Experts and Doctors on molecular chaperones in Germany


Locale: Germany
Topic: molecular chaperones

Top Publications

  1. Prip Buus C, Westerman B, Schmitt M, Langer T, Neupert W, Schwarz E. Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Lett. 1996;380:142-6 pubmed
    ..Only the absence of Mdj1p led to enhanced protein aggregation. Thus, a central role in the transient protection against heat stress is attributed to this mitochondrial DnaJ homologue. ..
  2. Blokesch M, Magalon A, Bock A. Interplay between the specific chaperone-like proteins HybG and HypC in maturation of hydrogenases 1, 2, and 3 from Escherichia coli. J Bacteriol. 2001;183:2817-22 pubmed
    ..The results indicate that the three hydrogenase isoenzymes not only are interacting at the functional level but are also interconnected during the maturation process. ..
  3. Schmid M, Simpson D, Sarioglu H, Lottspeich F, Gietl C. The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2001;98:5353-8 pubmed
    ..We propose that ricinosomes accumulate during senescence by programmed cell death and are activated by release of protons from acidic vacuoles. ..
  4. Geissler A, Rassow J, Pfanner N, Voos W. Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins. Mol Cell Biol. 2001;21:7097-104 pubmed
  5. Song H, Mulrooney S, Huber R, Hausinger R. Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation. J Biol Chem. 2001;276:49359-64 pubmed
  6. Multhaup G, Strausak D, Bissig K, Solioz M. Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance. Biochem Biophys Res Commun. 2001;288:172-7 pubmed publisher
  7. Weber M, Beckering C, Marahiel M. Complementation of cold shock proteins by translation initiation factor IF1 in vivo. J Bacteriol. 2001;183:7381-6 pubmed
    ..Two of the possible explanation models are discussed. ..
  8. Becker T, Hartl F, Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol. 2002;158:1277-85 pubmed
    ..We suggest that CD40 is a cochaperone-like receptor mediating the uptake of exogenous Hsp70-peptide complexes by macrophages and dendritic cells. ..
  9. Kubitscheck U, GRUNWALD D, Hoekstra A, Rohleder D, Kues T, Siebrasse J, et al. Nuclear transport of single molecules: dwell times at the nuclear pore complex. J Cell Biol. 2005;168:233-43 pubmed
    ..Together with the known transport rates, our data suggest that nucleocytoplasmic transport occurs via multiple parallel pathways within single NPCs. ..

More Information

Publications234 found, 100 shown here

  1. Simon I, Schaefer M, Reichert J, Stremmel W. Analysis of the human Atox 1 homologue in Wilson patients. World J Gastroenterol. 2008;14:2383-7 pubmed
    ..Based on the data of this study, no major role can be attributed to Atox1 in the pathophysiology or clinical variation of Wilson disease. ..
  2. Steinebrunner I, Landschreiber M, Krause Buchholz U, Teichmann J, Rödel G. HCC1, the Arabidopsis homologue of the yeast mitochondrial copper chaperone SCO1, is essential for embryonic development. J Exp Bot. 2011;62:319-30 pubmed publisher
    ..Growth of the complemented yeast mutant was enhanced by the addition of copper to the medium. The data demonstrate that HCC1 is essential for embryo development in Arabidopsis, possibly due to its role in cytochrome c oxidase assembly. ..
  3. Bracher A, Starling Windhof A, Hartl F, Hayer Hartl M. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat Struct Mol Biol. 2011;18:875-80 pubmed publisher
    ..The RbcL(8)(RbcX(2))(8) structure also suggests that RbcS functions by stabilizing the '60s loop' of RbcL in the catalytically active conformation. ..
  4. Bowman A, Hammond C, Stirling A, Ward R, Shang W, El Mkami H, et al. The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Res. 2014;42:6038-51 pubmed publisher
    ..The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism. ..
  5. Oecal S, Socher E, Uthoff M, Ernst C, Zaucke F, Sticht H, et al. The pH-dependent Client Release from the Collagen-specific Chaperone HSP47 Is Triggered by a Tandem Histidine Pair. J Biol Chem. 2016;291:12612-26 pubmed publisher
    ..This effect is mainly caused by a lower koff at the low pH values. ..
