Results 101 to 110 of about 299,473 (288)
The ALS‐associated E425K mutation uncouples DNAJC7 from the Hsp70 chaperone cycle
The FEBS Journal, EarlyView.DNAJC7 is a J‐domain protein that plays a key role in protein quality control by regulating Hsp70 activity and preventing protein aggregation. We find that the ALS‐associated E425K mutation in DNAJC7 disrupts productive interaction and activation of Hsp70, thereby blocking the transfer and refolding of client proteins such as TDP‐43.
Bar Elmaleh +2 more
wiley +1 more source
Global SUMO proteome responses guide gene regulation, mRNA biogenesis, and plant stress responses
Frontiers in Plant Science, 2012 Small-ubiquitin-like MOdifier (SUMO) is a key regulator of abiotic stress, disease resistance and development in plants. The identification of >350 plant SUMO targets has revealed many processes modulated by SUMO and potential consequences of SUMO on ...
Magdalena eMazur +1 more
doaj +1 more source
A role for SUMO modification in transcriptional repression and activation [PDF]
, 2007 Since the discovery of the SUMO (small ubiquitin-like modifier) family of proteins just over a decade ago, a plethora of substrates have been uncovered including many regulators of transcription.
David +26 more
core +1 more source
Cell Reports, 2019 Signaling by the ubiquitin-related SUMO pathway relies on coordinated conjugation and deconjugation events. SUMO-specific deconjugating enzymes counterbalance SUMOylation, but comprehensive insight into their substrate specificity and regulation is ...
K. Wagner +9 more
semanticscholar +1 more source
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2004 SUMO (small ubiquitin-related modifier) family proteins are not only structurally but also mechanistically related to ubiquitin in that they are posttranslationally attached to other proteins. As ubiquitin, SUMO is covalently linked to its substrates via amide (isopeptide) bonds formed between its C-terminal glycine residue and the epsilon-amino group ...
openaire +2 more sources
Lock, relax, load, and shoot: a molecular perspective on Nedd4 regulation
The FEBS Journal, EarlyView.Structural basis of inactive and active states of the Nedd4 HECT E3 ligase subfamily, following a ‘lock, relax, load, and shoot’ mechanism. In the locked, autoinhibited state, intramolecular domain interactions restrain the HECT domain. Relaxation releases these restraints, allowing loading of ubiquitin onto the catalytic cysteine, followed by the ...
Masa Janosev +2 more
wiley +1 more source
Cellular Physiology and Biochemistry, 2017 Background: It has been reported that blocking small ubiquitin-like modifier (SUMO) conjugation by silencing SUMO gene remarkably decreased tumor growth in vivo.
Lifang Jin +4 more
doaj +1 more source
Charged by the market : electricity deregulation is finally starting to stir up retail competition in Maryland [PDF]
Electric utilities ; Federal Reserve District ...
Vanessa Sumo
core
SUMOylation of NaV1.2 channels mediates the early response to acute hypoxia in central neurons. [PDF]
, 2016 The mechanism for the earliest response of central neurons to hypoxia-an increase in voltage-gated sodium current (INa)-has been unknown. Here, we show that hypoxia activates the Small Ubiquitin-like Modifier (SUMO) pathway in rat cerebellar granule ...
Goldstein, Steve An +2 more
core +2 more sources