메뉴 건너뛰기




Volumn 1747, Issue 1, 2005, Pages 93-97

Human ribosomal protein S13: Cloning, expression, refolding, and structural stability

Author keywords

Expression; Human ribosomal protein S13; Refolding; Secondary structure

Indexed keywords

RECOMBINANT PROTEIN; RIBOSOMAL PROTEIN S13; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 12844252484     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.10.001     Document Type: Article
Times cited : (10)

References (23)
  • 4
    • 0032486089 scopus 로고    scopus 로고
    • Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; A cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 a resolution
    • P. Dube, G. Bacher, H. Stark, F. Mueller, F. Zemlin, M. van Heel, and R. Brimacombe Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; a cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 A resolution J. Mol. Biol. 279 1998 403 421
    • (1998) J. Mol. Biol. , vol.279 , pp. 403-421
    • Dube, P.1    Bacher, G.2    Stark, H.3    Mueller, F.4    Zemlin, F.5    Van Heel, M.6    Brimacombe, R.7
  • 5
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • I.G. Wool Extraribosomal functions of ribosomal proteins Trends Biochem. Sci. 1996 164 165
    • (1996) Trends Biochem. Sci. , pp. 164-165
    • Wool, I.G.1
  • 6
    • 1342265497 scopus 로고    scopus 로고
    • RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis
    • C.Y. Jang, J.Y. Lee, and J. Kim RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis FEBS Lett. 560 2004 81 85
    • (2004) FEBS Lett. , vol.560 , pp. 81-85
    • Jang, C.Y.1    Lee, J.Y.2    Kim, J.3
  • 7
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Y. Zhang, G.W. Wolf, K. Bhat, A. Jin, T. Allio, W.A. Burkhart, and Y. Xiong Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway Mol. Cell. Biol. 23 2003 8902 8912
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 9
    • 0142227209 scopus 로고    scopus 로고
    • Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
    • B. Mazumder, P. Sampath, V. Seshadri, R.K. Maitra, P.E. DiCorleto, and P.L. Fox Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control Cell 115 2003 187 198
    • (2003) Cell , vol.115 , pp. 187-198
    • Mazumder, B.1    Sampath, P.2    Seshadri, V.3    Maitra, R.K.4    Dicorleto, P.E.5    Fox, P.L.6
  • 11
    • 0001320597 scopus 로고    scopus 로고
    • Mammalian ribosomes: The structure and the evolution of the proteins
    • J.W.B. Hershey M. Mathews N. Sonenberg Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • I.G. Wool, Y.-L. Chan, and A. Glueck Mammalian ribosomes: the structure and the evolution of the proteins J.W.B. Hershey M. Mathews N. Sonenberg Translational Control 1998 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 685 732
    • (1998) Translational Control , pp. 685-732
    • Wool, I.G.1    Chan, Y.-L.2    Glueck, A.3
  • 12
    • 13144276305 scopus 로고    scopus 로고
    • Conformational variability of the N-terminal helix in the structure of ribosomal protein S15
    • W.M. Clemons Jr., C. Davies, S.W. White, and V. Ramakrishnan Conformational variability of the N-terminal helix in the structure of ribosomal protein S15 Structure 6 1998 429 438
    • (1998) Structure , vol.6 , pp. 429-438
    • Clemons Jr., W.M.1    Davies, C.2    White, S.W.3    Ramakrishnan, V.4
  • 13
    • 0036303417 scopus 로고    scopus 로고
    • Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16 S RNA
    • D.E. Brodersen, W.M. Clemons Jr., A.P. Carter, B.T. Wimberly, and V. Ramakrishnan Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA J. Mol. Biol. 316 2002 725 768
    • (2002) J. Mol. Biol. , vol.316 , pp. 725-768
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Wimberly, B.T.4    Ramakrishnan, V.5
  • 14
    • 0034615759 scopus 로고    scopus 로고
    • Structure of the S15, S6, S18-rRNA complex: Assembly of the 30S ribosome central domain
    • S.C. Agalarov, G. Sridhar Prasad, P.M. Funke, C.D. Stout, and J.R Williamson Structure of the S15, S6, S18-rRNA complex: assembly of the 30S ribosome central domain Science 288 2000 107 113
    • (2000) Science , vol.288 , pp. 107-113
    • Agalarov, S.C.1    Sridhar Prasad, G.2    Funke, P.M.3    Stout, C.D.4    Williamson, J.R.5
  • 15
    • 0037361107 scopus 로고    scopus 로고
    • Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26
    • A. Malygin, O. Baranovskaya, A. Ivanov, and G. Karpova Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26 Protein Expr. Purif. 28 2003 57 62
    • (2003) Protein Expr. Purif. , vol.28 , pp. 57-62
    • Malygin, A.1    Baranovskaya, O.2    Ivanov, A.3    Karpova, G.4
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • T.E. Creighton Oxford University Press Oxford
    • D.P. Goldenberg Analysis of protein conformation by gel electrophoresis T.E. Creighton Protein Structure, a Practical Approach 1989 Oxford University Press Oxford 225 250
    • (1989) Protein Structure, a Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 19
    • 0034571236 scopus 로고    scopus 로고
    • Proteins S7, S10, S16, and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt
    • A.A. Malygin, D.D. Shaulo, and G.G. Karpova Proteins S7, S10, S16, and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt Biochim. Biophys. Acta 1494 2000 213 216
    • (2000) Biochim. Biophys. Acta , vol.1494 , pp. 213-216
    • Malygin, A.A.1    Shaulo, D.D.2    Karpova, G.G.3
  • 20
    • 0033042935 scopus 로고    scopus 로고
    • Analysis of protein circular dichroism spectra based on the tertiary structure classification
    • N. Sreerama, S.Yu. Venyaminov, and R.W. Woody Analysis of protein circular dichroism spectra based on the tertiary structure classification Protein Sci. 8 1999 370 380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Yu.2    Woody, R.W.3
  • 21
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • R.F. Doolittle Academic Press NY
    • J. Garnier, J.-F. Gibrat, and B. Robson GOR method for predicting protein secondary structure from amino acid sequence R.F. Doolittle Methods in Enzymology vol. 266 1996 Academic Press NY 540 553
    • (1996) Methods in Enzymology , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.-F.2    Robson, B.3
  • 22
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 23
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • G. Pollastri, D. Przybylski, B. Rost, and P. Baldi Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles Proteins 47 2002 228 235
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.