  6. Merlin A, von Ahsen O, Craig E, Dietmeier K, Pfanner N. A mutant form of mitochondrial GrpE suppresses the sorting defect caused by an alteration in the presequence of cytochrome b2. J Mol Biol. 1997;273:1-6 pubmed
  7. Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, et al. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol. 2008;15:641-50 pubmed publisher
    ..ClpB rings are highly unstable, which may facilitate dissociation from trapped substrates during threading. ..
  8. Schweiger R, Müller N, Schmitt M, Soll J, Schwenkert S. AtTPR7 is a chaperone-docking protein of the Sec translocon in Arabidopsis. J Cell Sci. 2012;125:5196-207 pubmed publisher
  9. Kube M, Chernikova T, Al Ramahi Y, Beloqui A, Lopez Cortez N, Guazzaroni M, et al. Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica. Nat Commun. 2013;4:2156 pubmed publisher
    ..Our findings are relevant in the context of microbial cold-adaptation mechanisms and the development of strategies for oil-spill mitigation in cold environments. ..
  10. Knittler M, Dirks S, Haas I. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci U S A. 1995;92:1764-8 pubmed
    ..Our data support the model that, by means of BiP interaction, the ER degradation mechanism has the potential to discriminate between partially and completely folded molecules. ..
  11. Stahl M, Beck J, Nassal M. Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to epsilon RNA binding. J Virol. 2007;81:13354-64 pubmed
  12. Knarr G, Kies U, Bell S, Mayer M, Buchner J. Interaction of the chaperone BiP with an antibody domain: implications for the chaperone cycle. J Mol Biol. 2002;318:611-20 pubmed
    ..However, the accessibility of the BiP-binding site in the non-native protein seems to influence the kinetics of complex formation. ..
  13. Asmus F, Gasser T. Dystonia-plus syndromes. Eur J Neurol. 2010;17 Suppl 1:37-45 pubmed publisher
    ..Recently, a novel form of dystonia-parkinsonism (DYT16) has been found to be linked to mutations in the PRKRA gene, whose relation to basal ganglia disorders is yet unknown . ..
  14. Kumar M, Sourjik V. Physical map and dynamics of the chaperone network in Escherichia coli. Mol Microbiol. 2012;84:736-47 pubmed publisher
    ..Our data suggest that protein folding within cells relies on highly ordered and direct channelling of substrates between chaperone systems and provide a comprehensive view of the underlying interactions and of their dynamics...
  15. Gupta R, Lakshmipathy S, Chang H, Etchells S, Hartl F. Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli. FEBS Lett. 2010;584:3620-4 pubmed publisher
    ..By delaying folding relative to translation, the PPIase domain may increase the propensity of misfolding for certain eukaryotic proteins that rely on a mechanism of co-translational, domain-wise folding. ..
  16. Schlapschy M, Skerra A. Periplasmic chaperones used to enhance functional secretion of proteins in E. coli. Methods Mol Biol. 2011;705:211-24 pubmed publisher
    ..Here, we present a detailed protocol how to use this system for the bacterial secretion of recombinant proteins, including human EGF as a new example, and we give hints on optimization of the expression procedure...
  17. Neuhofer W, Fraek M, X Beck F. Heat shock protein 72, a chaperone abundant in renal papilla, counteracts urea-mediated inhibition of enzymes. Pflugers Arch. 2002;445:67-73 pubmed
    ..Hence, in addition to the trimethylamine osmolytes, HSP72 may participate in counteracting urea-mediated effects on protein function in the renal papilla. ..
  18. Bhat J, Miličić G, Thieulin Pardo G, Bracher A, Maxwell A, Ciniawsky S, et al. Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase. Mol Cell. 2017;67:744-756.e6 pubmed publisher
    ..The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair. ..
  19. Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, et al. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell. 2005;121:1059-69 pubmed
    ..We suggest that this process reflects the evolutionary origin of the IMS from the periplasmic space of the prokaryotic ancestors of mitochondria. ..
  20. Heidrich N, Bauriedl S, Barquist L, Li L, Schoen C, Vogel J. The primary transcriptome of Neisseria meningitidis and its interaction with the RNA chaperone Hfq. Nucleic Acids Res. 2017;45:6147-6167 pubmed publisher
    ..Our genome-wide RNA compendium will allow for a better understanding of meningococcal transcriptome organization and riboregulation with implications for colonization of the human nasopharynx. ..
