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Science (New York, N.Y.)|January 26, 2002
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosinJose M Barral, Alex H Hutagalung, Achim Brinker, et al.The EMBO Journal|February 21, 2009
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3Martin Gamerdinger, Parvana Hajieva, A Murat Kaya, et al.Nature Structural & Molecular Biology|August 8, 2025
Structural analyses define the molecular basis of clusterin chaperone functionPatricia Yuste-Checa, Alonso I Carvajal, Chenchen Mi, et al.Proceedings of the National Academy of Sciences of the United States of America|December 1, 2012
Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCTFlorian Rüßmann, Markus J Stemp, Leonie Mönkemeyer, et al.Nature|November 4, 2011
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activaseOliver Mueller-Cajar, Mathias Stotz, Petra Wendler, et al.EMBO Reports|January 17, 2004
In vivo analysis of the overlapping functions of DnaK and trigger factorPierre Genevaux, France Keppel, Françoise Schwager, et al.Nature Chemical Biology|January 7, 2015
Opposing effects of folding and assembly chaperones on evolvability of RubiscoPaulo Durão, Harald Aigner, Péter Nagy, et al.The Journal of Biological Chemistry|April 21, 2012
Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexesYi-Chin C Tsai, Oliver Mueller-Cajar, Sandra Saschenbrecker, et al.The Journal of Biological Chemistry|November 6, 2014
Role of small subunit in mediating assembly of red-type form I RubiscoJidnyasa Joshi, Oliver Mueller-Cajar, Yi-Chin C Tsai, et al.Journal of Molecular Biology|April 28, 2015
Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES ComplexesShubhasis Haldar, Amit J Gupta, Xiao Yan, et al.Pageof 21