Matches in SemOpenAlex for { <https://semopenalex.org/work/W4236214925> ?p ?o ?g. }
Showing items 1 to 49 of
49
with 100 items per page.
- W4236214925 endingPage "570a" @default.
- W4236214925 startingPage "570a" @default.
- W4236214925 abstract "Aberrant protein folding is implicated in several devastating neurodegenerative diseases. Intractable inclusions containing the proteins TDP-43 and FUS are implicated in some cases of amyotrophic lateral sclerosis, while amyloid fibers comprised of α-synuclein are implicated in Parkinson's disease. Hsp104, an AAA+ protein from yeast, functions in regulating the disassembly of amorphous aggregates as well as prions. There are no other proteins known that are capable of specifically disassembling and solubilizing amyloid. Though Hsp104 is highly conserved, it has no human homologue. Therefore, we have developed potentiated Hsp104 variants and applied them to disease models of TDP-43, FUS, and α-synuclein pathology. These potentiated Hsp104 variants dissolve the aggregates, return the proteins to their proper cellular location, and strongly suppress toxicity in each of these disease models at levels far greater than wild-type. Surprisingly, we have also found that at certain positions in Hsp104, generic mutations to nearly any class of amino acid yield a hyperactive protein capable of eliminating aggregates. These “gatekeeper” residues reveal important new insights into the mechanism by which Hsp104 dissolves amyloid." @default.
- W4236214925 created "2022-05-12" @default.
- W4236214925 creator A5084836766 @default.
- W4236214925 date "2013-01-01" @default.
- W4236214925 modified "2023-09-28" @default.
- W4236214925 title "Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events" @default.
- W4236214925 doi "https://doi.org/10.1016/j.bpj.2012.11.3168" @default.
- W4236214925 hasPublicationYear "2013" @default.
- W4236214925 type Work @default.
- W4236214925 citedByCount "0" @default.
- W4236214925 crossrefType "journal-article" @default.
- W4236214925 hasAuthorship W4236214925A5084836766 @default.
- W4236214925 hasBestOaLocation W42362149251 @default.
- W4236214925 hasConcept C136238340 @default.
- W4236214925 hasConcept C185592680 @default.
- W4236214925 hasConcept C204328495 @default.
- W4236214925 hasConcept C2777633098 @default.
- W4236214925 hasConcept C55493867 @default.
- W4236214925 hasConcept C59822182 @default.
- W4236214925 hasConcept C86803240 @default.
- W4236214925 hasConcept C95444343 @default.
- W4236214925 hasConceptScore W4236214925C136238340 @default.
- W4236214925 hasConceptScore W4236214925C185592680 @default.
- W4236214925 hasConceptScore W4236214925C204328495 @default.
- W4236214925 hasConceptScore W4236214925C2777633098 @default.
- W4236214925 hasConceptScore W4236214925C55493867 @default.
- W4236214925 hasConceptScore W4236214925C59822182 @default.
- W4236214925 hasConceptScore W4236214925C86803240 @default.
- W4236214925 hasConceptScore W4236214925C95444343 @default.
- W4236214925 hasIssue "2" @default.
- W4236214925 hasLocation W42362149251 @default.
- W4236214925 hasOpenAccess W4236214925 @default.
- W4236214925 hasPrimaryLocation W42362149251 @default.
- W4236214925 hasRelatedWork W103782306 @default.
- W4236214925 hasRelatedWork W1568341003 @default.
- W4236214925 hasRelatedWork W2052156860 @default.
- W4236214925 hasRelatedWork W2112335210 @default.
- W4236214925 hasRelatedWork W2149996174 @default.
- W4236214925 hasRelatedWork W2790534435 @default.
- W4236214925 hasRelatedWork W2809404391 @default.
- W4236214925 hasRelatedWork W2896878547 @default.
- W4236214925 hasRelatedWork W2999966139 @default.
- W4236214925 hasRelatedWork W4231731157 @default.
- W4236214925 hasVolume "104" @default.
- W4236214925 isParatext "false" @default.
- W4236214925 isRetracted "false" @default.
- W4236214925 workType "article" @default.