  21. Knoblauch N, Rudiger S, Schönfeld H, Driessen A, Schneider Mergener J, Bukau B. Substrate specificity of the SecB chaperone. J Biol Chem. 1999;274:34219-25 pubmed
    ..SecB may rather be a general chaperone whose involvement in translocation is mediated by interactions of SecB and signal sequences of SecB-bound preproteins with the translocation apparatus. ..
  22. Padmanabhan N, Fichtner L, Dickmanns A, Ficner R, Schulz J, Braus G. The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress. Mol Biol Cell. 2009;20:68-77 pubmed publisher
    ..Suppression studies with Deltaynm3 led to the discovery of chaperone activity in a nucleolar peptidyl-prolyl cis-trans isomerase, Fpr3, which could partly relieve the heat sensitivity of Deltaynm3. ..
  23. Gautschi M, Mun A, Ross S, Rospert S. A functional chaperone triad on the yeast ribosome. Proc Natl Acad Sci U S A. 2002;99:4209-14 pubmed
    ..The combination of in vitro and in vivo data supports a model in which Ssb1/2p, Ssz1p, and zuotin act in concert on nascent chains while they are being synthesized. ..
  24. Brychzy A, Rein T, Winklhofer K, Hartl F, Young J, Obermann W. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 2003;22:3613-23 pubmed
    ..At normal levels substoichiometric to Hsp90 and Hsp70, this activity optimizes the function of the multichaperone machinery. ..
  25. Sibbing D, Asmus F, Konig I, Tezenas du Montcel S, Vidailhet M, Sangla S, et al. Candidate gene studies in focal dystonia. Neurology. 2003;61:1097-101 pubmed
    ..The authors failed to confirm a previously reported association with a polymorphism in DRD5. No evidence for an involvement of DYT1, DRD5, HLA-DRB, or polymorphisms in the homocysteine pathway in the pathogenesis of F-ITD was found. ..
  26. Sevvana M, Biadene M, Ma Q, Guo C, Soling H, Sheldrick G, et al. Structural elucidation of the PDI-related chaperone Wind with the help of mutants. Acta Crystallogr D Biol Crystallogr. 2006;62:589-94 pubmed
  27. Winnefeld M, Grewenig A, Schnolzer M, Spring H, Knoch T, Gan E, et al. Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest. Exp Cell Res. 2006;312:2500-14 pubmed
  28. Graubner W, Schierhorn A, Brüser T. DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J Biol Chem. 2007;282:7116-24 pubmed
    ..The overall results suggest that SlyD and DnaK are in the set of chaperones that can serve as general Tat signal-binding proteins. DnaK has additional functions that are indispensable for the targeting of CueO. ..
  29. Peisker K, Braun D, Wölfle T, Hentschel J, Funfschilling U, Fischer G, et al. Ribosome-associated complex binds to ribosomes in close proximity of Rpl31 at the exit of the polypeptide tunnel in yeast. Mol Biol Cell. 2008;19:5279-88 pubmed publisher
    ..Rpl31, while not essential for binding of RAC to the ribosome, might be involved in proper function of the chaperone complex. ..
  30. Mayer M, Reinstein J, Buchner J. Modulation of the ATPase cycle of BiP by peptides and proteins. J Mol Biol. 2003;330:137-44 pubmed
    ..We show that, in contrast to smaller peptides, the non-native protein domain decelerates the rate limiting hydrolysis step of the ATPase cycle. ..
  31. Sharma S, Chakraborty K, Müller B, Astola N, Tang Y, Lamb D, et al. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell. 2008;133:142-53 pubmed publisher
    ..Segmental chain release and compaction may be important in avoiding misfolding by proteins that fail to fold efficiently through spontaneous hydrophobic collapse. ..
  32. Lotz G, Lin H, Harst A, Obermann W. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem. 2003;278:17228-35 pubmed
    ..Thus, our results identify a novel type of cofactor involved in the regulation of the molecular chaperone Hsp90. ..
  33. Faou P, Tropschug M. Neurospora crassa CyPBP37: a cytosolic stress protein that is able to replace yeast Thi4p function in the synthesis of vitamin B1. J Mol Biol. 2004;344:1147-57 pubmed publisher
    ..In addition to its function in thiazole synthesis, CyPBP37 is a stress-inducible protein. N.crassa cyclophilin41 can chaperone the folding of CyPBP37, its own binding partner...
