The N-Terminal Domain of Aliivibrio fischeri LuxR Is a Target of the GroEL ChaperoninMANUKHOV, Ilya V; MELKINA, Ol'ga E; GORYANIN, Ignatii I et al.Journal of bacteriology. 2010, Vol 192, Num 20, pp 5549-5551, issn 0021-9193, 3 p.Article

A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperoninYIJIE GAO; MELKI, R; WALDEN, P. D et al.The Journal of cell biology. 1994, Vol 125, Num 5, pp 989-996, issn 0021-9525Article

Evolutionary relationships among eubacterial groups as inferred from GroEL (chaperonin) sequence comparisonsVIALE, A. M; ARAKAKI, A. K; SONCINI, F. C et al.International journal of systematic bacteriology. 1994, Vol 44, Num 3, pp 527-533, issn 0020-7713Article

Functional consequences of single:double ring transitions in chaperonins: life in the coldFERRER, Manuel; LÜNSDORF, Heinrich; CHERNIKOVA, Tatyana N et al.Molecular microbiology (Print). 2004, Vol 53, Num 1, pp 167-182, issn 0950-382X, 16 p.Article

Differential expression of the multiple chaperonins of Mycobacterium smegmatisRAO, Tara; LUND, Peter A.FEMS microbiology letters. 2010, Vol 310, Num 1, pp 24-31, issn 0378-1097, 8 p.Article

A more precise characterization of chaperonin substratesRAINERI, Emanuele; RIBECA, Paolo; SERRANO, Luis et al.Bioinformatics (Oxford. Print). 2010, Vol 26, Num 14, pp 1685-1689, issn 1367-4803, 5 p.Article

Expression and Functional Characterization of the First Bacteriophage-Encoded ChaperoninKUROCHKINA, Lidia P; SEMENYUK, Pavel I; ORLOV, Victor N et al.Journal of virology. 2012, Vol 86, Num 18, pp 10103-10111, issn 0022-538X, 9 p.Article

The htpAB operon of Legionella pneumophila cannot be deleted in the presence of the groE chaperonin operon of Escherichia coliNASRALLAH, Gheyath K; GAGNON, Elizabeth; ORTON, Dennis J et al.Canadian journal of microbiology. 2011, Vol 57, Num 11, pp 943-952, issn 0008-4166, 10 p.Article

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondriaHÖHFELD, J; HARTL, F. U.The Journal of cell biology. 1994, Vol 126, Num 2, pp 305-315, issn 0021-9525Article

Distinct mechanisms regulate expression of the two major groEL homologues in Rhizobium leguminosarumGOULD, Phillip; MAGUIRE, Maria; LUND, Peter A et al.Archives of microbiology. 2007, Vol 187, Num 1, pp 1-14, issn 0302-8933, 14 p.Article

GroEL-like protein complex of thermophilic bacterium Thermus aquaticusMIKULIK, K; BENADA, O.Biochemical and biophysical research communications (Print). 1993, Vol 197, Num 2, pp 716-721, issn 0006-291XArticle

Residues in chaperonin GroEL required for polypeptide binding and releaseFENTON, W. A; KASHI, Y; FURTAK, K et al.Nature (London). 1994, Vol 371, Num 6498, pp 614-619, issn 0028-0836Article

Multiple chaperonins in bacteria-whyso many?LUND, Peter A.FEMS microbiology reviews. 2009, Vol 33, Num 4, pp 785-800, issn 0168-6445, 16 p.Article

Heat shock promoter of thermophilic chaperonin operonOHTA, T; HONDA, K; SAITO, K et al.Biochemical and biophysical research communications (Print). 1993, Vol 191, Num 2, pp 550-557, issn 0006-291XArticle

Interactions between a luteovirus and the GroEL chaperonin protein of the symbiotic bacterium Buchnera aphidicola of aphidsBOUVAINE, Sophie; BOONHAM, Neil; DOUGLAS, Angela E et al.Journal of general virology. 2011, Vol 92, pp 1467-1474, issn 0022-1317, 8 p., 6Article

Kinetic analysis of interactions between archaeal prefoldin and chaperoninZAKO, Tamotsu; FUNATSU, Takashi; YOHDA, Masafumi et al.Recent research developments in biophysics vol. 3 - 2004 Part II. Recent research developments in biophysics. 2004, pp 475-483, isbn 81-7895-130-4, 9 p.Book Chapter

The rosettazyme: A synthetic cellulosomeMITSUZAWA, Shigenobu; KAGAWA, Hiromi; YIFEN LI et al.Journal of biotechnology. 2009, Vol 143, Num 2, pp 139-144, issn 0168-1656, 6 p.Article

Chaperonin-mediated protein folding : GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavityLANGER, T; PFEIFER, G; MARTIN, J et al.EMBO journal (Print). 1992, Vol 11, Num 13, pp 4757-4765, issn 0261-4189Article

The unfolding story of the chaperoninsCOATES, A. R. M; HENDERSON, B; MASCAGNI, P et al.Biotechnology & genetic engineering reviews. 1999, Vol 16, pp 393-405, issn 0264-8725Article

Cooperativity of α- and β-Subunits of Group II Chaperonin from the Hyperthermophilic Archaeum Aeropyrum pernix KlKIM, Jeong-Hwan; LEE, Jin-Woo; SHIN, Eun-Jung et al.Journal of microbiology and biotechnology. 2011, Vol 21, Num 2, pp 212-217, issn 1017-7825, 6 p.Article

Predicting relatedness of bacterial genomes using the chaperonin-60 universal target (cpn60 UT): Application to Thermoanaerobacrer speciesVERBEKE, Tobin J; SPARLING, Richard; HILL, Janet E et al.Systematic and applied microbiology (Print). 2011, Vol 34, Num 3, pp 171-179, issn 0723-2020, 9 p.Article

Antigenic group II chaperonin in Methanobrevibacter oralis may cross-react with human chaperonin CCTYAMABE, K; MAEDA, H; KOKEGUCHI, S et al.Molecular oral microbiology (Print). 2010, Vol 25, Num 2, pp 112-122, issn 2041-1006, 11 p.Article

Comparative analysis of the protein folding activities of two chaperonin subunits of Thermococcus strain KS-1 : the effects of beryllium fluorideYOSHIDA, Takao; IIZUKA, Ryo; ITAMI, Keisuke et al.Extremophiles (Tokyo. Print). 2007, Vol 11, Num 2, pp 225-235, issn 1431-0651, 11 p.Article

Streptococcus iniae, a human and animal pathogen : Specific identification by the chaperonin 60 gene identification methodSWEE HAN GOH; DRIEDGER, D; SMITH, J. A et al.Journal of clinical microbiology (Print). 1998, Vol 36, Num 7, pp 2164-2166, issn 0095-1137Article

Asymmetrical interaction of GroEL and GroES in the ATPase cycle to assisted protein foldingHAYER-HARTL, M. K; MARTIN, J; HARTI, F. U et al.Science (Washington, D.C.). 1995, Vol 269, Num 5225, pp 836-841, issn 0036-8075Article