Matches in SemOpenAlex for { <https://semopenalex.org/work/W4235128066> ?p ?o ?g. }
Showing items 1 to 81 of
81
with 100 items per page.
- W4235128066 endingPage "4384" @default.
- W4235128066 startingPage "4377" @default.
- W4235128066 abstract "The proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans consists of at least 14 unlike subunits (designated Nqo1-14). The NDH-1 is composed of two segments (the peripheral and membrane segments). The membrane domain segment appears to be made up of seven subunits (Nqo7, -8, -10-14). In this report, the characterization of the Paracoccus Nqo11 subunit has been investigated. An antibody against the C-terminal 12 amino acid residues of the Paracoccus Nqo11 subunit (Nqo11c) has been raised. The Nqo11c antibody reacted with a single band (11 kDa) of the Paracoccus membranes and cross-reacted with Rhodobactor capsulatus membranes. The Nqo11 subunit was not able to be extracted from the Paracoccus membranes by NaI or alkaline treatment, unlike the peripheral subunits (Nqo1 and Nqo6). The C-terminal region of the Paracoccus Nqo11 is exposed to the cytoplasmic phase. For further characterization of the Paracoccus Nqo11 subunit, the subunit was overexpressed in Escherichia coli by using the maltose-binding protein (MBP) fusion system. The MBP-fused Nqo11 subunit was expressed in the E. coli membranes (but not in soluble phase) and was extracted by Triton X-100. The isolated MBP-fused Nqo11 subunit interacted with the phospholipid vesicles and suppressed their membrane fluidity. Topological studies of the Nqo11 subunit expressed in E. coli membranes have been performed by using cysteine mapping and immunochemical analyses. The data suggest that the Nqo11 subunit has three transmembrane segments and its C-terminus protrudes into the cytoplasmic phase." @default.
- W4235128066 created "2022-05-12" @default.
- W4235128066 creator A5010100269 @default.
- W4235128066 creator A5026936772 @default.
- W4235128066 creator A5030605627 @default.
- W4235128066 creator A5080582789 @default.
- W4235128066 date "2002-03-06" @default.
- W4235128066 modified "2023-09-25" @default.
- W4235128066 title "Characterization of the Membrane Domain Nqo11 Subunit of the Proton-Translocating NADH-Quinone Oxidoreductase of <i>Paracoccus denitrificans</i>" @default.
- W4235128066 cites W1015595619 @default.
- W4235128066 cites W1587218958 @default.
- W4235128066 cites W1606704458 @default.
- W4235128066 cites W1969830416 @default.
- W4235128066 cites W2020208382 @default.
- W4235128066 cites W207256323 @default.
- W4235128066 cites W2072615411 @default.
- W4235128066 cites W2079000030 @default.
- W4235128066 cites W2094128071 @default.
- W4235128066 cites W2101871915 @default.
- W4235128066 cites W2152770371 @default.
- W4235128066 cites W2395794698 @default.
- W4235128066 cites W2417473218 @default.
- W4235128066 cites W4299496276 @default.
- W4235128066 doi "https://doi.org/10.1021/bi025525d" @default.
- W4235128066 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11914084" @default.
- W4235128066 hasPublicationYear "2002" @default.
- W4235128066 type Work @default.
- W4235128066 citedByCount "15" @default.
- W4235128066 countsByYear W42351280662012 @default.
- W4235128066 crossrefType "journal-article" @default.
- W4235128066 hasAuthorship W4235128066A5010100269 @default.
- W4235128066 hasAuthorship W4235128066A5026936772 @default.
- W4235128066 hasAuthorship W4235128066A5030605627 @default.
- W4235128066 hasAuthorship W4235128066A5080582789 @default.
- W4235128066 hasConcept C104292427 @default.
- W4235128066 hasConcept C104317684 @default.
- W4235128066 hasConcept C118892022 @default.
- W4235128066 hasConcept C144647389 @default.
- W4235128066 hasConcept C161200384 @default.
- W4235128066 hasConcept C181199279 @default.
- W4235128066 hasConcept C185592680 @default.
- W4235128066 hasConcept C2779268744 @default.
- W4235128066 hasConcept C2780640746 @default.
- W4235128066 hasConcept C41625074 @default.
- W4235128066 hasConcept C55493867 @default.
- W4235128066 hasConcept C560191 @default.
- W4235128066 hasConcept C86803240 @default.
- W4235128066 hasConceptScore W4235128066C104292427 @default.
- W4235128066 hasConceptScore W4235128066C104317684 @default.
- W4235128066 hasConceptScore W4235128066C118892022 @default.
- W4235128066 hasConceptScore W4235128066C144647389 @default.
- W4235128066 hasConceptScore W4235128066C161200384 @default.
- W4235128066 hasConceptScore W4235128066C181199279 @default.
- W4235128066 hasConceptScore W4235128066C185592680 @default.
- W4235128066 hasConceptScore W4235128066C2779268744 @default.
- W4235128066 hasConceptScore W4235128066C2780640746 @default.
- W4235128066 hasConceptScore W4235128066C41625074 @default.
- W4235128066 hasConceptScore W4235128066C55493867 @default.
- W4235128066 hasConceptScore W4235128066C560191 @default.
- W4235128066 hasConceptScore W4235128066C86803240 @default.
- W4235128066 hasIssue "13" @default.
- W4235128066 hasLocation W42351280661 @default.
- W4235128066 hasLocation W42351280662 @default.
- W4235128066 hasOpenAccess W4235128066 @default.
- W4235128066 hasPrimaryLocation W42351280661 @default.
- W4235128066 hasRelatedWork W2092661111 @default.
- W4235128066 hasRelatedWork W2107584639 @default.
- W4235128066 hasRelatedWork W2145020089 @default.
- W4235128066 hasRelatedWork W2156144788 @default.
- W4235128066 hasRelatedWork W2395684028 @default.
- W4235128066 hasRelatedWork W2487646191 @default.
- W4235128066 hasRelatedWork W251897196 @default.
- W4235128066 hasRelatedWork W4200053646 @default.
- W4235128066 hasRelatedWork W4386271761 @default.
- W4235128066 hasRelatedWork W69410109 @default.
- W4235128066 hasVolume "41" @default.
- W4235128066 isParatext "false" @default.
- W4235128066 isRetracted "false" @default.
- W4235128066 workType "article" @default.