  34. Schneider H, Westermann B, Neupert W, Brunner M. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J. 1996;15:5796-803 pubmed
    ..Subsequently, the release of mt-Hsp70 from the polypeptide chain is triggered by Mge1p which promotes release of ADP from mt-Hsp70. Rebinding of ATP to mt-Hsp70 completes the reaction cycle. ..
  35. Clausen T, Southan C, Ehrmann M. The HtrA family of proteases: implications for protein composition and cell fate. Mol Cell. 2002;10:443-55 pubmed
    ..Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate. ..
  36. Grundmann K, Laubis Herrmann U, Bauer I, Dressler D, Vollmer Haase J, Bauer P, et al. Frequency and phenotypic variability of the GAG deletion of the DYT1 gene in an unselected group of patients with dystonia. Arch Neurol. 2003;60:1266-70 pubmed
    ..A priori prediction of the mutation carrier status in dystonic patients and genetic counseling of affected families with respect to the clinical manifestation may prove difficult. ..
  37. Veyel D, Sommer F, Muranaka L, R tgers M, Lemaire S, Schroda M. In vitro characterization of bacterial and chloroplast Hsp70 systems reveals an evolutionary optimization of the co-chaperones for their Hsp70 partner. Biochem J. 2014;460:13-24 pubmed publisher
  38. Sirrenberg C, Bauer M, Guiard B, Neupert W, Brunner M. Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22. Nature. 1996;384:582-5 pubmed
    ..Import of proteins of the AAC family is independent of Tim23, and import of matrix targeting signals containing preproteins is independent of Tim22. ..
  39. Barral J, Broadley S, Schaffar G, Hartl F. Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol. 2004;15:17-29 pubmed
    ..Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies. ..
  40. Blamowska M, Neupert W, Hell K. Biogenesis of the mitochondrial Hsp70 chaperone. J Cell Biol. 2012;199:125-35 pubmed publisher
    ..Binding of an adenine nucleotide triggered release of Hep1 and folding of the intermediate into native mtHsp70. Thus, Hep1 acts as a specialized chaperone mediating the de novo folding of an Hsp70 chaperone. ..
  41. Ma C, Haslbeck M, Babujee L, Jahn O, Reumann S. Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes. Plant Physiol. 2006;141:47-60 pubmed
    ..Thus, plants are exceptional among eukaryotes in employing sHsps in the peroxisome matrix to prevent unspecific aggregation of partially denatured proteins under both physiological and stress conditions. ..
  42. Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 2000;101:199-210 pubmed
    ..The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes. ..
  43. Zirn B, Grundmann K, Huppke P, Puthenparampil J, Wolburg H, Riess O, et al. Novel TOR1A mutation p.Arg288Gln in early-onset dystonia (DYT1). J Neurol Neurosurg Psychiatry. 2008;79:1327-30 pubmed publisher
    ..The sequence change described here may be a novel pathogenic mutation of TOR1A in DYT1. ..
  44. Gebauer M, Zeiner M, Gehring U. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 1997;417:109-13 pubmed
    ..These interacting proteins thus appear to cooperate in affecting the chaperoning activity of hsp70/hsc70. ..
  45. Buchner J. Hsp90 & Co. - a holding for folding. Trends Biochem Sci. 1999;24:136-41 pubmed
  46. Thielmann Y, Weiergräber O, Mohrlüder J, Willbold D. Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. FEBS J. 2009;276:1140-52 pubmed publisher
    ..Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general. ..
  47. Hainzl O, Wegele H, Richter K, Buchner J. Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem. 2004;279:23267-73 pubmed
    ..Taken together, Cns1 is a potent cochaperone of Ssa1. Our findings highlight the importance of the regulation of Hsp70 function in the context of the Hsp90 chaperone cycle. ..
  48. Gebauer M, Zeiner M, Gehring U. Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70. Mol Cell Biol. 1998;18:6238-44 pubmed
    ..Thus, not only do the major domains of hsp70 chaperones communicate with each other, but cofactors interacting with these domains affect each other as well. ..
  49. Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, et al. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 1999;18:6934-49 pubmed
    ..chaperones/heat-shock response/Hsp70/protein denaturation/thermotolerance ..
