FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2148471582> ?p ?o ?g. }

• W2148471582 endingPage "1607" @default.
• W2148471582 startingPage "1599" @default.
• W2148471582 abstract "The cell wall of the biflagellate alga Chlamydomonas reinhardtii is a multilayered, extracellular matrix composed of carbohydrates and 20-25 polypeptides. To learn more about the forces responsible for the integrity of this cellulose-deficient cell wall, we have begun studies to identify and characterize the framework of the wall and to determine the effects of the cell wall-degrading enzyme, lysin, on framework structure and protein composition. In these studies we used walls released into the medium by mating gametes. When isolated shed walls are degraded by exogenously added lysin, no changes are detected in the charge or molecular weight of the 20-25 wall proteins and glycoproteins when analyzed on one- and two-dimensional polyacrylamide gels, which suggests that degradation of these shed walls is due either to cleavage of peptide bonds very near the ends of polypeptides or that degradation occurs via a mechanism other than proteolysis. Incubation of walls with Sarkosyl-urea solutions removes most of the proteins and yields thin structures that appear to be the frameworks of the walls. Analysis by polyacrylamide gel electrophoresis shows that the frameworks are highly enriched in a polypeptide of Mr 100,000. Treatment of frameworks with lysin leads to their degradation, which indicates that this part of the wall is a substrate for the enzyme. Although lysin converts the Mr 100,000 polypeptide from an insoluble to a soluble form, there is no detectable change in Mr of the framework protein. Solubilization in the absence of lysin requires treatment with SDS and dithiothreitol at 100 degrees C. These results suggest that the Chlamydomonas cell wall is composed of two separate domains: one containing approximately 20 proteins held together by noncovalent interactions and a second domain, containing only a few proteins, which constitutes the framework of the wall. The result that shed walls can be solubilized by boiling in SDS-dithiothreitol indicates that disulfide linkages are critical for wall integrity. Using an alternative method for isolating walls from mechanically disrupted gametes, we have also shown that a wall-shaped portion of these unshed walls is insoluble under the same conditions in which shed walls are soluble. One interpretation of these results is that wall release during mating and the wall degradation that follows may involve distinct biochemical events." @default.
• W2148471582 created "2016-06-24" @default.
• W2148471582 creator A5018309043 @default.
• W2148471582 creator A5055013798 @default.
• W2148471582 creator A5061001149 @default.
• W2148471582 creator A5090729574 @default.
• W2148471582 date "1985-10-01" @default.
• W2148471582 modified "2023-10-17" @default.
• W2148471582 title "The Chlamydomonas cell wall: characterization of the wall framework." @default.
• W2148471582 cites W1498367774 @default.
• W2148471582 cites W1532655503 @default.
• W2148471582 cites W1603867270 @default.
• W2148471582 cites W1775749144 @default.
• W2148471582 cites W1972764933 @default.
• W2148471582 cites W1982092087 @default.
• W2148471582 cites W1992521021 @default.
• W2148471582 cites W1997983436 @default.
• W2148471582 cites W2014321075 @default.
• W2148471582 cites W2018289835 @default.
• W2148471582 cites W2027421061 @default.
• W2148471582 cites W2054131393 @default.
• W2148471582 cites W2075814065 @default.
• W2148471582 cites W2083453910 @default.
• W2148471582 cites W2100837269 @default.
• W2148471582 cites W2139175710 @default.
• W2148471582 cites W2331433450 @default.
• W2148471582 doi "https://doi.org/10.1083/jcb.101.4.1599" @default.
• W2148471582 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2113912" @default.
• W2148471582 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2413047" @default.
• W2148471582 hasPublicationYear "1985" @default.
• W2148471582 type Work @default.
• W2148471582 sameAs 2148471582 @default.
• W2148471582 citedByCount "96" @default.
• W2148471582 countsByYear W21484715822012 @default.
• W2148471582 countsByYear W21484715822013 @default.
