The effect of the hexahistidine-tag in the oligomerization of HSC70 constructs.
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M. Ladjimi | Mouna Amor-Mahjoub | Jean-Philippe Suppini | Nathalie Gomez-Vrielyunck | Moncef Ladjimi | J. Suppini | M. Amor-Mahjoub | N. Gomez-Vrielyunck
[1] Jian-ning Liu,et al. An efficient system for production of recombinant urokinase-type plasminogen activator. , 1997, Protein expression and purification.
[2] M. Little,et al. Bacterial expression and refolding of single-chain Fv fragments with C-terminal cysteines , 1995, Cell Biophysics.
[3] F. Hartl,et al. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.
[4] P. Schuck,et al. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. , 2000, Biopolymers.
[5] Jason C. Young,et al. Pathways of chaperone-mediated protein folding in the cytosol , 2004, Nature Reviews Molecular Cell Biology.
[6] S. Brakmann,et al. Expression and purification of histidine-tagged bacteriophage T7 DNA polymerase. , 2005, Protein expression and purification.
[7] C. Ban,et al. Oligomerization of a MutS Mismatch Repair Protein from Thermus aquaticus * , 1999, The Journal of Biological Chemistry.
[8] C. Gibbs,et al. A nickel chelate microtiter plate assay for six histidine-containing proteins. , 1996, Analytical biochemistry.
[9] M. Ladjimi,et al. Effect of Nucleotides, Peptides, and Unfolded Proteins on the Self-association of the Molecular Chaperone HSC70* , 1996, The Journal of Biological Chemistry.
[10] V. Gaberc-Porekar,et al. Perspectives of immobilized-metal affinity chromatography. , 2001, Journal of biochemical and biophysical methods.
[11] A. Nordheim,et al. Affinity purification of histidine-tagged proteins transiently produced in HeLa cells. , 1992, Gene.
[12] P. Young,et al. Current trends in molecular recognition and bioseparation. , 1995, Journal of chromatography. A.
[13] G. Bentley,et al. Sequence analysis of a monoclonal antibody specific for the preS2 region of hepatitis B surface antigen, and the cloning, expression and characterisation of its single‐chain Fv construction , 1998, FEBS letters.
[14] M. Feiss,et al. Cloning, Expression, and Biochemical Characterization of Hexahistidine-tagged Terminase Proteins* , 1999, The Journal of Biological Chemistry.
[15] Martin Hammarström,et al. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors , 2004, Journal of Structural and Functional Genomics.
[16] M. Ladjimi,et al. Self-association of the molecular chaperone HSC70. , 1995, Biochemistry.
[17] B. Villoutreix,et al. Quaternary structure of the HSC70 cochaperone HIP. , 2000, Biochemistry.
[18] J. Hopp,et al. Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt(II)-carboxymethylaspartate crosslinked agarose. , 1999, Journal of chromatography. A.
[19] C. Angelidis,et al. Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms. , 1999, European journal of biochemistry.
[20] E K M Ueda,et al. Current and prospective applications of metal ion-protein binding. , 2003, Journal of chromatography. A.
[21] E. Kremmer,et al. Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions. , 1997, BioTechniques.
[22] J. Pedersen,et al. Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases. , 1999, Protein expression and purification.
[23] N. Hynes,et al. Characterization of scFv-421, a single-chain antibody targeted to p53. , 1997, Biochemical and biophysical research communications.
[24] B. Bukau,et al. The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components (*) , 1995, The Journal of Biological Chemistry.
[25] Beatrice Vallone,et al. Large-scale purification and crystallization of the endoribonuclease XendoU: troubleshooting with His-tagged proteins , 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.
[26] H M Sassenfeld,et al. Engineering proteins for purification. , 1990, Trends in biotechnology.
[27] T. The,et al. Immobilised metal-ion affinity chromatography purification of histidine-tagged recombinant proteins: a wash step with a low concentration of EDTA. , 2001, Journal of chromatography. B, Biomedical sciences and applications.
[28] Tristan J. Vaughan,et al. Human Antibodies with Sub-nanomolar Affinities Isolated from a Large Non-immunized Phage Display Library , 1996, Nature Biotechnology.
[29] J. Rothman,et al. The ATPase core of a clathrin uncoating protein. , 1987, The Journal of biological chemistry.
[30] C. Piesse,et al. Expression and purification of rat recombinant aminopeptidase B secreted from baculovirus-infected insect cells. , 2004, Protein expression and purification.