  50. Andersen O, Yeung C, Vorum H, Wellner M, Andreassen T, Erdmann B, et al. Essential role of the apolipoprotein E receptor-2 in sperm development. J Biol Chem. 2003;278:23989-95 pubmed
  51. Eulalio A, Huntzinger E, Nishihara T, Rehwinkel J, Fauser M, Izaurralde E. Deadenylation is a widespread effect of miRNA regulation. RNA. 2009;15:21-32 pubmed publisher
    ..These results indicate that miRNAs promote mRNA decay by altering mRNP composition and/or conformation, rather than by directly interfering with the binding and function of ribosomal subunits. ..
  52. Hartl F, Hayer Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574-81 pubmed publisher
  53. Haslbeck V, Eckl J, Kaiser C, Papsdorf K, Hessling M, Richter K. Chaperone-interacting TPR proteins in Caenorhabditis elegans. J Mol Biol. 2013;425:2922-39 pubmed publisher
    ..5, did not show any binding to Hsc70 or Hsp90, suggesting that only about 15 of the TPR-domain-containing proteins in C. elegans interact with chaperones, while the many others may have evolved to bind other ligands...
  54. Lenhard T, Reiländer H. Engineering the folding pathway of insect cells: generation of a stably transformed insect cell line showing improved folding of a recombinant membrane protein. Biochem Biophys Res Commun. 1997;238:823-30 pubmed
  55. Dudek J, Volkmer J, Bies C, Guth S, Müller A, Lerner M, et al. A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. EMBO J. 2002;21:2958-67 pubmed
  56. Westhoff B, Chapple J, van der Spuy J, Hohfeld J, Cheetham M. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr Biol. 2005;15:1058-64 pubmed
    ..In this way, HSJ1 isoforms participate in ER-associated degradation (ERAD) and protect neurons against cytotoxic protein aggregation. ..
  57. Küffner R, Rohr A, Schmiede A, Krull C, Schulte U. Involvement of two novel chaperones in the assembly of mitochondrial NADH:Ubiquinone oxidoreductase (complex I). J Mol Biol. 1998;283:409-17 pubmed
    ..These results indicate that the two proteins are novel chaperones specific for complex I membrane arm assembly. ..
  58. Simhadri V, Reiners K, Hansen H, Topolar D, Simhadri V, Nohroudi K, et al. Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function. PLoS ONE. 2008;3:e3377 pubmed publisher
    ..The manipulation of the exosomal regulation may offer a novel strategy to induce tumor immunity or inhibit autoimmune diseases caused by NK cell-activation. ..
  59. Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell. 2005;120:73-84 pubmed
    ..In yeast, this escort pathway guides a transcription factor from its activation in the cytosol to its final degradation and also mediates proteolysis at the endoplasmic reticulum by the ERAD pathway. ..
  60. Groh J, Ribechini E, Stadler D, Schilling T, Lutz M, Martini R. Sialoadhesin promotes neuroinflammation-related disease progression in two mouse models of CLN disease. Glia. 2016;64:792-809 pubmed publisher
    ..Our data also indicate that a rarely described CD8+CD122+ T-cell population can regulate the corresponding diseases. These studies provide insights into CLN pathogenesis and may guide in designing immuno-regulatory treatment strategies. ..
  61. Hofweber R, Horn G, Langmann T, Balbach J, Kremer W, Schmitz G, et al. The influence of cold shock proteins on transcription and translation studied in cell-free model systems. FEBS J. 2005;272:4691-702 pubmed
    ..The data are in line with a hypothesis that CSPs act on bulk protein expression not as RNA chaperones but inhibit their transcription and translation by rather unspecific nucleic acid binding. ..
  62. Arndt V, Daniel C, Nastainczyk W, Alberti S, Hohfeld J. BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol Biol Cell. 2005;16:5891-900 pubmed
    ..The presented data therefore establish multiple mechanisms to control the destructive activity of the CHIP ubiquitin ligase in human cells. ..
  63. Sell K, Storch K, Hahn G, Lee Kirsch M, Ramantani G, Jackson S, et al. Variable clinical course in acute necrotizing encephalopathy and identification of a novel RANBP2 mutation. Brain Dev. 2016;38:777-80 pubmed publisher
    ..Clinical and radiological features are presented and differential diagnoses are discussed. This report adds to the current knowledge of the phenotype in ANE, caused by mutations in RANBP2 gene. ..
  64. Behrens S. Periplasmic chaperones--new structural and functional insights. Structure. 2002;10:1469-71 pubmed
    ..New intriguing functional insights are provided by the solved crystal structure of the periplasmic chaperone SurA. ..
