Results 91 to 100 of about 13,634 (224)

Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10

, 1995
We have recently reported the cloning of a cDNA coding for a stress inducible human chaperonin 10. The protein was shown to possess 100% identity with the bovine homologue and a single amino acid replacement (glycine to serine at position 52) compared to
Gianluca Fossati, Legname, Giuseppe, Gromo, Gianni, Marcucci F, Modena, Daniela, Gianni Gromo, Daniela Modena, Fabrizio Marcucci, Marcucci, Fabrizio, Fossati, G, Monzini N, Monzini, N, Marcucci, F, Modena D., Giuseppe Legname, Nicoletta Monzini, Monzini, Nicoletta, Modena, D., Fossati, Gianluca, Gromo, G, Fossati G, Gromo G   +21 more
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A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus

, 1998
The chaperonins are high-molecular-weight protein complexes having a characteristic double-ring toroidal shape; they are thought to aid the folding of denatured or newly synthesized polypeptides.
LONDEI, Paola, Londei, P., Condò, I, Reinhardt, R, CONDO', IVANO, RUGGERO D., REINHARDT R., Londei, P, Ruggero, D, CONDÒ I.   +9 more
core   +1 more source

Beyond Folding: The Dual Life of Hsp60 in Tissue Homeostasis and Pathophysiology

Applied Biosciences
The heat shock protein 60 (Hsp60) is a highly conserved molecular chaperonin belonging to the chaperone system, a complex network that maintains proteostasis and regulates numerous cellular processes beyond protein folding.
Giuseppa D’Amico, Melania Ionelia Gratie, Giuseppe Vergilio, Francesco Cappello, Alessandra Maria Vitale   +4 more
doaj   +1 more source

Chaperonin 60: Molecular, cellular and structural studies to define its role as an information molecule [PDF]

, 2000
Experimental evidence obtained in this thesis establishes that the purified, recombinant, E. coli chaperonin 60 protein, GroEL, is a potent stimulator of cytokine production by human peripheral blood mononuclear cells (PBMCs) and that this cytokine ...
Khan, Sahar
core  

Effects of metformin on human monocytic THP-1 cells - Implications for type 2 diabetes mellitus

, 2010
Metformin is an anti-hyperglycaemic agent widely prescribed for type 2 diabetes (T2D). Despite decades of clinical use, its exact pharmacological mechanism(s) is yet to be definitively determined.
Tsuei, An-Chi
core  

Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin.

, 2010
Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits.
de Cárcer, G, Valpuesta, JM, Bragado-Nilsson, Elisabeth, Beloso, A, Marina Serna, Mesa, P, Robinson, Carol V, Bragado-Nilsson, E, Carol V Robinson, Montoya, G, Valpuesta, José M, Muñoz, IG, Robinson, CV, Ah Young Park, Serna, Marina, Inés G Muñoz, Malumbres, Marcos, Serna, M, Zhou, M, Montoya, Guillermo, José M Valpuesta, de Cárcer, Guillermo, Malumbres, M, Park, Ah Young, Ana Beloso, Min Zhou, Guillermo Montoya, Guillermo de Cárcer, Hugo Yébenes, Park, AY, Mesa, Pablo, Pablo Mesa, Zhou, Min, Marcos Malumbres, Yébenes, H, Elisabeth Bragado-Nilsson, Yébenes, Hugo, Beloso, Ana, Muñoz, Inés G   +38 more
core   +1 more source

Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states

Nature Communications
Mitochondrial chaperonin Heat Shock Protein 60 kDa (Hsp60) oversees the correct folding of client proteins in cooperation with Hsp10. Hsp60 monomers M first form 7-meric Single rings (S), which then pair into 14-meric Double rings (D) that accommodate ...
Luca Torielli, Federica Guarra, Hao Shao, Jason E. Gestwicki, Stefano A. Serapian, Giorgio Colombo   +5 more
doaj   +1 more source

A Model In Vitro System to Study Heat Shock Protein 60 (HSP60) Expression in Response to Mitochondrial Impairment in Human Cells

, 2013
Heat Shock Proteins (HSPs) are a class of ubiquitously expressed and functionally related proteins found in all living organisms from humans to bacteria.
Hall, Luke
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Equatorial split of holo-chaperonin from Thermus thermophilus by ATP and K+

, 1995
Holo-chaperonin molecule from Thermus thermophilus is a bullet-shaped particle whose cylinder part and round top are composed of two stacked rings of the cpn60 heptamer and a single ring of the cpn10 heptamer, respectively. We found that it splits at the
Hideki Taguchi, Sasabe, Hiroyuki, Hiroyuki Sasabe, Masasuke Yoshida, Ishii, Noriyuki, Taguchi, Hideki, Noriyuki Ishii, Yoshida, Masasuke   +7 more
core   +1 more source

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]

, 1992
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Ostermann, Joachim, Hartl, Franz-Ulrich, Rassow, Joachim, Neupert, Walter, Horwich, Arthur, Horwich, Arthur L., Koll, Hans, Guiard, Bernard   +7 more
core   +1 more source