[31] M. Murtaugh,et al. High-level secretion of two antibody single chain Fv fragments by Pichia pastoris. , 1997, Journal of immunological methods.
[32] J. Janson,et al. Production, purification and characterization of recombinant human interferon γ , 1992 .
[33] A. Plückthun,et al. The Functional Expression of Antibody Fv Fragments in Ischhuchia coli: Improved Vectors and a Generally Applicable Purification Technique , 1991, Bio/Technology.
[34] V. Diehl,et al. A new series of pET-derived vectors for high efficiency expression of Pseudomonas exotoxin-based fusion proteins. , 1999, Gene.
[35] L. Hendershot,et al. Interconversion of three differentially modified and assembled forms of BiP. , 1992, The EMBO journal.
[36] D. Kuntz,et al. A Single Chain Fv Fragment of P-glycoprotein-specific Monoclonal Antibody C219 , 1997, The Journal of Biological Chemistry.
[37] A. Fink,et al. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[38] Sunanda R. Narayanan,et al. Preparative affinity chromatography of proteins , 1990 .
[39] I. Takenaka,et al. Hsc70-binding Peptides Selected from a Phage Display Peptide Library that Resemble Organellar Targeting Sequences (*) , 1995, The Journal of Biological Chemistry.
[40] T. Laue,et al. Modern applications of analytical ultracentrifugation. , 1999, Annual review of biophysics and biomolecular structure.
[41] J. Porath,et al. Metal chelate affinity chromatography, a new approach to protein fractionation , 1975, Nature.
[42] M. Ladjimi,et al. The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70* , 1997, The Journal of Biological Chemistry.
[43] V. Gaberc-Porekar,et al. Influence of the protein oligomericity on final yield after affinity tag removal in purification of recombinant proteins. , 2006, Journal of chromatography. A.
[44] Lei Fang,et al. An Improved Strategy for High‐Level Production of Human Vasostatin120–180 , 2008, Biotechnology progress.
[45] V. Gaberc-Porekar,et al. Attachment of Histidine Tags to Recombinant Tumor Necrosis Factor-Alpha Drastically Changes Its Properties , 2002, TheScientificWorldJournal.
[46] M. Gething,et al. Substrate Binding Induces Depolymerization of the C-terminal Peptide Binding Domain of Murine GRP78/BiP* , 1998, The Journal of Biological Chemistry.
[47] M. Uhlén,et al. Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins. , 1997, Protein expression and purification.
[48] Michael B. Murphy,et al. High-throughput purification of hexahistidine-tagged proteins expressed in E. coli. , 2005, Methods in molecular biology.
[49] Zhinan Xu,et al. Efficient production of a soluble fusion protein containing human beta-defensin-2 in E. coli cell-free system. , 2005, Journal of biotechnology.
[50] E. Eisenberg,et al. Effect of Constitutive 70-kDa Heat Shock Protein Polymerization on Its Interaction with Protein Substrate* , 1996, The Journal of Biological Chemistry.
[51] F. Hartl,et al. Molecular chaperones in cellular protein folding. , 1995, BioEssays : news and reviews in molecular, cellular and developmental biology.
[52] D. Waugh,et al. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. , 2006, Protein expression and purification.
[53] W. Tarpley,et al. Metal affinity chromatography of recombinant HIV‐1 reverse transcriptase containing a human renin cleavable metal binding domain , 1991, Biotechnology and applied biochemistry.
[54] C. Ebel,et al. Oligomerization of the 17-kDa peptide-binding domain of the molecular chaperone HSC70. , 1999, European journal of biochemistry.
[55] G. Kneale,et al. Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site. , 2005, Protein expression and purification.
[56] J. Chang,et al. Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. , 1993, The Journal of biological chemistry.
[57] G. Chaga,et al. Twenty-five years of immobilized metal ion affinity chromatography: past, present and future. , 2001, Journal of biochemical and biophysical methods.
[58] G. Petersen,et al. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. , 2006, Protein expression and purification.
[59] Craig M. Ogata,et al. Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK , 1996, Science.
[60] Bostjan Kobe,et al. Crystal structures of fusion proteins with large‐affinity tags , 2003, Protein science : a publication of the Protein Society.
[61] V. Gaberc-Porekar,et al. Histidines in affinity tags and surface clusters for immobilized metal-ion affinity chromatography of trimeric tumor necrosis factor alpha. , 1999, Journal of chromatography. A.