메뉴 건너뛰기




Volumn 20, Issue 5, 2010, Pages 640-648

Cellular structural biology

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CASEIN KINASE; CELL PROTEIN; CYCLIN DEPENDENT KINASE 1; INTRINSICALLY DISORDERED PROTEIN; PROTEIN FKBP12; PROTEIN G; PROTEIN G B1; PROTEIN TTHA1718; TAU PROTEIN; THYMOSIN BETA4; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 78049446457     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.07.006     Document Type: Review
Times cited : (72)

References (56)
  • 2
    • 70350149994 scopus 로고    scopus 로고
    • The 'super-resolution' revolution
    • Davis I. The 'super-resolution' revolution. Biochem Soc Trans 2009, 37:1042-1044.
    • (2009) Biochem Soc Trans , vol.37 , pp. 1042-1044
    • Davis, I.1
  • 4
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson C.V., Sali A., Baumeister W. The molecular sociology of the cell. Nature 2007, 450:973-982.
    • (2007) Nature , vol.450 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 5
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 2001, 26:597-604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 6
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: an important but neglected aspect of the intracellular environment
    • Ellis R.J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr Opin Struct Biol 2001, 11:114-119.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 7
    • 34248187130 scopus 로고    scopus 로고
    • Looking into live cells with in-cell NMR spectroscopy
    • Selenko P., Wagner G. Looking into live cells with in-cell NMR spectroscopy. J Struct Biol 2007, 158:244-253.
    • (2007) J Struct Biol , vol.158 , pp. 244-253
    • Selenko, P.1    Wagner, G.2
  • 8
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: a versatile tool for drug discovery
    • Cheriyan M., Perler F.B. Protein splicing: a versatile tool for drug discovery. Adv Drug Deliv Rev 2009, 61:899-907.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 9
    • 75549088827 scopus 로고    scopus 로고
    • Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy
    • Lundstrom P., Vallurupalli P., Hansen D.F., Kay L.E. Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy. Nat Protoc 2009, 4:1641-1648.
    • (2009) Nat Protoc , vol.4 , pp. 1641-1648
    • Lundstrom, P.1    Vallurupalli, P.2    Hansen, D.F.3    Kay, L.E.4
  • 10
    • 51749087029 scopus 로고    scopus 로고
    • A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli
    • Tong K.I., Yamamoto M., Tanaka T. A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli. J Biomol NMR 2008, 42:59-67.
    • (2008) J Biomol NMR , vol.42 , pp. 59-67
    • Tong, K.I.1    Yamamoto, M.2    Tanaka, T.3
  • 14
  • 15
    • 43949111008 scopus 로고    scopus 로고
    • Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy
    • Li C., Charlton L.M., Lakkavaram A., Seagle C., Wang G., Young G.B., Macdonald J.M., Pielak G.J. Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy. J Am Chem Soc 2008, 130:6310-6311.
    • (2008) J Am Chem Soc , vol.130 , pp. 6310-6311
    • Li, C.1    Charlton, L.M.2    Lakkavaram, A.3    Seagle, C.4    Wang, G.5    Young, G.B.6    Macdonald, J.M.7    Pielak, G.J.8
  • 16
    • 44349088135 scopus 로고    scopus 로고
    • Residue-level interrogation of macromolecular crowding effects on protein stability
    • Charlton L.M., Barnes C.O., Li C., Orans J., Young G.B., Pielak G.J. Residue-level interrogation of macromolecular crowding effects on protein stability. J Am Chem Soc 2008, 130:6826-6830.
    • (2008) J Am Chem Soc , vol.130 , pp. 6826-6830
    • Charlton, L.M.1    Barnes, C.O.2    Li, C.3    Orans, J.4    Young, G.B.5    Pielak, G.J.6
  • 17
    • 48249099670 scopus 로고    scopus 로고
    • Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli
    • Croke R.L., Sallum C.O., Watson E., Watt E.D., Alexandrescu A.T. Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Sci 2008, 17:1434-1445.
    • (2008) Protein Sci , vol.17 , pp. 1434-1445
    • Croke, R.L.1    Sallum, C.O.2    Watson, E.3    Watt, E.D.4    Alexandrescu, A.T.5
  • 18
    • 29544433937 scopus 로고    scopus 로고
    • Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder
    • McNulty B.C., Young G.B., Pielak G.J. Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder. J Mol Biol 2006, 355:893-897.
    • (2006) J Mol Biol , vol.355 , pp. 893-897
    • McNulty, B.C.1    Young, G.B.2    Pielak, G.J.3
  • 20
    • 52449084468 scopus 로고    scopus 로고
    • Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy
    • Curtis-Fisk J., Spencer R.M., Weliky D.P. Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy. J Am Chem Soc 2008, 130:12568-12569.
    • (2008) J Am Chem Soc , vol.130 , pp. 12568-12569
    • Curtis-Fisk, J.1    Spencer, R.M.2    Weliky, D.P.3
  • 24
    • 31744435251 scopus 로고    scopus 로고
    • Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
    • Burz D.S., Dutta K., Cowburn D., Shekhtman A. Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR). Nat Methods 2006, 3:91-93.
    • (2006) Nat Methods , vol.3 , pp. 91-93
    • Burz, D.S.1    Dutta, K.2    Cowburn, D.3    Shekhtman, A.4
