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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexesIdentification of a tissue-selective heat shock response regulatory networkStaphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activationThe Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONSThe architecture of functional modules in the Hsp90 co-chaperone Sti1/HopReversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX AssociationMixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.Cns1 is an activator of the Ssa1 ATPase activity.Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle.The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90Axin cancer mutants form nanoaggregates to rewire the Wnt signaling networkSelective activators of protein phosphatase 5 target the auto-inhibitory mechanism.Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defectsEnergetics by NMR: site-specific binding in a positively cooperative systemDownregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegansThe balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.The Hsp90 chaperone machinery.A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.daf-41/p23: A Small Protein Heating Up Lifespan RegulationMonomeric myosin V uses two binding regions for the assembly of stable translocation complexes.A Grp on the Hsp90 mechanism.The heat shock response: life on the verge of death.Hsp90 in non-mammalian metazoan model systems.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.Construction and evaluation of yeast expression networks by database-guided predictionsA network of genes connects polyglutamine toxicity to ploidy control in yeastHsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization.Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin.Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.The charged linker region is an important regulator of Hsp90 function.Nematode Sgt1-homologue D1054.3 binds open and closed conformations of Hsp90 via distinct binding sites.
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description
researcher ORCID ID = 0000-0002-8952-9642
@en
name
Klaus Richter
@ast
Klaus Richter
@en
Klaus Richter
@es
Klaus Richter
@nl
type
label
Klaus Richter
@ast
Klaus Richter
@en
Klaus Richter
@es
Klaus Richter
@nl
prefLabel
Klaus Richter
@ast
Klaus Richter
@en
Klaus Richter
@es
Klaus Richter
@nl
P21
P31
P496
0000-0002-8952-9642