • Yewdell, J.W.1    David, A.2
  • 116
    • 82455192402 scopus 로고    scopus 로고
    • DRiPs solidify: progress in understanding endogenous MHC class I antigen processing
    • 21962745, 3200450
    • Yewdell JW: DRiPs solidify: progress in understanding endogenous MHC class I antigen processing. Trends Immunol. 2011;32(xx):548-558. 21962745 10.1016/j.it.2011.08.001 3200450
    • (2011) Trends Immunol , vol.32 , Issue.20 , pp. 548-558
    • Yewdell, J.W.1
  • 117
    • 0034613080 scopus 로고    scopus 로고
    • Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase
    • 11024463
    • Arechaga I Miroux B Karrasch S: Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase. FEBS Lett. 2000;482(3):215-9. 11024463 10.1016/S0014-5793(00)02054-8
    • (2000) FEBS Lett , vol.482 , Issue.3 , pp. 215-219
    • Arechaga, I.1    Miroux, B.2    Karrasch, S.3
  • 118
    • 77954218288 scopus 로고    scopus 로고
    • Further assembly required: construction and dynamics of the endoplasmic reticulum network
    • 20559323, 2897125
    • Park SH Blackstone C: Further assembly required: construction and dynamics of the endoplasmic reticulum network. EMBO Rep. 2010;11(7):515-521. 20559323 10.1038/embor.2010.92 2897125
    • (2010) EMBO Rep , vol.11 , Issue.7 , pp. 515-521
    • Park, S.H.1    Blackstone, C.2
  • 119
    • 77957020240 scopus 로고    scopus 로고
    • Emerging themes of ER organization in the development and maintenance of axons
    • 20678923, 2946456
    • Renvoisé B Blackstone C: Emerging themes of ER organization in the development and maintenance of axons. Curr Opin Neurobiol. 2010;20(5):531-537. 20678923 10.1016/j.conb.2010.07.001 2946456
    • (2010) Curr Opin Neurobiol , vol.20 , Issue.5 , pp. 531-537
    • Renvoisé, B.1    Blackstone, C.2
  • 120
    • 33745238126 scopus 로고    scopus 로고
    • Cubic membranes: a legend beyond the Flatland* of cell membrane organization
    • 16785319, 2063909
    • Almsherqi ZA Kohlwein SD Deng Y: Cubic membranes: a legend beyond the Flatland* of cell membrane organization. J Cell Biol. 2006;173(6):839-844. 16785319 10.1083/jcb.200603055 2063909
    • (2006) J Cell Biol , vol.173 , Issue.6 , pp. 839-844
    • Almsherqi, Z.A.1    Kohlwein, S.D.2    Deng, Y.3
  • 121
    • 33745752369 scopus 로고    scopus 로고
    • Endoplasmic reticulum architecture: structures in flux
    • 16806883
    • Borgese N Francolini M Snapp E: Endoplasmic reticulum architecture: structures in flux. Curr Opin Cell Biol. 2006;18(4):358-364. 16806883 10.1016/j.ceb.2006.06.008
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.4 , pp. 358-364
    • Borgese, N.1    Francolini, M.2    Snapp, E.3
  • 122
    • 79956144642 scopus 로고    scopus 로고
    • A postreductionist framework for protein biochemistry
    • 21587250
    • Laue T Demeler B: A postreductionist framework for protein biochemistry. Nat Chem Biol. 2011;7(6):331-334. 21587250 10.1038/nchembio.575
    • (2011) Nat Chem Biol , vol.7 , Issue.6 , pp. 331-334
    • Laue, T.1    Demeler, B.2
  • 123
    • 0032908135 scopus 로고    scopus 로고
    • 1H-NMR characterization of acid-induced unfolding of CHABII
    • 10048923
    • Song J Jamin N Gilquin B: A gradual disruption of tight side-chain packing: 2D 1H-NMR characterization of acid-induced unfolding of CHABII. Nat Struct Biol. 1999;6(2):129-134. 10048923 10.1038/5815
    • (1999) Nat Struct Biol , vol.6 , Issue.2 , pp. 129-134
    • Song, J.1    Jamin, N.2    Gilquin, B.3
  • 124
    • 16244403367 scopus 로고    scopus 로고
    • Molecular mechanism underlying the thermal stability and pH-induced unfolding of CHABII
    • 15808864
    • Wei Z Song J: Molecular mechanism underlying the thermal stability and pH-induced unfolding of CHABII. J Mol Biol. 2005;348(1):205-218. 15808864 10.1016/j.jmb.2005.02.028
    • (2005) J Mol Biol , vol.348 , Issue.1 , pp. 205-218
    • Wei, Z.1    Song, J.2
  • 125
    • 79952463416 scopus 로고    scopus 로고
    • Dynamical driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain
    • 21390281, 3044768
    • Shi J Han N Lim L: Dynamical driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain. PLoS Comput Biol. 2011;7(2):e1001084. 21390281 10.1371/journal.pcbi.1001084 3044768
    • (2011) PLoS Comput Biol , vol.7 , Issue.2 , pp. e1001084
    • Shi, J.1    Han, N.2    Lim, L.3
  • 126
    • 84875163039 scopus 로고    scopus 로고
    • Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering
    • 23524290
    • Matsumuraa Y Shinjoa M Matsuib T: Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering. Biophys Chem. 2013;175-176:39-46 23524290 10.1016/j.bpc.2013.02.005
    • (2013) Biophys Chem , vol.175-176 , pp. 39-46
    • Matsumuraa, Y.1    Shinjoa, M.2    Matsuib, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.