Geltinger F, et al. (2020) The transfer of specific mitochondrial lipids and proteins to lipid droplets contributes to proteostasis upon stress and aging in the eukaryotic model system Saccharomyces cerevisiae. Geroscience 42(1):19-38 PMID:31676965
Rehn A, et al. (2020) A methylated lysine is a switch point for conformational communication in the chaperone Hsp90. Nat Commun 11(1):1219 PMID:32139682
Sima S, et al. (2019) Genome-wide analysis of yeast expression data based on a priori generated co-regulation cliques. Microb Cell 6(3):160-176 PMID:30854393
Papsdorf K, et al. (2016) Construction and evaluation of yeast expression networks by database-guided predictions. Microb Cell 3(6):236-247 PMID:28357360
Zierer BK, et al. (2016) Importance of cycle timing for the function of the molecular chaperone Hsp90. Nat Struct Mol Biol 23(11):1020-1028 PMID:27723736
Miller SB, et al. (2015) Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. EMBO J 34(6):778-97 PMID:25672362
Eckl JM, et al. (2014) Nematode Sgt1-homologue D1054.3 binds open and closed conformations of Hsp90 via distinct binding sites. Biochemistry 53(15):2505-14 PMID:24660900
Jahn M, et al. (2014) The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. Proc Natl Acad Sci U S A 111(50):17881-6 PMID:25468961
Rinnerthaler M, et al. (2013) Mmi1, the yeast homologue of mammalian TCTP, associates with stress granules in heat-shocked cells and modulates proteasome activity. PLoS One 8(10):e77791 PMID:24204967
Hagn F, et al. (2011) Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nat Struct Mol Biol 18(10):1086-93 PMID:21892170
Li J, et al. (2011) Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol 18(1):61-6 PMID:21170051
Hessling M, et al. (2009) Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol 16(3):287-93 PMID:19234467
Heuck A, et al. (2007) Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes. Proc Natl Acad Sci U S A 104(50):19778-83 PMID:18056806
Pachler K, et al. (2004) Functional interaction in establishment of ribosomal integrity between small subunit protein rpS6 and translational regulator rpL10/Grc5p. FEMS Yeast Res 5(3):271-80 PMID:15556089
Richter K, et al. (2004) The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol 342(5):1403-13 PMID:15364569
Stromer T, et al. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279(12):11222-8 PMID:14722093
Richter K, et al. (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J Biol Chem 278(12):10328-33 PMID:12525481
Mayr C, et al. (2000) Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J Biol Chem 275(44):34140-6 PMID:10942767
Weikl T, et al. (2000) C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. J Mol Biol 303(4):583-92 PMID:11054293
Schüller HJ, et al. (1995) DNA binding site of the yeast heteromeric Ino2p/Ino4p basic helix-loop-helix transcription factor: structural requirements as defined by saturation mutagenesis. FEBS Lett 370(1-2):149-52 PMID:7649294
Richter K, et al. (1980) The effect of delta-aminolevulinate on catalase T-messenger RNA levels in delta-aminolevulinate synthase-defective mutants of Saccharomyces cerevisiae. J Biol Chem 255(17):8019-22 PMID:6997287