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Volumn 3, Issue , 2013, Pages

Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP2) from Haloferax volcanii

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; UBIQUITIN;

EID: 84881337801     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02136     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. Origin and function of ubiquitin-like proteins. Nature 458, 422-429 (2009).
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 2
    • 77952866393 scopus 로고    scopus 로고
    • More modifiers move on dna damage
    • Morris, J. R. More modifiers move on DNA damage. Cancer Res 70, 3861 (2010).
    • (2010) Cancer Res , vol.70 , pp. 3861
    • Morris, J.R.1
  • 3
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L. & Siepmann, T. J. Pathways of ubiquitin conjugation. FASEB J 11, 1257-1268 (1997). (Pubitemid 27527889)
    • (1997) FASEB Journal , vol.11 , Issue.14 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 4
    • 0032585099 scopus 로고    scopus 로고
    • The ligation systems for ubiquitin and ubiquitin-like proteins
    • Tanaka, K., Suzuki, T. & Chiba, T. The ligation systems for ubiquitin and ubiquitin-like proteins. Mol Cells 8, 503 (1998).
    • (1998) Mol Cells , vol.8 , pp. 503
    • Tanaka, K.1    Suzuki, T.2    Chiba, T.3
  • 5
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat Cell Biol 2, 153-157 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 153-157
    • Hochstrasser, M.1
  • 6
    • 34248222062 scopus 로고    scopus 로고
    • A novel superfamily containing the beta-grasp fold involved in binding diverse soluble ligands
    • Burroughs, A. M., Balaji, S., Iyer, L. M. & Aravind, L. A novel superfamily containing the beta-grasp fold involved in binding diverse soluble ligands. Biol Direct 2 (2007).
    • (2007) Biol Direct , pp. 2
    • Burroughs, A.M.1    Balaji, S.2    Iyer, L.M.3    Aravind, L.4
  • 7
    • 33747219426 scopus 로고    scopus 로고
    • The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like b-grasp domains
    • Iyer, L. M., Burroughs, A. M. & Aravind, L. The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like b-grasp domains. Genome Biol 7, R60 (2006).
    • (2006) Genome Biol , vol.7
    • Iyer, L.M.1    Burroughs, A.M.2    Aravind, L.3
  • 8
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of mycobacterium tuberculosis
    • Pearce, M. J., Mintseris, J., Ferreyra, J., Gygi, S. P. & Darwin, K. H. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science's STKE 322, 1104 (2008).
    • (2008) Science's STKE , vol.322 , pp. 1104
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 9
    • 59149094603 scopus 로고    scopus 로고
    • Proteasomal protein degradation in mycobacteria is dependent upon a prokaryotic ubiquitin-like protein
    • Burns, K. E., Liu, W. T., Boshoff, H. I. M., Dorrestein, P. C. & Barry, C. E. Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein. J Biol Chem 284, 3069-3075 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 3069-3075
    • Burns, K.E.1    Liu, W.T.2    Boshoff, H.I.M.3    Dorrestein, P.C.4    Barry, C.E.5
  • 10
    • 77950524360 scopus 로고    scopus 로고
    • The mycobacterial mpa-proteasome unfolds and degrades pupylated substrates by engaging pup's n-terminus
    • Striebel, F., Hunkeler, M., Summer, H. & Weber-Ban, E. The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus. EMBO J 29, 1262-1271 (2010).
    • (2010) EMBO J , vol.29 , pp. 1262-1271
    • Striebel, F.1    Hunkeler, M.2    Summer, H.3    Weber-Ban, E.4
  • 11
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel, F. et al. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 16, 647-651 (2009).
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 647-651
    • Striebel, F.1
  • 12
    • 70149094758 scopus 로고    scopus 로고
    • Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein
    • Liao, S. et al. Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. Biochem. J 422, 207-215 (2009).
    • (2009) Biochem. J , vol.422 , pp. 207-215
    • Liao, S.1
  • 13
    • 68949184714 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein pup is intrinsically disordered
    • Chen, X. et al. Prokaryotic ubiquitin-like protein pup is intrinsically disordered. J Mol Biol 392, 208-217 (2009).
    • (2009) J Mol Biol , vol.392 , pp. 208-217
    • Chen, X.1
  • 14
    • 73849149089 scopus 로고    scopus 로고
    • Ubiquitin-like small archaeal modifier proteins (samps) in haloferax volcanii
    • Humbard, M. A. et al.Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii. Nature 463, 54-60 (2010).
    • (2010) Nature , vol.463 , pp. 54-60
    • Humbard, M.A.1
  • 15
    • 79952729890 scopus 로고    scopus 로고
    • E1-and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea
    • Miranda, H. V. et al. E1-and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea. Proc Natl Acad Sci U S A 108, 4417 (2011).
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4417
    • Miranda, H.V.1
  • 16
    • 79551497252 scopus 로고    scopus 로고
    • Crystal structure of ubiquitin-like small archaeal modifier protein 1 (samp1) from haloferax volcanii
    • Jeong, Y. J., Jeong, B. C. & Song, H. K. Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii. Biochem Biophys Res Commun 405, 112-117 (2011).
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 112-117
    • Jeong, Y.J.1    Jeong, B.C.2    Song, H.K.3
  • 18
    • 42949104034 scopus 로고    scopus 로고
    • Microbial life at high salt concentrations: Phylogenetic and metabolic diversity
    • Oren, A. Microbial life at high salt concentrations: phylogenetic and metabolic diversity. Saline Systems 4, 13 (2008).
    • (2008) Saline Systems , vol.4 , pp. 13
    • Oren, A.1
  • 19
    • 73949105836 scopus 로고    scopus 로고
    • Structural basis for the aminoacid composition of proteins from halophilic archea
    • Tadeo, X. et al. Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biol 7, e1000257 (2009).
    • (2009) PLoS Biol , vol.7
    • Tadeo, X.1
  • 20
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on unix pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6, 277-293 (1995).
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 22
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J BiomolNMR13, 289-302 (1999). (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 23
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & nmr system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallographica Section D: Biological Crystallography 54, 905-921 (1998).
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 24
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • DOI 10.1023/A:1008365802830
    • Linge, J. & Nilges, M. Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation. J Biomol NMR 13, 51-59 (1999). (Pubitemid 29089239)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.1 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 26
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14, 51 (1996).
    • (1996) J Mol Graph , vol.14 , pp. 51
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 28
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura, K., Dudley, J., Nei, M. & Kumar, S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24, 1596-1599 (2007). (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.