메뉴 건너뛰기




Volumn 1764, Issue 1, 2006, Pages 44-54

Three-dimensional domain-swapped oligomers of ribonuclease A: Identification of a fifth tetramer, pentamers and hexamers, and detection of trace heptameric, octameric and nonameric species

Author keywords

RNase A hexamer; RNase A oligomer; RNase A pentamer; RNase A tetramer; Three dimensional domain swapping

Indexed keywords

DIVYNILSULFONE; OLIGOMER; POLYMER; RIBONUCLEASE A; SULFONE DERIVATIVE; TETRAMER; UNCLASSIFIED DRUG;

EID: 33644841204     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.10.011     Document Type: Article
Times cited : (42)

References (21)
  • 2
    • 0013805383 scopus 로고
    • Preparation and properties of two active forms of ribonuclease dimer
    • R.G. Fruchter, and A.M. Crestfield Preparation and properties of two active forms of ribonuclease dimer J. Biol. Chem. 240 1965 3868 3874
    • (1965) J. Biol. Chem. , vol.240 , pp. 3868-3874
    • Fruchter, R.G.1    Crestfield, A.M.2
  • 3
    • 0029833445 scopus 로고    scopus 로고
    • The activity on double-stranded RNA of aggregates of ribonuclease a higher than dimers increases as a function of the size of the aggregates
    • M. Libonati, M. Bertoldi, and S. Sorrentino The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates Biochem. J. 318 1996 287 290
    • (1996) Biochem. J. , vol.318 , pp. 287-290
    • Libonati, M.1    Bertoldi, M.2    Sorrentino, S.3
  • 4
    • 0001483424 scopus 로고    scopus 로고
    • Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme
    • G. Gotte, M. Bertoldi, and M. Libonati Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme Eur. J. Biochem. 265 1999 680 687
    • (1999) Eur. J. Biochem. , vol.265 , pp. 680-687
    • Gotte, G.1    Bertoldi, M.2    Libonati, M.3
  • 5
    • 0033773675 scopus 로고    scopus 로고
    • Dimer formation by a "monomeric" protein
    • C. Park, and R.T. Raines Dimer formation by a "monomeric" protein Protein Sci. 9 2000 2026 2033
    • (2000) Protein Sci. , vol.9 , pp. 2026-2033
    • Park, C.1    Raines, R.T.2
  • 6
    • 0037518055 scopus 로고    scopus 로고
    • Thermal aggregation of ribonuclease A. a contribution to the understanding of the role of 3D domain swapping in protein aggregation
    • G. Gotte, F. Vottariello, and M. Libonati Thermal aggregation of ribonuclease A. A contribution to the understanding of the role of 3D domain swapping in protein aggregation J. Biol. Chem. 278 2003 10763 10769
    • (2003) J. Biol. Chem. , vol.278 , pp. 10763-10769
    • Gotte, G.1    Vottariello, F.2    Libonati, M.3
  • 7
    • 0032584210 scopus 로고    scopus 로고
    • The crystal structure of a 3D domain-swapped dimer of RNase a at 2.1-Å resolution
    • Y. Liu, P.J. Hart, M.P. Schlunegger, and D. Eisenberg The crystal structure of a 3D domain-swapped dimer of RNase A at 2.1-Å resolution Proc. Natl. Acad. Sci. U. S. A. 95 1998 3437 3442
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3437-3442
    • Liu, Y.1    Hart, P.J.2    Schlunegger, M.P.3    Eisenberg, D.4
  • 8
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase a dimer with implications for amyloid formation
    • Y. Liu, G. Gotte, M. Libonati, and D. Eisenberg A domain-swapped RNase A dimer with implications for amyloid formation Nat. Struct. Biol. 8 2001 211 214
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 10
    • 0036145653 scopus 로고    scopus 로고
    • Structures of the two 3D domain-swapped RNase a trimers
    • Y. Liu, G. Gotte, M. Libonati, and D. Eisenberg Structures of the two 3D domain-swapped RNase A trimers Protein Sci. 11 2002 371 380
    • (2002) Protein Sci. , vol.11 , pp. 371-380
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 11
    • 0034802585 scopus 로고    scopus 로고
    • Structural properties of trimers and tetramers of ribonuclease a
    • A. Nenci, G. Gotte, M. Bertoldi, and M. Libonati Structural properties of trimers and tetramers of ribonuclease A Protein Sci. 10 2001 2017 2027
    • (2001) Protein Sci. , vol.10 , pp. 2017-2027
    • Nenci, A.1    Gotte, G.2    Bertoldi, M.3    Libonati, M.4
  • 12
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Y. Liu, and D. Eisenberg 3D domain swapping: as domains continue to swap Protein Sci. 11 2002 1285 1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 13
    • 4344637862 scopus 로고    scopus 로고
    • Oligomerization of ribonuclease A. Two novel three-dimensional domain-swapped tetramers
    • G. Gotte, and M. Libonati Oligomerization of ribonuclease A. Two novel three-dimensional domain-swapped tetramers J. Biol. Chem. 279 2004 36670 36679
    • (2004) J. Biol. Chem. , vol.279 , pp. 36670-36679
    • Gotte, G.1    Libonati, M.2
  • 14
    • 2942722363 scopus 로고    scopus 로고
    • Oligomerization of bovine ribonuclease A: Structural and functional features of its multimers
    • M. Libonati, and G. Gotte Oligomerization of bovine ribonuclease A: structural and functional features of its multimers Biochem. J. 380 2004 311 327
    • (2004) Biochem. J. , vol.380 , pp. 311-327
    • Libonati, M.1    Gotte, G.2
  • 15
    • 9744278349 scopus 로고    scopus 로고
    • Biological actions of the oligomers of ribonuclease A, CMLS
    • M. Libonati Biological actions of the oligomers of ribonuclease A, CMLS Cell. Mol. Life Sci. 61 2004 2431 2436
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2431-2436
    • Libonati, M.1
  • 16
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • T.E. Creighton (Ed.), Oxford University Press, IRL Press, Oxford, UK
    • D.P. Goldenberg, Analysis of protein conformation by gel electrophoresis, in: T.E. Creighton (Ed.), Protein Structure. A practical approach., Oxford University Press, IRL Press, Oxford, UK, 1989, pp. 225-250.
    • (1989) Protein Structure. A Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 18
    • 84872631302 scopus 로고
    • A spectrophotometric method for the measurement of ribonuclease activity
    • M. Kunitz A spectrophotometric method for the measurement of ribonuclease activity J. Biol. Chem. 164 1946 563 568
    • (1946) J. Biol. Chem. , vol.164 , pp. 563-568
    • Kunitz, M.1
  • 19
    • 0034803919 scopus 로고    scopus 로고
    • Degradation of double-stranded RNA by mammalian pancreatic-type ribonucleases
    • M. Libonati, and S. Sorrentino Degradation of double-stranded RNA by mammalian pancreatic-type ribonucleases Methods Enzymol. 341 2001 234 248
    • (2001) Methods Enzymol. , vol.341 , pp. 234-248
    • Libonati, M.1    Sorrentino, S.2
  • 21
    • 0015242862 scopus 로고
    • Degradation of poly(A) and double-stranded RNA by aggregates of pancreatic ribonuclease
    • M. Libonati Degradation of poly(A) and double-stranded RNA by aggregates of pancreatic ribonuclease Biochim. Biophys. Acta 228 1971 440 445
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 440-445
    • Libonati, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.