Results 171 to 180 of about 27,779 (210)

Preparation and characterization of polyclonal antibodies against human chaperonin 10

Cell Stress & Chaperones, 2000
Early pregnancy factor (EPF) has been identified as an extracellular homologue of chaperonin 10 (Cpn10), a heat shock protein that functions within the cell as a molecular chaperone. Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10 molecule and their application to specific protein ...
Somodevilla-Torres, Maria J., Hillyard, Narelle C., Morton, Halle, Alewood, Dianne, Halliday, Judy A., Alewood, Paul F., Vesey, David A., Walsh, Michael D., Cavanagh, Alice C.   +8 more
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The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter

Gene, 1997
Chaperonins are a class of stress-inducible molecular chaperones involved in protein folding. We report the cloning, sequencing and characterisation of the rat mitochondrial chaperonin 60 and chaperonin 10 genes. The two genes are arranged in a head-to-head configuration and together comprise 14 kb and contain 14 introns.
Ryan, Michael T., Herd, Susanna M., Sberna, Gian, Samuel, Melanie M., Hoogenraad, Nicholas J., Hoj, Peter Bordier   +5 more
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Structure ofMycobacterium tuberculosischaperonin-10 at 3.5 Å resolution

Acta Crystallographica Section D Biological Crystallography, 2002
Chaperonin-60 (cpn60) and chaperonin-10 (cpn10) are essential proteins involved in ATP-dependent folding of several intracellular proteins in the bacterial cell. Folding of the nascent substrate polypeptide takes place in the large central cavity formed by each ring of the tetradecameric cpn60. This large cavity is closed upon capping by the heptameric
Bhupesh, Taneja, Shekhar C, Mande
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Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae

Science, 1996
Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a ...
S C, Mande, V, Mehra, B R, Bloom, W G, Hol   +3 more
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Macromolecular Crowding Extended to a Heptameric System: The Co-chaperonin Protein 10

Biochemistry, 2011
Experiments on monomeric proteins have shown that macromolecular crowding can stabilize toward heat perturbation and also modulate native-state structure. To assess the effects of macromolecular crowding on unfolding of an oligomeric protein, we here tested the effects of the synthetic crowding agent Ficoll 70 on human cpn10 (GroES in E.
Ximena, Aguilar, Christoph, F Weise, Tobias, Sparrman, Magnus, Wolf-Watz, Pernilla, Wittung-Stafshede   +4 more
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The Mycobacterium tuberculosis chaperonin 10 monomer exhibits structural plasticity

Biopolymers, 2004
AbstractThe conditions which favor dissociation of oligomeric Mycobacterium tuberculosis chaperonin 10 and the solution structure of the monomer were studied by analytical ultracentrifugation, size exclusion chromatography, fluorescence, and circular dichroism spectroscopies.
Gianluca, Fossati, Pietro, Cremonesi, Gaetano, Izzo, Emanuele, Rizzi, Giovanni, Sandrone, Stephen, Harding, Neil, Errington, Christopher, Walters, Brian, Henderson, Michael M, Roberts, Anthony R M, Coates, Paolo, Mascagni   +11 more
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Early pregnancy factor: An extracellular chaperonin 10 homologue

Immunology & Cell Biology, 1998
Early pregnancy factor (EPF) has been identified as a homologue of chaperonin 10 (cpn10) with immunosuppressive and growth factor properties. As a homologue of cpn10, it belongs to the heat shock family of proteins (hsp) but, unlike other members of this family, EPF is detected extracellularly.
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Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1994
A full-length cDNA clone encoding chaperonin 10 (cpn10) from a HeLa cell cDNA library was isolated. The cDNA is 538 bp in length, contains an ATG codon and a putative polyadenylation signal, and specifies a protein of 102 amino acids. Immunoprecipitation experiment showed that this human cpn10 has an apparent molecular mass of 11 kDa in sodium ...
J J, Chen, D J, McNealy, S, Dalal, E J, Androphy   +3 more
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Molecular Cloning, Expression, and Characterization of Chaperonin-60 and Chaperonin-10 from a Thermophilic Bacterium, Thermus thermophilus HB81

The Journal of Biochemistry, 1995
The gene coding a chaperonin from a thermophilic bacterium, Thermus thermophilus HB8, was cloned and sequenced. The operon structure was the same as those of other bacterial chaperonins and the deduced amino acid sequences of both subunits were highly homologous to those of other chaperonins. The cloned genes of chaperonin subunits, chaperonin-10 (T.th
Kei Amada, Masafumi Yohda, Masafumi Odaka, Isao Endo, Noriyuki Ishii, HIDEKI TAGUCHI, MASASUKE YOSHIDA   +6 more
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Occurrence of Chaperonin 60 and Chaperonin 10 in primary and secondary bacterial symbionts of aphids: Implications for the evolution of an endosymbiotic system in aphids

Journal of Molecular Evolution, 1993
All aphids harbor symbiotrophic prokaryotes ("primary symbionts") in a specialized-abdominal cell, the bacteriocyte. Chaperonin 60 (Cpn60, symbionin) and chaperonin 10 (Cpn10), which are high and low molecular weight heatshock proteins, were sought in tissues of more than 60 aphid species.
T, Fukatsu, H, Ishikawa
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