  65. Esser C, Scheffner M, Hohfeld J. The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J Biol Chem. 2005;280:27443-8 pubmed
    ..Our data reveal that mutant and wild-type p53 transiently associate with molecular chaperones and can be diverted onto a degradation pathway through this association. ..
  66. Schlapschy M, Grimm S, Skerra A. A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli. Protein Eng Des Sel. 2006;19:385-90 pubmed
    ..Hence, pTUM4 represents a novel helper vector which complements existing cytosolic chaperone coexpression plasmids and should be useful for the functional secretion of various recombinant proteins with hampered folding efficiency. ..
  67. Schaffar G, Breuer P, Boteva R, Behrends C, Tzvetkov N, Strippel N, et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell. 2004;15:95-105 pubmed
    ..These results outline a molecular mechanism of cellular toxicity in polyQ disease and can explain the beneficial effects of molecular chaperones. ..
  68. Falk S, Sinning I. cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins. J Biol Chem. 2010;285:21655-61 pubmed publisher
    ..Taken together, we define cpSRP43 as a highly specific chaperone for LHCPs in addition to its established function as a targeting factor for this family of membrane proteins. ..
  69. Tripp J, Hahn A, Koenig P, Flinner N, Bublak D, Brouwer E, et al. Structure and conservation of the periplasmic targeting factor Tic22 protein from plants and cyanobacteria. J Biol Chem. 2012;287:24164-73 pubmed publisher
    ..The three-dimensional structure allows the definition of conserved hydrophobic pockets comparable with those of ClpS or BamB. The results presented suggest a function of Tic22 in outer membrane biogenesis. ..
  70. Ramos P, Höckendorff J, Johnson E, Varshavsky A, Dohmen R. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell. 1998;92:489-99 pubmed
    ..We also show that the propeptide of the Pre2p/Doa3p beta subunit is required for Ump1p's function in proteasome maturation. ..
  71. Strub A, Rottgers K, Voos W. The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria. EMBO J. 2002;21:2626-35 pubmed
    ..Hence, the determination of a crucial Hsp70 function via the peptide-binding domain suggests a new regulatory principle for Hsp70 domain cooperation. ..
  72. Rumpf S, Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell. 2006;21:261-9 pubmed
    ..We propose that the balance between the distinct substrate-processing cofactors may determine whether a substrate is multiubiquitylated and routed to the proteasome for degradation or deubiquitylated and/or released for other purposes. ..
  73. Kettern N, Dreiseidler M, Tawo R, Hohfeld J. Chaperone-assisted degradation: multiple paths to destruction. Biol Chem. 2010;391:481-9 pubmed publisher
    ..Here, we discuss recent insights into molecular mechanisms underlying chaperone-assisted degradation in mammalian cells and highlight its biomedical relevance. ..
  74. Hartl F, Bracher A, Hayer Hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 2011;475:324-32 pubmed publisher
    ..Interventions in these and numerous other pathological states may spring from a detailed understanding of the pathways underlying proteome maintenance. ..
  75. Schlapschy M, Dommel M, Hadian K, Fogarasi M, Korndörfer I, Skerra A. The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Biol Chem. 2004;385:137-43 pubmed
    ..Using the recombinant protein equipped with the Strep-tag II at its N-terminus, suitable crystallization conditions for Skp were found. A first data set was collected to 2.60 A resolution. ..
  76. Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid F. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry. 2006;45:20-33 pubmed
    ..The SlyD proteins are also well suited for biotechnological applications. As fusion partners they facilitate the refolding and increase the solubility of aggregation-prone proteins such as the gp41 ectodomain fragment of HIV-1. ..
  77. Berger F, Berkholz J, Breustedt T, Ploen D, Munz B. Skeletal muscle-specific variant of nascent polypeptide associated complex alpha (skNAC): implications for a specific role in mammalian myoblast differentiation. Eur J Cell Biol. 2012;91:150-5 pubmed publisher
    ..Taken together, our data suggest that skNAC regulates specific aspects of myogenesis. ..
  78. Prusty A, Meduri R, Prusty B, Vanselow J, Schlosser A, Fischer U. Impaired spliceosomal UsnRNP assembly leads to Sm mRNA down-regulation and Sm protein degradation. J Cell Biol. 2017;216:2391-2407 pubmed publisher
    ..Our studies identify an elaborate safeguarding system that prevents individual Sm proteins from aggregating, contributing to cellular UsnRNP homeostasis. ..
