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Volumn 291, Issue 8, 2016, Pages 3776-3784

A unique tool for cellular structural biology: In-cell NMR

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; MACROMOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84964595271     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R115.643247     Document Type: Review
Times cited : (71)

References (57)
  • 2
    • 0035913735 scopus 로고    scopus 로고
    • Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy
    • Serber, Z., Ledwidge, R., Miller, S. M., and Dötsch, V. (2001) Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J. Am. Chem. Soc. 123, 8895-8901
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8895-8901
    • Serber, Z.1    Ledwidge, R.2    Miller, S.M.3    Dötsch, V.4
  • 6
    • 31744435251 scopus 로고    scopus 로고
    • Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
    • Burz, D. S., Dutta, K., Cowburn, D., and Shekhtman, A. (2006) Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR). Nat. Methods. 3, 91-93
    • (2006) Nat. Methods. , vol.3 , pp. 91-93
    • Burz, D.S.1    Dutta, K.2    Cowburn, D.3    Shekhtman, A.4
  • 7
    • 34250680620 scopus 로고    scopus 로고
    • In-cell NMR for protein-protein interactions (STINT-NMR)
    • Burz, D. S., Dutta, K., Cowburn, D., and Shekhtman, A. (2006) In-cell NMR for protein-protein interactions (STINT-NMR). Nat. Protoc. 1, 146-152
    • (2006) Nat. Protoc. , vol.1 , pp. 146-152
    • Burz, D.S.1    Dutta, K.2    Cowburn, D.3    Shekhtman, A.4
  • 8
    • 49749108543 scopus 로고    scopus 로고
    • In-cell biochemistry using NMR spectroscopy
    • Burz, D. S., and Shekhtman, A. (2008) In-cell biochemistry using NMR spectroscopy. PLoS One 3, e2571
    • (2008) PLoS One , vol.3
    • Burz, D.S.1    Shekhtman, A.2
  • 9
    • 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., and Shekhtman, A. (2009) Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR). J. Med. Chem. 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
  • 10
    • 84894236263 scopus 로고    scopus 로고
    • Nonuniform sampling and maximum entropy reconstruction in multidimensional NMR
    • Hoch, J. C., and Maciejewski, M. W., Mobli, M., Schuyler, A. D., and Stern, A. S. (2014) Nonuniform sampling and maximum entropy reconstruction in multidimensional NMR. Acc. Chem. Res. 47, 708-717
    • (2014) Acc. Chem. Res. , vol.47 , pp. 708-717
    • Hoch, J.C.1    Maciejewski, M.W.2    Mobli, M.3    Schuyler, A.D.4    Stern, A.S.5
  • 11
    • 20444393525 scopus 로고    scopus 로고
    • Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • Schanda, P., and Brutscher, B. (2005) Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J. Am. Chem. Soc. 127, 8014-8015
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 12
    • 23744476746 scopus 로고    scopus 로고
    • Multidimensional NMR spectroscopy for protein characterization and assignment inside cells
    • Reardon, P. N., and Spicer, L. D. (2005) Multidimensional NMR spectroscopy for protein characterization and assignment inside cells. J. Am. Chem. Soc. 127, 10848-10849
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10848-10849
    • Reardon, P.N.1    Spicer, L.D.2
  • 15
    • 84907021256 scopus 로고    scopus 로고
    • 13C NMR spectroscopy for the study of intrinsically disordered proteins
    • 13C NMR spectroscopy for the study of intrinsically disordered proteins. Nat. Protoc. 9, 2005-2016
    • (2014) Nat. Protoc. , vol.9 , pp. 2005-2016
    • Felli, I.C.1    Gonnelli, L.2    Pierattelli, R.3
  • 16
    • 84896976898 scopus 로고    scopus 로고
    • 13C detection to study intrinsically disordered proteins
    • 13C detection to study intrinsically disordered proteins. J. Magn. Reson. 241, 115-125
    • (2014) J. Magn. Reson. , vol.241 , pp. 115-125
    • Felli, I.C.1    Pierattelli, R.2
  • 18
    • 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., and Wagner, G. (2006) Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes. Proc. Natl. Acad. Sci. U.S.A. 103, 11904-11909
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11904-11909
    • Selenko, P.1    Serber, Z.2    Gadea, B.3    Ruderman, J.4    Wagner, G.5
  • 21
    • 84875902527 scopus 로고    scopus 로고
    • Investigation of quadruplex structure under physiological conditions using in-cell NMR
