About: The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function
Creator	Duncan, Roy Cashdollar, L Lee, Patrick Leone, Gustav0 Mah,', David Price, Angela
Source	Elsevier; Medline; PMC
abstract	Abstract The oligomerization domain of the reovirus cell attachment protein (σ1) was probed using the type 3 reovirus of synthesized in vitro. Trypsin cleaved the α1 protein (49K molecular weight) approximately in the middle and yielded a 26K N-terminal fragment and a 23K C-terminal fragment. Under conditions which allowed for the identification of intact σ1 in the oligomeric form (∼200K) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the N-terminal 26K fragment was found to exist as stable trimers (80K) and, to a less extent, as dimers (54K), whereas the C-terminal fragment remained in the monomeric form. A polypeptide (161 amino acids) containing the N-terminal heptad repeat region synthesized in vitro was capable of forming stable dimers and trimers. Using various criteria, we demonstrated that the stability of the intact σ1 oligomer is conferred mainly by the N-terminal heptad repeat region. Our results are summarized in a model in which individual heptad repeats are held together in a three-stranded α-helical coiled-coil structure via both hydrophobic and electrostatic interactions.
has issue date	1991-05-31(xsd:dateTime)
bibo:doi	10.1016/0042-6822(91)90677-4
bibo:pmid	2024469
has license	els-covid
sha1sum (hex)	1c8c5fe41c96cc291ac0cfa5ea8fcd84c811d7c1
schema:url	https://doi.org/10.1016/0042-6822%2891%2990677-4
resource representing a document's title	The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function
has PubMed Central identifier	PMC7130816
has PubMed identifier	2024469
schema:publication	Virology
resource representing a document's body	covid:1c8c5fe41c96cc291ac0cfa5ea8fcd84c811d7c1#body_text
is schema:about of	named entity 'FUNCTION' named entity 'OLIGOMERIZATION' named entity 'protein' named entity 'REPEAT REGION' named entity 'CONDITIONS' named entity 'IN VITRO' named entity 'EXTENT' named entity 'OLIGOMER' named entity 'REPEAT REGION' named entity 'PROTEIN ' named entity '2801' named entity 'INTRINSIC' named entity 'POLYPEPTIDE' named entity 'N-TERMINAL ' named entity 'INTERACTIONS' named entity 'FORM' named entity 'ELECTROSTATIC' named entity 'DEMONSTRATED' named entity 'COILED-COIL' named entity 'CLEAVED' named entity 'DIMERS' named entity 'FORMING' named entity 'REPEATS' named entity 'DOMAIN' named entity 'APPROXIMATELY' named entity 'MIDDLE' named entity 'CAPABLE' named entity 'USING' named entity 'VARIOUS' named entity 'IDENTIFICATION' named entity 'STABILITY' named entity 'SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS' named entity 'OUR' named entity 'CELL ATTACHMENT' named entity 'TRYPSIN' named entity 'TYPE 3' named entity '28161' named entity 'CELL ATTACHMENT' named entity 'PVS' named entity 'RESULTS' named entity 'MODEL' named entity 'FOUND' named entity 'N-TERMINAL FRAGMENT' named entity 'CONTAINING' named entity 'HYDROPHOBIC' named entity 'OLIGOMER' named entity 'POSSESSES' named entity 'RESPONSIBLE' named entity 'STABILITY' named entity 'REOVIRUS' named entity 'SYNTHESIZED' named entity 'CRITERIA' named entity 'REOVIRUS' named entity 'EXIST' named entity 'STRUCTURE' named entity 'ACADEMIC' named entity 'HELICAL' named entity 'INDIVIDUAL' named entity 'HELD' named entity 'AMINO ACIDS' named entity 'STABLE' named entity 'C-TERMINAL' named entity 'INTACT' named entity 'MOLECULAR WEIGHT' named entity 'PROBED' named entity 'OLIGOMERIZATION' named entity 'ALLOWED' named entity 'N-TERMINAL ' named entity 'PROTEIN ' named entity 'FRAGMENT' named entity 'fragment' named entity 'amino acids' named entity 'monomeric' named entity 'trimers' named entity 'Under' named entity 'domain'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software