Matches in SemOpenAlex for { <https://semopenalex.org/work/W2319317984> ?p ?o ?g. }
Showing items 1 to 49 of
49
with 100 items per page.
- W2319317984 endingPage "974" @default.
- W2319317984 startingPage "965" @default.
- W2319317984 abstract "26S proteasome is the major molecular machine that is responsible for protein degradation in eukaryotic cells. By specifically eliminating target proteins, it is involved in almost every life activities of organisms. 26S proteasome consists of 47 protein members, and can be divided into 19S regulatory particle and 20S core particle. The target protein substrate with polyubiquitin-tag was firstly recognized by 19S regulatory particle, and then unfolded and translocated into 20S core particle for degradation. Due to the structural composition complexity and huge molecular weight of 26S proteasome, the complete structure cannot be resolved with the current X-ray and NMR technology. Only crystal structures of some single subunits and small subcomplex are resolved so far. Yet Cryo-EM technology is under primary developing period in rather a long time. The efforts towards the 3D structure reconstitution of 26S proteasome were not effective. In the past few years, along with experience accumulation in large molecular complexes structure resolved by X-ray, and technical revolution in Cryo-EM field, the 3D structure reconstitution of the complete 26S proteasome moves into a new promising stage. This manuscript reviews the recent important progress in structural biology of 26S proteasome and prospects the development and challenge in the future." @default.
- W2319317984 created "2016-06-24" @default.
- W2319317984 creator A5012059549 @default.
- W2319317984 creator A5053695037 @default.
- W2319317984 date "2014-10-01" @default.
- W2319317984 modified "2023-09-25" @default.
- W2319317984 title "Progress in Structural Biology of 26S Proteasome" @default.
- W2319317984 doi "https://doi.org/10.1360/052014-162" @default.
- W2319317984 hasPublicationYear "2014" @default.
- W2319317984 type Work @default.
- W2319317984 sameAs 2319317984 @default.
- W2319317984 citedByCount "3" @default.
- W2319317984 countsByYear W23193179842015 @default.
- W2319317984 countsByYear W23193179842016 @default.
- W2319317984 countsByYear W23193179842023 @default.
- W2319317984 crossrefType "journal-article" @default.
- W2319317984 hasAuthorship W2319317984A5012059549 @default.
- W2319317984 hasAuthorship W2319317984A5053695037 @default.
- W2319317984 hasConcept C27740335 @default.
- W2319317984 hasConcept C70721500 @default.
- W2319317984 hasConcept C78458016 @default.
- W2319317984 hasConcept C86803240 @default.
- W2319317984 hasConcept C95444343 @default.
- W2319317984 hasConceptScore W2319317984C27740335 @default.
- W2319317984 hasConceptScore W2319317984C70721500 @default.
- W2319317984 hasConceptScore W2319317984C78458016 @default.
- W2319317984 hasConceptScore W2319317984C86803240 @default.
- W2319317984 hasConceptScore W2319317984C95444343 @default.
- W2319317984 hasIssue "10" @default.
- W2319317984 hasLocation W23193179841 @default.
- W2319317984 hasOpenAccess W2319317984 @default.
- W2319317984 hasPrimaryLocation W23193179841 @default.
- W2319317984 hasRelatedWork W1979573002 @default.
- W2319317984 hasRelatedWork W2036842083 @default.
- W2319317984 hasRelatedWork W2061542922 @default.
- W2319317984 hasRelatedWork W2064901328 @default.
- W2319317984 hasRelatedWork W2079283433 @default.
- W2319317984 hasRelatedWork W2190176143 @default.
- W2319317984 hasRelatedWork W2262989315 @default.
- W2319317984 hasRelatedWork W2949168305 @default.
- W2319317984 hasRelatedWork W3147681563 @default.
- W2319317984 hasRelatedWork W4210585717 @default.
- W2319317984 hasVolume "44" @default.
- W2319317984 isParatext "false" @default.
- W2319317984 isRetracted "false" @default.
- W2319317984 magId "2319317984" @default.
- W2319317984 workType "article" @default.