Results 121 to 130 of about 16,706 (173)

Cation-Mediated Interplay of Loops in Chaperonin-10

Journal of Biomolecular Structure and Dynamics, 2006
The ubiquitously occurring chaperonins consist of a large tetradecameric Chaperonin-60, forming a cylindrical assembly, and a smaller heptameric Chaperonin-10. For a functional protein folding cycle, Chaperonin-10 caps the cylindrical Chaperonin-60 from one end forming an asymmetric complex.
Swetha, Vijayakrishnan, Rohini, Qamra, Chandra S, Verma, Ranjan, Sen, Shekhar C, Mande   +4 more
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Identification and cloning of human chaperonin 10 homologue

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1994
We have identified a heat-shock-inducible 10 kDa protein in the human hepatoma cell line HepG2. The total RNA extracted from the heat-shocked cells was amplified by reverse transcription PCR (polymerase chain reaction) using 21 5' and 18 3' oligonucleotides of rat cpn10 (chaperonin10) cDNA as primers.
Monzini N, Legname, Giuseppe, Marcucci F, Gromo G, Modena D.   +4 more
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Overproduction and purification of Mycobacterium tuberculosis chaperonin 10

Gene, 1994
The overexpression of the Mycobacterium tuberculosis chaperonin 10 (Cpn10)-encoding gene was accomplished using baculovirus expression vectors. The product was immunoreactive with a Cpn10 monoclonal antibody (mAb) and had an electrophoretic mobility identical to authentic Cpn10. The baculovirus system was most successful in terms of reaching nearly the
D, Atkins, H, al-Ghusein, C, Prehaud, A R, Coates   +3 more
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Purification and characterization of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brockii

European Journal of Biochemistry, 1994
Chaperonin 60 and chaperonin 10 (GroEL and GroES homologues, respectively) have been isolated from extracts of the anaerobic thermophile Thermoanaerobacter brockii. A simple and rapid purification for chaperonin 60 made use of hydrophobic and anion‐exchange chromatographies, and could be readily scaled up; approximately 2 mg pure chaperonin 60 was ...
Truscott, KN, Hoj, PB, Scopes, RK
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Arabidopsis Chloroplast Chaperonin 10 Is a Calmodulin-Binding Protein

Biochemical and Biophysical Research Communications, 2000
Calcium regulates diverse cellular activities in plants through the action of calmodulin (CaM). By using (35)S-labeled CaM to screen an Arabidopsis seedling cDNA expression library, a cDNA designated as AtCh-CPN10 (Arabidopsis thaliana chloroplast chaperonin 10) was cloned.
T, Yang, B W, Poovaiah
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Purification and characterization of chaperonin 10 from Chromatium vinosum

Archives of Biochemistry and Biophysics, 1992
Chromatium vinosum contains a polypeptide that is functionally and structurally similar to the Escherichia coli chaperonin 10. The protein has been purified to homogeneity by sucrose density gradient centrifugation followed by gel filtration using a Bio-Gel A-1.5 m column.
J A, Torres-Ruiz, B A, McFadden
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The Human Early Pregnancy Factor/Chaperonin 10 Gene Family

Biochemical and Molecular Medicine, 1996
cDNA clones corresponding to the sequence for human early pregnancy factor were isolated from a human melanoma library and hybridized to DNA digested with four restriction enzymes obtained from twelve different subjects. Up to 20 cross hybridizing bands were observed.
Summers, K. M., Murphy, R. M., Webb, G. C., Peters, G. B., Morton, H., Cassady, A. I., Cavanagh, A. C.   +6 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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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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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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