메뉴 건너뛰기




Volumn 30, Issue 12, 2014, Pages 3507-3512

Surface-mediated protein disaggregation

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; HYDROPHOBICITY; SURFACE CHEMISTRY;

EID: 84897496792     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la5000155     Document Type: Article
Times cited : (7)

References (25)
  • 2
    • 84985225141 scopus 로고
    • Collagen-enzyme complex membranes and their performance in biocatalytic modules
    • Wang, S. S.; Vieth, W. R. Collagen-enzyme complex membranes and their performance in biocatalytic modules Biotechnol. Bioeng. 1973, 15, 93-115
    • (1973) Biotechnol. Bioeng. , vol.15 , pp. 93-115
    • Wang, S.S.1    Vieth, W.R.2
  • 3
    • 84872334138 scopus 로고    scopus 로고
    • Nanobiotechnology as a novel paradigm for enzyme immobilisation and stabilisation with potential applications in biodiesel production
    • Verma, M. L.; Barrow, C. J.; Puri, M. Nanobiotechnology as a novel paradigm for enzyme immobilisation and stabilisation with potential applications in biodiesel production Appl. Microbiol. Biotechnol. 2013, 97, 23-39
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 23-39
    • Verma, M.L.1    Barrow, C.J.2    Puri, M.3
  • 4
    • 79961235658 scopus 로고    scopus 로고
    • Perspective of recent progress in immobilization of enzymes
    • Tran, D. N.; Balkus, K. J. Perspective of recent progress in immobilization of enzymes ACS Catal. 2011, 1 956-968
    • (2011) ACS Catal. , vol.1 , pp. 956-968
    • Tran, D.N.1    Balkus, K.J.2
  • 5
    • 33645891453 scopus 로고    scopus 로고
    • Challenges in biocatalysis for enzyme-based biofuel cells
    • Kim, J.; Jia, H. F.; Wang, P. Challenges in biocatalysis for enzyme-based biofuel cells Biotechnol. Adv. 2006, 24, 296-308
    • (2006) Biotechnol. Adv. , vol.24 , pp. 296-308
    • Kim, J.1    Jia, H.F.2    Wang, P.3
  • 6
    • 33745748175 scopus 로고    scopus 로고
    • Increasing protein stability through control of the nanoscale environment
    • Asuri, P.; Karajanagi, S. S.; Yang, H. C.; Yim, T. J.; Kane, R. S.; Dordick, J. S. Increasing protein stability through control of the nanoscale environment Langmuir 2006, 22, 5833-5836
    • (2006) Langmuir , vol.22 , pp. 5833-5836
    • Asuri, P.1    Karajanagi, S.S.2    Yang, H.C.3    Yim, T.J.4    Kane, R.S.5    Dordick, J.S.6
  • 8
    • 49049098668 scopus 로고    scopus 로고
    • Thermodynamic and kinetic origins of Alzheimer's and related diseases: A chemical engineer's perspective
    • Hall, C. K. Thermodynamic and kinetic origins of Alzheimer's and related diseases: a chemical engineer's perspective AIChE J. 2008, 54, 1956-1962
    • (2008) AIChE J. , vol.54 , pp. 1956-1962
    • Hall, C.K.1
  • 9
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • Nguyen, H. D.; Hall, C. K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 16180-16185
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 10
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek, K.; Lewandowska, A.; Zietkiewicz, S. Chaperones in control of protein disaggregation EMBO J. 2008, 27 328-335
    • (2008) EMBO J. , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 11
    • 84874393637 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
    • Rosenzweig, R.; Moradi, S.; Zarrine-Afsar, A.; Glover, J. R.; Kay, L. E. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction Science 2013, 339, 1080-1083
    • (2013) Science , vol.339 , pp. 1080-1083
    • Rosenzweig, R.1    Moradi, S.2    Zarrine-Afsar, A.3    Glover, J.R.4    Kay, L.E.5
  • 13
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular-proteins
    • Dill, K. A. Theory for the folding and stability of globular-proteins Biochemistry 1985, 24 1501-1509
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 14
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. Some factors in the interpretation of protein denaturation Adv. Protein Chem. 1959, 14, 1-63
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 15
    • 84880263124 scopus 로고    scopus 로고
    • Stability of proteins inside a hydrophobic cavity
    • Radhakrishna, M.; Grimaldi, J.; Belfort, G.; Kumar, S. K. Stability of proteins inside a hydrophobic cavity Langmuir 2013, 29, 8922-8928
    • (2013) Langmuir , vol.29 , pp. 8922-8928
    • Radhakrishna, M.1    Grimaldi, J.2    Belfort, G.3    Kumar, S.K.4
  • 17
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular-proteins
    • Yue, K.; Dill, K. A. Forces of tertiary structural organization in globular-proteins Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 146-150
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 146-150
    • Yue, K.1    Dill, K.A.2
  • 19
    • 33646987405 scopus 로고
    • Optimized Monte-Carlo data-Analysis
    • Ferrenberg, A. M.; Swendsen, R. H. Optimized Monte-Carlo data-Analysis Phys. Rev. Lett. 1989, 63, 1195-1198
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 20
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules 0.1. The method
    • Kumar, S.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A.; Rosenberg, J. M. The weighted histogram analysis method for free-energy calculations on biomolecules 0.1. The method J. Comput. Chem. 1992, 13, 1011-1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 21
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F.; Dobson, C. M. Amyloid formation by globular proteins under native conditions Nat. Chem. Biol. 2009, 5, 15-22
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 22
    • 0035949430 scopus 로고    scopus 로고
    • Stabilization of proteins in confined spaces
    • Zhou, H. X.; Dill, K. A. Stabilization of proteins in confined spaces Biochemistry 2001, 40, 11289-11293
    • (2001) Biochemistry , vol.40 , pp. 11289-11293
    • Zhou, H.X.1    Dill, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.