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Volumn 399, Issue , 2005, Pages 177-192

Using NMR spectroscopy to monitor ubiquitin chain conformation and interactions with ubiquitin-binding domains

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITY; COMPLEX FORMATION; LABELING INDEX; MEASUREMENT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; SIGNAL TRANSDUCTION; STOICHIOMETRY;

EID: 28844440078     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)99012-5     Document Type: Review
Times cited : (32)

References (29)
  • 1
    • 0037376172 scopus 로고    scopus 로고
    • Ubiquitin: Not just for proteasomes anymore
    • Aguilar R.C., and Wendland B. Ubiquitin: Not just for proteasomes anymore Curr. Opin. Cell Biol. 15 2003 184 190
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 184-190
    • Aguilar, R.C.1    Wendland, B.2
  • 2
    • 0020482581 scopus 로고
    • A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
    • Berliner L.J., Grunwald J., Hankovszky H.O., and Hideg K. A novel reversible thiol-specific spin label: Papain active site labeling and inhibition Anal. Biochem. 119 1982 450 455
    • (1982) Anal. Biochem. , vol.119 , pp. 450-455
    • Berliner, L.J.1    Grunwald, J.2    Hankovszky, H.O.3    Hideg, K.4
  • 3
    • 0037433504 scopus 로고    scopus 로고
    • Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • Clore G.M., and Schwieters C.D. Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics J. Am. Chem. Soc. 125 2003 2902 2912
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 4
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook W.J., Jeffrey L.C., Kasperek E., and Pickart C.M. Structure of tetraubiquitin shows how multiubiquitin chains can be formed J. Mol. Biol. 236 1994 601 609
    • (1994) J. Mol. Biol. , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3    Pickart, C.M.4
  • 5
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., and Bonvin A.M. HADDOCK: A protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125 2003 1731 1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 6
    • 0035840960 scopus 로고    scopus 로고
    • Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
    • Donaldson L.W., Skrynnikov N.R., Choy W.Y., Muhandiram D.R., Sarkar B., Forman-Kay J.D., and Kay L.E. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy J. Am. Chem. Soc. 123 2001 9843 9847
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9843-9847
    • Donaldson, L.W.1    Skrynnikov, N.R.2    Choy, W.Y.3    Muhandiram, D.R.4    Sarkar, B.5    Forman-kay, J.D.6    Kay, L.E.7
  • 7
    • 0031566963 scopus 로고    scopus 로고
    • The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: Analysis of 15N relaxation with monomer/dimer equilibration
    • Fushman D., Cahill S., and Cowburn D. The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: Analysis of 15N relaxation with monomer/dimer equilibration J. Mol. Biol. 266 1997 173 194
    • (1997) J. Mol. Biol. , vol.266 , pp. 173-194
    • Fushman, D.1    Cahill, S.2    Cowburn, D.3
  • 8
    • 2942544364 scopus 로고    scopus 로고
    • Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements
    • Fushman D., Varadan R., Assfalg M., and Walker O. Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements Progr. NMR Spectrosc. 44 2004 189 214
    • (2004) Progr. NMR Spectrosc. , vol.44 , pp. 189-214
    • Fushman, D.1    Varadan, R.2    Assfalg, M.3    Walker, O.4
  • 11
    • 0034775555 scopus 로고    scopus 로고
    • Distance mapping of protein-binding sites using spin-labeled oligosaccharide ligands
    • Jain N.U., Venot A., Umemoto K., Leffler H., and Prestegard J.H. Distance mapping of protein-binding sites using spin-labeled oligosaccharide ligands Protein Sci. 10 2001 2393 2400
    • (2001) Protein Sci. , vol.10 , pp. 2393-2400
    • Jain, N.U.1    Venot, A.2    Umemoto, K.3    Leffler, H.4    Prestegard, J.H.5
  • 13
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen P.A. Spin labeling of proteins Methods Enzymol. 177 1989 86 121
    • (1989) Methods Enzymol. , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 14
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • McCracken A.A., and Brodsky J.L. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD) Bioessays 25 2003 868 877