• W2148471582 countsByYear W21484715822014 @default.
• W2148471582 countsByYear W21484715822015 @default.
• W2148471582 countsByYear W21484715822016 @default.
• W2148471582 countsByYear W21484715822017 @default.
• W2148471582 countsByYear W21484715822018 @default.
• W2148471582 countsByYear W21484715822019 @default.
• W2148471582 countsByYear W21484715822020 @default.
• W2148471582 countsByYear W21484715822021 @default.
• W2148471582 countsByYear W21484715822022 @default.
• W2148471582 countsByYear W21484715822023 @default.
• W2148471582 crossrefType "journal-article" @default.
• W2148471582 hasAuthorship W2148471582A5018309043 @default.
• W2148471582 hasAuthorship W2148471582A5055013798 @default.
• W2148471582 hasAuthorship W2148471582A5061001149 @default.
• W2148471582 hasAuthorship W2148471582A5090729574 @default.
• W2148471582 hasBestOaLocation W21484715821 @default.
• W2148471582 hasConcept C104317684 @default.
• W2148471582 hasConcept C125235067 @default.
• W2148471582 hasConcept C12554922 @default.
• W2148471582 hasConcept C143065580 @default.
• W2148471582 hasConcept C181199279 @default.
• W2148471582 hasConcept C22538091 @default.
• W2148471582 hasConcept C2776441376 @default.
• W2148471582 hasConcept C2776580309 @default.
• W2148471582 hasConcept C2777727519 @default.
• W2148471582 hasConcept C2777824588 @default.
• W2148471582 hasConcept C2781307694 @default.
• W2148471582 hasConcept C547475151 @default.
• W2148471582 hasConcept C55493867 @default.
• W2148471582 hasConcept C86803240 @default.
• W2148471582 hasConceptScore W2148471582C104317684 @default.
• W2148471582 hasConceptScore W2148471582C125235067 @default.
• W2148471582 hasConceptScore W2148471582C12554922 @default.
• W2148471582 hasConceptScore W2148471582C143065580 @default.
• W2148471582 hasConceptScore W2148471582C181199279 @default.
• W2148471582 hasConceptScore W2148471582C22538091 @default.
• W2148471582 hasConceptScore W2148471582C2776441376 @default.
• W2148471582 hasConceptScore W2148471582C2776580309 @default.
• W2148471582 hasConceptScore W2148471582C2777727519 @default.
• W2148471582 hasConceptScore W2148471582C2777824588 @default.
• W2148471582 hasConceptScore W2148471582C2781307694 @default.
• W2148471582 hasConceptScore W2148471582C547475151 @default.
• W2148471582 hasConceptScore W2148471582C55493867 @default.
• W2148471582 hasConceptScore W2148471582C86803240 @default.
• W2148471582 hasIssue "4" @default.
• W2148471582 hasLocation W21484715821 @default.
• W2148471582 hasLocation W21484715822 @default.
• W2148471582 hasLocation W21484715823 @default.
• W2148471582 hasLocation W21484715824 @default.
• W2148471582 hasOpenAccess W2148471582 @default.
• W2148471582 hasPrimaryLocation W21484715821 @default.
• W2148471582 hasRelatedWork W1969672244 @default.
• W2148471582 hasRelatedWork W2043153675 @default.
• W2148471582 hasRelatedWork W2072317909 @default.
• W2148471582 hasRelatedWork W2124837873 @default.
• W2148471582 hasRelatedWork W2127695978 @default.
• W2148471582 hasRelatedWork W2148471582 @default.
• W2148471582 hasRelatedWork W2160901777 @default.
• W2148471582 hasRelatedWork W2228981914 @default.
• W2148471582 hasRelatedWork W2914026614 @default.
• W2148471582 hasRelatedWork W2998515493 @default.
• W2148471582 hasVolume "101" @default.
• W2148471582 isParatext "false" @default.

• next