    • Hänsel, R., Foldynová-Trantírková, S., Dötsch, V., and Trantírek, L. (2013) Investigation of quadruplex structure under physiological conditions using in-cell NMR. Top. Curr. Chem. 330, 47-65
    • (2013) Top. Curr. Chem. , vol.330 , pp. 47-65
    • Hänsel, R.1    Foldynová-Trantírková, S.2    Dötsch, V.3    Trantírek, L.4
  • 24
    • 68249145921 scopus 로고    scopus 로고
    • Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a poreforming toxin, streptolysin O
    • Ogino, S., Kubo, S., Umemoto, R., Huang, S., Nishida, N., and Shimada, I. (2009) Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a poreforming toxin, streptolysin O. J. Am. Chem. Soc. 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
  • 25
    • 85042436934 scopus 로고    scopus 로고
    • Bekei, B. (2013) In-cell NMR Spectroscopy in Mammalian Cells. Ph.D. thesis, Freie Universität Berlin, Germany
  • 27
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu, A. R., Lu, W., and Jones, E. Y. (2006) A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D. Biol. Crystallogr. 62, 1243-1250
    • (2006) Acta Crystallogr. D. Biol. Crystallogr. , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 29
    • 84879360441 scopus 로고    scopus 로고
    • Visualization of redox-controlled protein fold in living cells
    • Banci, L., Barbieri, L., Luchinat, E., and Secci, E. (2013) Visualization of redox-controlled protein fold in living cells. Chem. Biol. 20, 747-752
    • (2013) Chem. Biol. , vol.20 , pp. 747-752
    • Banci, L.1    Barbieri, L.2    Luchinat, E.3    Secci, E.4
  • 33
    • 84872413122 scopus 로고    scopus 로고
    • A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells
    • Kubo, S., Nishida, N., Udagawa, Y., Takarada, O., Ogino, S., and Shimada, I. (2013) A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells. Angew. Chem. Int. Ed. Engl. 52, 1208-1211
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 1208-1211
    • Kubo, S.1    Nishida, N.2    Udagawa, Y.3    Takarada, O.4    Ogino, S.5    Shimada, I.6
  • 35
    • 84942122066 scopus 로고    scopus 로고
    • Hydrogen exchange of disordered proteins in Escherichia coli
    • Smith, A. E., and Zhou, L. Z., and Pielak, G. J. (2015) Hydrogen exchange of disordered proteins in Escherichia coli. Protein Sci. 24, 706-713
    • (2015) Protein Sci. , vol.24 , pp. 706-713
    • Smith, A.E.1    Zhou, L.Z.2    Pielak, G.J.3
  • 36
    • 79957787217 scopus 로고    scopus 로고
    • Macromolecular crowding fails to fold a globular protein in cells
    • Schlesinger, A. P., Wang, Y., Tadeo, X., Millet, O., and Pielak, G. J. (2011) Macromolecular crowding fails to fold a globular protein in cells. J. Am. Chem. Soc. 133, 8082-8085
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8082-8085
    • Schlesinger, A.P.1    Wang, Y.2    Tadeo, X.3    Millet, O.4    Pielak, G.J.5
  • 37
    • 79551565926 scopus 로고    scopus 로고
    • Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy
    • Barnes, C. O., and Monteith, W. B., and Pielak, G. J. (2011) Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. Chembiochem 12, 390-391
    • (2011) Chembiochem , vol.12 , pp. 390-391
    • Barnes, C.O.1    Monteith, W.B.2    Pielak, G.J.3
  • 38
    • 80055013471 scopus 로고    scopus 로고
    • Exploring weak, transient protein-protein interactionsin crowdedin vivoenvironments by in-cell nuclear magnetic resonance spectroscopy
    • Wang, Q., Zhuravleva, A., and Gierasch, L. M. (2011) Exploring weak, transient protein-protein interactionsin crowdedin vivoenvironments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry 50, 9225-9236
    • (2011) Biochemistry , vol.50 , pp. 9225-9236
    • Wang, Q.1    Zhuravleva, A.2    Gierasch, L.M.3
  • 39
    • 77955686807 scopus 로고    scopus 로고
    • Effects of proteins on protein diffusion
    • Wang, Y., Li, C., and Pielak, G. J. (2010) Effects of proteins on protein diffusion. J. Am. Chem. Soc. 132, 9392-9397
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9392-9397
    • Wang, Y.1    Li, C.2    Pielak, G.J.3
  • 42
    • 84905652881 scopus 로고    scopus 로고
    • Residue level quantification of protein stability in living cells
    • Monteith, W. B., and Pielak, G. J. (2014) Residue level quantification of protein stability in living cells. Proc. Natl. Acad. Sci. U.S.A. 111, 11335-11340