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 15
    • 1642482834 scopus 로고    scopus 로고
    • Specificity of the interaction between ubiquitin-associated domains and ubiquitin
    • Mueller T.D., Kamionka M., and Feigon J. Specificity of the interaction between ubiquitin-associated domains and ubiquitin J. Biol. Chem. 279 2004 11926 11936
    • (2004) J. Biol. Chem. , vol.279 , pp. 11926-11936
    • Mueller, T.D.1    Kamionka, M.2    Feigon, J.3
  • 16
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M., and Tansey W.P. How the ubiquitin-proteasome system controls transcription Nat. Rev. Mol. Cell. Biol. 4 2003 192 201
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 17
    • 1542298300 scopus 로고    scopus 로고
    • H2B ubiquitylation: The end is in sight
    • Osley M.A. H2B ubiquitylation: The end is in sight Biochim. Biophys. Acta 1677 2004 74 78
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 74-78
    • Osley, M.A.1
  • 19
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart C.M. Ubiquitin enters the new millennium Mol. Cell. 8 2001 499 504
    • (2001) Mol. Cell. , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 20
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart C.M., and Fushman D. Polyubiquitin chains: Polymeric protein signals Curr. Opin. Chem. Biol. 8 2004 610 616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 21
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski J., Beal R., Hoffmann L., Wilkinson K.D., Cohen R.E., and Pickart C.M. Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths J. Biol. Chem. 272 1997 23712 23721
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffmann, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 22
    • 0141480905 scopus 로고    scopus 로고
    • Binding surface mapping of intra and inter domain interactions among hHR23B, ubiquitin and poly ubiquitin binding site 2 of S5a
    • Ryu K.S., Lee K.J., Bae S.H., Kim B.K., Kim K.A., and Choi B.S. Binding surface mapping of intra and inter domain interactions among hHR23B, ubiquitin and poly ubiquitin binding site 2 of S5a J. Biol. Chem. 278 2003 36621 36627
    • (2003) J. Biol. Chem. , vol.278 , pp. 36621-36627
    • Ryu, K.S.1    Lee, K.J.2    Bae, S.H.3    Kim, B.K.4    Kim, K.A.5    Choi, B.S.6
  • 24
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiqutin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan R., Assfalg M., Haririnia A., Raasi S., Pickart C., and Fushman D. Solution conformation of Lys63-linked di-ubiqutin chain provides clues to functional diversity of polyubiquitin signaling J. Biol. Chem. 279 2004 7055 7063
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 25
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan R., Walker O., Pickart C., and Fushman D. Structural properties of polyubiquitin chains in solution J. Mol. Biol. 324 2002 637 647
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 26
    • 2342535099 scopus 로고    scopus 로고
    • Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from 15N relaxation data using computer program ROTDIF
    • Walker O., Varadan R., and Fushman D. Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from 15N relaxation data using computer program ROTDIF J. Magn. Reson. 168 2004 336 345
    • (2004) J. Magn. Reson. , vol.168 , pp. 336-345
    • Walker, O.1    Varadan, R.2    Fushman, D.3
  • 27
    • 0345686439 scopus 로고    scopus 로고
    • Ubiquitin recognition by the DNA repair protein hHR23a
    • Wang Q., Goh A.M., Howley P.M., and Walters K.J. Ubiquitin recognition by the DNA repair protein hHR23a Biochemistry 42 2003 13529 13535
    • (2003) Biochemistry , vol.42 , pp. 13529-13535
    • Wang, Q.1    Goh, A.M.2    Howley, P.M.3    Walters, K.J.4
  • 28
    • 0242299265 scopus 로고    scopus 로고
    • Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings
    • Wohnert J., Franz K.J., Nitz M., Imperiali B., and Schwalbe H. Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings J. Am. Chem. Soc. 125 2003 13338-1339.
    • (2003) J. Am. Chem. Soc. , vol.125
    • Wohnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 29
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg E.R. Mapping protein-protein interactions in solution by NMR spectroscopy Biochemistry 41 2002 1 7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.