Matches in SemOpenAlex for { <https://semopenalex.org/work/W2912266507> ?p ?o ?g. }
Showing items 1 to 67 of
67
with 100 items per page.
- W2912266507 endingPage "185a" @default.
- W2912266507 startingPage "184a" @default.
- W2912266507 abstract "GDH-1 which converts glutamate to alpha-ketoglutarate and ammonia while reducing NAD(P) is constitutively expressed in all nucleated cells of mammals. Encoded by a nuclear gene, its mitochondrial matrix concentration is high (5-10 mg /ml). Turnover is also high considering a mitochondrial t 1/2 of 1-2 days. The MW of GDH-1 subunits is 56K. Newly synthesized enzyme precursor subunits are transported into mitochondria, are rapidly cleaved and assemble there to the enzymatically active homo-hexamer of 336K MW. Furthermore, bovine liver GDH-1 does form complexes of about 1.5 Mill at concentration above 2-3 mg/ml. Activating point mutations (e.g H454Y) cause life threatening hyperinsulinism. To better understand the biology of this protein, essential for life and of high medical relevance, we are using tryptophan and ANS fluorescence to study (in model experiments) the process of disassembly caused by urea and reassembly after urea removal by dilution or dialysis. An extensive literature beginning with the report by Olson and Anfinsen in 1952 provides useful background information. We show by monitoring tryptophan and ANS fluorescence that the trimer of the protein, formed at 3M urea, can be readily reassembled to the original higher molecular forms but that smaller structures, formed when exposed to urea exceeding 3 M, cannot be reassembled to the original multimeric forms. At this juncture we focus on the reversible process between 0 and 3 M urea, determining the rates of interconversion of multimeric forms as influenced by pH, temperature, the enzyme's substrates and its known allosteric modifiers using tryptophan fluorescence. We are testing a hypothesis that interconversion rates between trimers, hexamers and poly-hexamers contribute to the regulation of GDH-1 which controls glutaminolysis in insulin secreting beta-cells and cancer cells." @default.
- W2912266507 created "2019-02-21" @default.
- W2912266507 creator A5027436570 @default.
- W2912266507 creator A5050182252 @default.
- W2912266507 creator A5079229712 @default.
- W2912266507 date "2019-02-01" @default.
- W2912266507 modified "2023-10-16" @default.
- W2912266507 title "Disassembling and Reassembling Complex Structure of Glutamate Dehydrogenase 1 (DGH-1), Monitored by Tryptophan and 1-Anilinonaphthalene-8-Sulfonate (ANS) Fluorimetry" @default.
- W2912266507 doi "https://doi.org/10.1016/j.bpj.2018.11.1024" @default.
- W2912266507 hasPublicationYear "2019" @default.
- W2912266507 type Work @default.
- W2912266507 sameAs 2912266507 @default.
- W2912266507 citedByCount "0" @default.
- W2912266507 crossrefType "journal-article" @default.
- W2912266507 hasAuthorship W2912266507A5027436570 @default.
- W2912266507 hasAuthorship W2912266507A5050182252 @default.
- W2912266507 hasAuthorship W2912266507A5079229712 @default.
- W2912266507 hasBestOaLocation W29122665071 @default.
- W2912266507 hasConcept C104292427 @default.
- W2912266507 hasConcept C104317684 @default.
- W2912266507 hasConcept C12554922 @default.
- W2912266507 hasConcept C170493617 @default.
- W2912266507 hasConcept C181199279 @default.
- W2912266507 hasConcept C185592680 @default.
- W2912266507 hasConcept C2776706248 @default.
- W2912266507 hasConcept C2777202666 @default.
- W2912266507 hasConcept C2780365088 @default.
- W2912266507 hasConcept C28859421 @default.
- W2912266507 hasConcept C515207424 @default.
- W2912266507 hasConcept C55493867 @default.
- W2912266507 hasConcept C61174792 @default.
- W2912266507 hasConcept C86803240 @default.
- W2912266507 hasConceptScore W2912266507C104292427 @default.
- W2912266507 hasConceptScore W2912266507C104317684 @default.
- W2912266507 hasConceptScore W2912266507C12554922 @default.
- W2912266507 hasConceptScore W2912266507C170493617 @default.
- W2912266507 hasConceptScore W2912266507C181199279 @default.
- W2912266507 hasConceptScore W2912266507C185592680 @default.
- W2912266507 hasConceptScore W2912266507C2776706248 @default.
- W2912266507 hasConceptScore W2912266507C2777202666 @default.
- W2912266507 hasConceptScore W2912266507C2780365088 @default.
- W2912266507 hasConceptScore W2912266507C28859421 @default.
- W2912266507 hasConceptScore W2912266507C515207424 @default.
- W2912266507 hasConceptScore W2912266507C55493867 @default.
- W2912266507 hasConceptScore W2912266507C61174792 @default.
- W2912266507 hasConceptScore W2912266507C86803240 @default.
- W2912266507 hasIssue "3" @default.
- W2912266507 hasLocation W29122665071 @default.
- W2912266507 hasOpenAccess W2912266507 @default.
- W2912266507 hasPrimaryLocation W29122665071 @default.
- W2912266507 hasRelatedWork W122755718 @default.
- W2912266507 hasRelatedWork W1540813780 @default.
- W2912266507 hasRelatedWork W1550996414 @default.
- W2912266507 hasRelatedWork W1644178486 @default.
- W2912266507 hasRelatedWork W2004312381 @default.
- W2912266507 hasRelatedWork W2011935905 @default.
- W2912266507 hasRelatedWork W2049974425 @default.
- W2912266507 hasRelatedWork W2413428975 @default.
- W2912266507 hasRelatedWork W2461573786 @default.
- W2912266507 hasRelatedWork W848914235 @default.
- W2912266507 hasVolume "116" @default.
- W2912266507 isParatext "false" @default.
- W2912266507 isRetracted "false" @default.
- W2912266507 magId "2912266507" @default.
- W2912266507 workType "article" @default.