  • 25
    • 34250680620 scopus 로고    scopus 로고
    • In-cell NMR for protein-protein interactions (STINT-NMR)
    • Burz D.S., Dutta K., Cowburn D., Shekhtman A. In-cell NMR for protein-protein interactions (STINT-NMR). Nat Protoc 2006, 1:146-152.
    • (2006) Nat Protoc , vol.1 , pp. 146-152
    • Burz, D.S.1    Dutta, K.2    Cowburn, D.3    Shekhtman, A.4
  • 26
    • 49749108543 scopus 로고    scopus 로고
    • In-cell biochemistry using NMR spectroscopy
    • Burz D.S., Shekhtman A. In-cell biochemistry using NMR spectroscopy. PLoS One 2008, 3:e2571.
    • (2008) PLoS One , vol.3
    • Burz, D.S.1    Shekhtman, A.2
  • 27
    • 66749112340 scopus 로고    scopus 로고
    • Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR)
    • Xie J., Thapa R., Reverdatto S., Burz D.S., Shekhtman A. Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR). J Med Chem 2009, 52:3516-3522.
    • (2009) J Med Chem , vol.52 , pp. 3516-3522
    • Xie, J.1    Thapa, R.2    Reverdatto, S.3    Burz, D.S.4    Shekhtman, A.5
  • 29
    • 0003007299 scopus 로고
    • Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments
    • Barna J.C.J., Laue E.D., Mayger M.R., Skilling J., Worrall S.J.P. Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments. J Magn Reson 1987, 73:69-77.
    • (1987) J Magn Reson , vol.73 , pp. 69-77
    • Barna, J.C.J.1    Laue, E.D.2    Mayger, M.R.3    Skilling, J.4    Worrall, S.J.P.5
  • 30
    • 0028469225 scopus 로고
    • Improved resolution in triple-resonance spectra by nonlinear sampling in the constant-time domain
    • Schmieder P, Stern A.S., Wagner G., Hoch J.C. Improved resolution in triple-resonance spectra by nonlinear sampling in the constant-time domain. J Biomol NMR 1994, 4:483-490.
    • (1994) J Biomol NMR , vol.4 , pp. 483-490
    • Schmieder, P.1    Stern, A.S.2    Wagner, G.3    Hoch, J.C.4
  • 31
    • 4243138246 scopus 로고    scopus 로고
    • Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction
    • Rovnyak D., Frueh D.P., Sastry M., Sun Z.Y.J., Stern A.S., Hoch J.C., Wagner G. Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J Magn Reson 2004, 170:15-21.
    • (2004) J Magn Reson , vol.170 , pp. 15-21
    • Rovnyak, D.1    Frueh, D.P.2    Sastry, M.3    Sun, Z.Y.J.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 32
    • 0002546906 scopus 로고
    • Reconstruction of phase sensitive 2D NMR spectra by maximum entropy
    • Laue E.D., Mayger M.R., Skilling J., Staunton J. Reconstruction of phase sensitive 2D NMR spectra by maximum entropy. J Magn Reson 1986, 68:14-29.
    • (1986) J Magn Reson , vol.68 , pp. 14-29
    • Laue, E.D.1    Mayger, M.R.2    Skilling, J.3    Staunton, J.4
  • 36
    • 33747059858 scopus 로고    scopus 로고
    • Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes
    • Selenko P., Serber Z., Gadea B., Ruderman J., Wagner G. Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes. Proc Natl Acad Sci USA 2006, 103:11904-11909.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11904-11909
    • Selenko, P.1    Serber, Z.2    Gadea, B.3    Ruderman, J.4    Wagner, G.5
  • 41
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M., Spillantini M.G. A century of Alzheimer's disease. Science 2006, 314:777-781.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 45
    • 41949097747 scopus 로고    scopus 로고
    • Studying posttranslational modifications by in-cell NMR
    • Lippens G., Landrieu I., Hanoulle X. Studying posttranslational modifications by in-cell NMR. Chem Biol 2008, 15:311-312.
    • (2008) Chem Biol , vol.15 , pp. 311-312
    • Lippens, G.1    Landrieu, I.2    Hanoulle, X.3
  • 47
    • 68249145921 scopus 로고    scopus 로고
    • Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O
    • Ogino S., Kubo S., Umemoto R., Huang S., Nishida N., Shimada I. Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O. J Am Chem Soc 2009, 131:10834-10835.
    • (2009) J Am Chem Soc , vol.131 , pp. 10834-10835
    • Ogino, S.1    Kubo, S.2    Umemoto, R.3    Huang, S.4    Nishida, N.5    Shimada, I.6
  • 50
    • 34250159870 scopus 로고    scopus 로고
    • A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
    • Lescop E., Schanda P., Brutscher B. A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson 2007, 187:163-169.
    • (2007) J Magn Reson , vol.187 , pp. 163-169
    • Lescop, E.1    Schanda, P.2    Brutscher, B.3
  • 51
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda P., Kupce E., Brutscher B. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR 2005, 33:199-211.
    • (2005) J Biomol NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3
  • 54
    • 34548641232 scopus 로고    scopus 로고
    • Retraction
    • Pielak G.J. Retraction. Biochemistry 2007, 46:8206.
    • (2007) Biochemistry , vol.46 , pp. 8206
    • Pielak, G.J.1
  • 56
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh B.J., Mastronarde D.N., Buttle K.F., Howell K.E., McIntosh J.R. Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc Natl Acad Sci U S A 2001, 98:2399-2406.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.