About: Chapter 2 Viral Channel-Forming Proteins

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Chapter 2 Viral Channel-Forming Proteins
Creator	Krüger, Jens Fischer, Wolfgang
Source	Elsevier; Medline; PMC
abstract	Channel-forming proteins are found in a number of viral genomes. In some cases, their role in the viral life cycle is well understood, in some cases it needs still to be elucidated. A common theme is that their mode of action involves a change of electrochemical or proton gradient across the lipid membrane which modulates the viral or cellular activity. Blocking these proteins can be a suitable therapeutic strategy as for some viruses this may be “lethal.” Besides the many biological relevant questions still to be answered, there are also many open questions concerning the biophysical side as well as structural information and the mechanism of function on a molecular level. The immanent biophysical issues are addressed and the work in the field is summarized.
has issue date	2009-05-31(xsd:dateTime)
bibo:doi	10.1016/s1937-6448(09)75002-6
bibo:pmid	19491052
has license	no-cc
sha1sum (hex)	435a3fad183adc29f255430a4eb0e1466329bde3
schema:url	https://doi.org/10.1016/s1937-6448%2809%2975002-6
resource representing a document's title	Chapter 2 Viral Channel-Forming Proteins
has PubMed Central identifier	PMC7104957
has PubMed identifier	19491052
schema:publication	Int Rev Cell Mol Biol
resource representing a document's body	covid:435a3fad183adc29f255430a4eb0e1466329bde3#body_text
is schema:about of	named entity 'Viral' named entity 'FORMING' named entity 'VIRAL' named entity 'PROTEINS' named entity 'CHANNEL' named entity 'proton' named entity 'Premkumar' named entity 'E. coli' named entity 'Vpu' named entity 'Vpu' named entity 'helical' named entity 'TM-1' named entity 'HIV-1' named entity 'CD4' named entity 'peptide' named entity 'protein' named entity 'channel-forming proteins' named entity 'host cell' named entity 'protein' named entity 'plasma membrane' named entity 'Schubert' named entity 'plasma membrane' named entity 'host cell' named entity 'peptide' named entity 'cation' named entity 'lateral' named entity 'hydrophilic' named entity 'monomers' named entity 'membrane permeability' named entity 'amino acids' named entity 'virion' named entity 'KcsA' named entity 'protein' named entity 'Vpu' named entity 'virus' named entity 'flux' named entity 'infectivity' named entity 'Vpu' named entity 'Xenopus oocytes' named entity 'electrochemical' named entity 'intracellular' named entity 'gramicidin' named entity 'Vpu' named entity 'secretory pathway' named entity 'large-scale' named entity 'open reading frame' named entity 'Cymes' named entity 'HIV' named entity 'eukaryotic' named entity 'drug resistance' named entity 'phosphatidylinositol phosphate' named entity 'spectroscopy' named entity 'helical' named entity 'Vpu' named entity 'cytoplasmic domain' named entity 'peptide' named entity 'amantadine' named entity 'C-terminus' named entity 'virus' named entity 'viral genome' named entity 'cell lines' named entity 'SARS-CoV' named entity 'HCV' named entity 'protein' named entity 'chlorella' named entity 'oscillation' named entity 'bovine viral diarrhea virus' named entity 'protons' named entity 'maltose-binding protein' named entity 'protein' named entity 'cytoplasmic domain' named entity 'alphavirus' named entity 'Myc' named entity 'helix' named entity 'fusion construct' named entity 'experimental studies' named entity 'cleavage' named entity 'hydrophobic' named entity 'virus particle' named entity 'SARS-CoV'

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