  79. Groll M, Bochtler M, Brandstetter H, Clausen T, Huber R. Molecular machines for protein degradation. Chembiochem. 2005;6:222-56 pubmed
    ..Some of these compounds may find therapeutic applications in contemporary medicine. ..
  80. Cario E, Golenbock D, Visintin A, Runzi M, Gerken G, Podolsky D. Trypsin-sensitive modulation of intestinal epithelial MD-2 as mechanism of lipopolysaccharide tolerance. J Immunol. 2006;176:4258-66 pubmed
  81. Jakob R, Zoldak G, Aumüller T, Schmid F. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc Natl Acad Sci U S A. 2009;106:20282-7 pubmed publisher
    ..The catalytic performance of these folding enzymes is thus determined by generic substrate recognition at the chaperone domain and efficient transfer to the active site in the prolyl isomerase domain. ..
  82. Bacher G, Pool M, Dobberstein B. The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor. J Cell Biol. 1999;146:723-30 pubmed
    ..Interaction between SRP and SRalpha then leads to release of the signal sequence from SRP and insertion into the translocon. GTP hydrolysis then results in dissociation of SR from the ribosome, and SRP from the SR. ..
  83. Hullmann J, Patzer S, Römer C, Hantke K, Braun V. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol Microbiol. 2008;69:926-37 pubmed publisher
    ..Colicin M is a suitable tool for the isolation of FkpA mutants used to elucidate the functions of the FkpA N- and C-domains. ..
  84. Welz D, Braun V. Ferric citrate transport of Escherichia coli: functional regions of the FecR transmembrane regulatory protein. J Bacteriol. 1998;180:2387-94 pubmed
  85. Klein U, Haindl M, Nigg E, Muller S. RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Mol Biol Cell. 2009;20:410-8 pubmed publisher
    ..These data thus delineate a mitotic SUMO2/3 conjugation-deconjugation cycle of Borealin and further assign a regulatory function of RanBP2 and SENP3 in the mitotic SUMO pathway. ..
  86. Sikor M, Mapa K, von Voithenberg L, Mokranjac D, Lamb D. Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET. EMBO J. 2013;32:1639-49 pubmed publisher
    ..These results indicate that the conformational cycle of Ssc1 is more elaborate than previously thought and provide insight into how the Hsp70s can perform a wide variety of functions. ..
  87. Schopf F, Biebl M, Buchner J. The HSP90 chaperone machinery. Nat Rev Mol Cell Biol. 2017;18:345-360 pubmed publisher
    ..Owing to the importance of HSP90 in the regulation of many cellular proteins, it has become a promising drug target for the treatment of several diseases, which include cancer and diseases associated with protein misfolding. ..
  88. Scholz C, Schaarschmidt P, Engel A, Andres H, Schmitt U, Faatz E, et al. Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules. J Mol Biol. 2005;345:1229-41 pubmed
    ..Covalent fusions with SlyD or FkpA might be valuable generic tools for the solubilization and activation of aggregation-prone proteins. ..
  89. Huppke P, Brendel C, Korenke G, Marquardt I, Donsante A, Yi L, et al. Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase. Hum Mutat. 2012;33:1207-15 pubmed publisher
    ..As a result, this mutation causes reduced SOD1 activity and may impair other mechanisms important for normal Cu homeostasis. CCS-Arg163Trp represents the primary example of a human mutation in a gene coding for a Cu chaperone. ..
  90. Muhlenhoff U, Gerber J, Richhardt N, Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 2003;22:4815-25 pubmed
    ..We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps. ..
  91. Patel G, Behrens Kneip S, Holst O, Kleinschmidt J. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry. 2009;48:10235-45 pubmed publisher
    ..The faster phase dominated when the experimental conditions favored the less compact form of aqueous OmpA...
  92. Kumar S, Reusch H, Ladilov Y. Acidic pre-conditioning suppresses apoptosis and increases expression of Bcl-xL in coronary endothelial cells under simulated ischaemia. J Cell Mol Med. 2008;12:1584-92 pubmed
    ..Over-expression of the anti apoptotic protein Bcl-xL is responsible for the increased resistance to apoptosis during ischaemic insult. ..