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 11335-11340
    • Monteith, W.B.1    Pielak, G.J.2
  • 43
    • 79955024130 scopus 로고    scopus 로고
    • Protein interactions in the Escherichia coli cytosol: An impediment to in-cell NMR spectroscopy
    • Crowley, P. B., Chow, E., and Papkovskaia, T. (2011) Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy. Chembiochem 12, 1043-1048
    • (2011) Chembiochem , vol.12 , pp. 1043-1048
    • Crowley, P.B.1    Chow, E.2    Papkovskaia, T.3
  • 44
    • 84928038173 scopus 로고    scopus 로고
    • Specific ion effects on macromolecular interactions in Escherichia coli extracts
    • Kyne, C., Ruhle, B., Gautier, V. W., and Crowley, P. B. (2015) Specific ion effects on macromolecular interactions in Escherichia coli extracts. Protein Sci. 24, 310-318
    • (2015) Protein Sci. , vol.24 , pp. 310-318
    • Kyne, C.1    Ruhle, B.2    Gautier, V.W.3    Crowley, P.B.4
  • 46
    • 0020135896 scopus 로고
    • Molecular evolution, intracellular organization, and the quinary structure of proteins
    • McConkey, E. H. (1982) Molecular evolution, intracellular organization, and the quinary structure of proteins. Proc. Natl. Acad. Sci. U.S.A. 79, 3236-3240
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3236-3240
    • McConkey, E.H.1
  • 47
    • 84883771864 scopus 로고    scopus 로고
    • Fate of pup inside the Mycobacterium proteasome studied by in-cell NMR
    • Maldonado, A. Y., and Burz, D. S., Reverdatto, S., and Shekhtman, A. (2013) Fate of pup inside the Mycobacterium proteasome studied by in-cell NMR. PLoS One 8, e74576
    • (2013) PLoS One , vol.8
    • Maldonado, A.Y.1    Burz, D.S.2    Reverdatto, S.3    Shekhtman, A.4
  • 48
    • 80755123408 scopus 로고    scopus 로고
    • Probing the interaction of cisplatin with the human copper chaperone Atox1 by solution and in-cell NMR spectroscopy
    • Arnesano, F., Banci, L., Bertini, I., Felli, I. C., Losacco, M., and Natile, G. (2011) Probing the interaction of cisplatin with the human copper chaperone Atox1 by solution and in-cell NMR spectroscopy. J. Am. Chem. Soc. 133, 18361-18369
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18361-18369
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Felli, I.C.4    Losacco, M.5    Natile, G.6
  • 50
    • 84884700421 scopus 로고    scopus 로고
    • Multi-phosphorylation of the intrinsically disordered unique domain of c-Src studied by in-cell and real-time NMR spectroscopy
    • Amata, I., Maffei, M., Igea, A., Gay, M., Vilaseca, M., Nebreda, A. R., and Pons, M. (2013) Multi-phosphorylation of the intrinsically disordered unique domain of c-Src studied by in-cell and real-time NMR spectroscopy. Chembiochem 14, 1820-1827
    • (2013) Chembiochem , vol.14 , pp. 1820-1827
    • Amata, I.1    Maffei, M.2    Igea, A.3    Gay, M.4    Vilaseca, M.5    Nebreda, A.R.6    Pons, M.7
  • 53
    • 84905233694 scopus 로고    scopus 로고
    • Structural insights of proteins in sub-cellular compartments: In-mitochondria NMR
    • Barbieri, L., Luchinat, E., and Banci, L. (2014) Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR. Biochim. Biophys. Acta. 1843, 2492-2496
    • (2014) Biochim. Biophys. Acta. , vol.1843 , pp. 2492-2496
    • Barbieri, L.1    Luchinat, E.2    Banci, L.3
  • 56
    • 84857512432 scopus 로고    scopus 로고
    • In-cell solid-state NMR as a tool to study proteins in large complexes
    • Reckel, S., and Lopez, J. J., Löhr, F., Glaubitz, C., and Dötsch, V. (2012) In-cell solid-state NMR as a tool to study proteins in large complexes. Chembiochem 13, 534-537
    • (2012) Chembiochem , vol.13 , pp. 534-537
    • Reckel, S.1    Lopez, J.J.2    Löhr, F.3    Glaubitz, C.4    Dötsch, V.5
  • 57
    • 84918516256 scopus 로고    scopus 로고
    • Combining in-cell NMR and x-ray fluorescence microscopy to reveal the intracellular maturation states of human superoxide dismutase 1
    • (Camb.)
    • Luchinat, E., Gianoncelli, A., Mello, T., Galli, A., and Banci, L. (2015) Combining in-cell NMR and x-ray fluorescence microscopy to reveal the intracellular maturation states of human superoxide dismutase 1. Chem. Commun. (Camb.) 51, 584-587
    • (2015) Chem. Commun. , vol.51 , pp. 584-587
    • Luchinat, E.1    Gianoncelli, A.2    Mello, T.3    Galli, A.4    Banci, L.5


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