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• W1693641788 abstract "Together with other molecular chaperones, small heat shock proteins are key components of the protein quality control system, which is comprised of several hundred proteins and acts to maintain proteome homeostasis in the cell. Small heat shock proteins bind unfolding proteins at an early stage, to prevent these from further unfolding and aggregating. Partially unfolded proteins are being held in a refolding competent state, to be refolded by other chaperones or degraded by the degradation machinery. In the stress response, small heat shock proteins are among the most highly upregulated, preparing the cell to absorb large quantities of partially unfolded proteins. In this way, they form the first line of defence against the threat of protein aggregation under stress conditions. The polydispersity and dynamics of the large small heat shock protein oligomers have complicated their structural and functional characterization. In particular, the molecular mechanism of substrate protein protection remains poorly understood.The work described in this thesis aims to characterize the molecular interactions between the plant small heat shock protein Hsp21 and model substrate proteins by crosslinking mass spectrometry. The model substrate proteins citrate synthase and malate dehydrogenase, both especially vulnerable to temperature-induced aggregation, were protected from aggregation by Hsp21 and therefore used to investigate the Hsp21-substrate interactions that confer protection. To be able to study the transient Hsp21-substrate interaction by crosslinking mass spectrometry, a workflow was developed based on isotope-labelled lysine-specific crosslinking, nano-LC MALDI-TOF/TOF mass spectrometry, and data analysis with the specialized software FINDX. During the development of this workflow, interactions within Hsp21 itself were characterized as a way to evaluate the method and to learn more about the conformation of Hsp21 in absence of substrate. The interpretation of the identified Hsp21-Hsp21 crosslinks required structural information on the Hsp21 oligomer, which was obtained by single particle negative stain electron microscopy. The combination of these data with native mass spectrometry and homology modelling, led to a structure model of the Hsp21 dodecamer. The in-depth analysis of Hsp21-Hsp21 crosslinks provided a framework for further application of the crosslinking mass spectrometry workflow to the Hsp21-substrate interactions. Finally, Hsp21-substrate crosslinks were identified that support the view that unfolding substrate proteins interact with the intrinsically disordered N-terminal region of the small heat shock protein Hsp21." @default.
• W1693641788 created "2016-06-24" @default.
• W1693641788 creator A5016651317 @default.
• W1693641788 date "2012-01-01" @default.
• W1693641788 modified "2023-09-25" @default.
• W1693641788 title "Exploring small heat shock protein chaperones by crosslinking mass spectrometry" @default.
• W1693641788 cites W1537274817 @default.
• W1693641788 cites W1539163333 @default.
• W1693641788 cites W1549405814 @default.
• W1693641788 cites W1790977108 @default.
• W1693641788 cites W1797775581 @default.
• W1693641788 cites W1815807971 @default.
• W1693641788 cites W1876533241 @default.
• W1693641788 cites W1907169978 @default.
• W1693641788 cites W1964298460 @default.
• W1693641788 cites W1964774325 @default.
• W1693641788 cites W1967086556 @default.
• W1693641788 cites W1971108880 @default.
• W1693641788 cites W1974830441 @default.
• W1693641788 cites W1980473471 @default.
• W1693641788 cites W1980531437 @default.
• W1693641788 cites W1981542877 @default.
• W1693641788 cites W1981593008 @default.
• W1693641788 cites W1982715618 @default.
• W1693641788 cites W1983299266 @default.
• W1693641788 cites W1983717205 @default.
• W1693641788 cites W1985219728 @default.
• W1693641788 cites W1988422519 @default.
• W1693641788 cites W1989252221 @default.
• W1693641788 cites W1990300808 @default.
• W1693641788 cites W1993718695 @default.
• W1693641788 cites W1996444327 @default.
• W1693641788 cites W1996483262 @default.
• W1693641788 cites W1997678546 @default.
• W1693641788 cites W1998747769 @default.
• W1693641788 cites W1999409260 @default.
• W1693641788 cites W2003261719 @default.
• W1693641788 cites W2005217783 @default.
• W1693641788 cites W2005279391 @default.
• W1693641788 cites W2007780468 @default.
• W1693641788 cites W2008855212 @default.
• W1693641788 cites W2010688395 @default.
• W1693641788 cites W2012285720 @default.
• W1693641788 cites W2012534919 @default.
• W1693641788 cites W2013429682 @default.
• W1693641788 cites W2016991749 @default.
• W1693641788 cites W2018084854 @default.
• W1693641788 cites W2018272940 @default.
• W1693641788 cites W2018645739 @default.
• W1693641788 cites W2019112593 @default.
• W1693641788 cites W2023096047 @default.
• W1693641788 cites W2023115652 @default.
• W1693641788 cites W2025493128 @default.
• W1693641788 cites W2026507477 @default.
• W1693641788 cites W2029937591 @default.
• W1693641788 cites W2032006582 @default.
• W1693641788 cites W2033104365 @default.
• W1693641788 cites W2035546135 @default.
• W1693641788 cites W2035739562 @default.
• W1693641788 cites W2040233624 @default.
• W1693641788 cites W2041779764 @default.
• W1693641788 cites W2041965795 @default.
• W1693641788 cites W2043008590 @default.
• W1693641788 cites W2043526011 @default.
• W1693641788 cites W2044031095 @default.
• W1693641788 cites W2044394400 @default.
• W1693641788 cites W2044690163 @default.
• W1693641788 cites W2045033562 @default.
• W1693641788 cites W2045175509 @default.
• W1693641788 cites W2045939425 @default.
• W1693641788 cites W2046201295 @default.
• W1693641788 cites W2046629597 @default.
• W1693641788 cites W2048141156 @default.
• W1693641788 cites W2049023418 @default.
• W1693641788 cites W2050265664 @default.
• W1693641788 cites W2054218747 @default.
• W1693641788 cites W2054507635 @default.
• W1693641788 cites W2059572899 @default.
• W1693641788 cites W2060971202 @default.
• W1693641788 cites W2061271983 @default.
• W1693641788 cites W2061835758 @default.
• W1693641788 cites W2062080188 @default.
• W1693641788 cites W2063618196 @default.
• W1693641788 cites W2064883096 @default.
• W1693641788 cites W2065240973 @default.
• W1693641788 cites W2067743529 @default.
• W1693641788 cites W2068262186 @default.
• W1693641788 cites W2068722030 @default.
• W1693641788 cites W2073035613 @default.
• W1693641788 cites W2073292063 @default.
• W1693641788 cites W2073401456 @default.
• W1693641788 cites W2076490473 @default.
• W1693641788 cites W2079547833 @default.
• W1693641788 cites W2079578946 @default.
• W1693641788 cites W2080877814 @default.
• W1693641788 cites W2084664870 @default.
• W1693641788 cites W2085180994 @default.
• W1693641788 cites W2086317564 @default.
• W1693641788 cites W2087087669 @default.
• W1693641788 cites W2088583078 @default.

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