In the original publication of the article, under the "Acknowledgement" section, the Grant No. 31611011097 should read as No. 31661143021.
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Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.
Annu Rev Biophys
May 2022
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA; email:
Molecular chaperones are the guardians of the proteome inside the cell. Chaperones recognize and bind unfolded or misfolded substrates, thereby preventing further aggregation; promoting correct protein folding; and, in some instances, even disaggregating already formed aggregates. Chaperones perform their function by means of an array of weak protein-protein interactions that take place over a wide range of timescales and are therefore invisible to structural techniques dependent upon the availability of highly homogeneous samples.
View Article and Find Full Text PDFCorrection to: Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay.
Biotechnol Lett
April 2020
State Key Laboratory of Bioreactor Engineering, Shanghai Collaborative Innovation Center for Biomanufacturing (SCICB), East China University of Science and Technology, 130 Meilong Rd, Shanghai, 200237, China.
In the original publication of the article, under the "Acknowledgement" section, the Grant No. 31611011097 should read as No. 31661143021.
View Article and Find Full Text PDFCombination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB.
J Biol Chem
December 2010
Department of Cellular Microbiology, Max-Planck-Institute for Infection Biology, 10117 Berlin, Germany.
Type III secretion systems (TTSSs) utilized by enteropathogenic bacteria require the presence of small, acidic virulence-associated chaperones for effective host cell infection. We adopted a combination of biochemical and cellular techniques to define the chaperone binding domains (CBDs) in the translocators IpaB and IpaC associated with the chaperone IpgC from Shigella flexneri. We identified a novel CBD in IpaB and furthermore precisely mapped the boundaries of the CBDs in both translocator proteins.
View Article and Find Full Text PDFMunc18-1 stabilizes syntaxin 1, but is not essential for syntaxin 1 targeting and SNARE complex formation.
J Neurochem
June 2005
Department of Functional Genomics, Center for Neurogenomics and Cognitive Research, Vrije Universiteit Amsterdam, Amsterdam, Netherlands.
Munc18-1, a member of the Sec1/Munc18 (SM) protein family, is essential for synaptic vesicle exocytosis. Munc18-1 binds tightly to the SNARE protein syntaxin 1, but the physiological significance and functional role of this interaction remain unclear. Here we show that syntaxin 1 levels are reduced by 70% in munc18-1 knockout mice.
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