SH2 domain protein interaction and possibilities for pharmacological intervention
Identifieur interne : 000A07 ( Istex/Curation ); précédent : 000A06; suivant : 000A08SH2 domain protein interaction and possibilities for pharmacological intervention
Auteurs : J. Beattie [Royaume-Uni]Source :
- Cellular Signalling [ 0898-6568 ] ; 1996.
English descriptors
- Teeft :
- Arginine residue, Beattie, Binding site, Binding sites, Binding specificity, Biochemistry, Biol, Biological signal, Cell lysates, Cell membrane, Chem, Crystal structure, Cytokine receptors, Cytoplasmic, Cytoplasmic domain, Cytoplasmic region, Cytoplasmic tyrosine kinases, Cytosolic, Cytosolic domain, Cytosolic region, Domain, Domain fusion protein, Domain interaction, Domain manipulation, Domain protein, Domain proteins, Domain transcription factors, Enzyme activity, Functional aspects, Functional data, Hamster polyoma middle, Homology domain, Important role, Kinase, Kinase domains, Large body, Maximal stimulation, Methylene group, Mitogenic response, Mitogenic signal, Pawson, Pdgf, Pdgf receptor, Peptide, Peptide analogues, Peptide binding, Peptide binding specificities, Peptide interactions, Peptide sequences, Peptide target sequence, Peptide target sequences, Pharmacological intervention, Phosphatase, Phosphate group, Phosphorylate sequences, Phosphorylated, Phosphorylation, Phosphotyrosine, Pi3k, Protein, Protein engagement, Protein peptide, Protein targets, Protein tyrosine kinases, Protein tyrosine phosphatase, Rate constants, Reagent, Recent studies, Receptor, Receptor autophosphorylation, Receptor engagement, Recognition motifs, Recognition properties, Residue, Same group, Schlessinger, Shoelson, Signal transducers, Signal transduction, Signal transduction proteins, Subsequent work, Target interaction, Target molecules, Target protein, Target sequence, Target sequences, Tetrahedron lett, Transcription, Transcription factor, Transcription factors, Transduction, Tyrosine, Tyrosine kinases, Tyrosine phosphatases, Tyrosine phosphorylation, Tyrosine residues, Vivo binding site, Widespread distribution.
Abstract
Abstract: SH2 domain containing proteins play a key role in the process of intracellular transmission of signalling events initiated at the cell surface. As a pre-requisite in the fulfilment of this function, these proteins bind to a variety of phospho-tyrosine (pY) containing target molecules. Delineation of these binding sites as essentially short linear peptides (both structurally and functionally) has led to the suggestion that the activity of these signalling complexes may be manipulated by the development of relatively simple peptide reagents. This review examines the range of possibilities open to this approach and the extent to which positive results have already been realised.
Url:
DOI: 10.1016/0898-6568(95)02033-0
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000A07
Links to Exploration step
ISTEX:203FB781EE6393486E02461E6B9C06B0D3FB0DE9Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>SH2 domain protein interaction and possibilities for pharmacological intervention</title><author><name sortKey="Beattie, J" sort="Beattie, J" uniqKey="Beattie J" first="J" last="Beattie">J. Beattie</name><affiliation wicri:level="1"><mods:affiliation>Hannah Research Institute, Ayr KA6 5HL, UK</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Hannah Research Institute, Ayr KA6 5HL</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:203FB781EE6393486E02461E6B9C06B0D3FB0DE9</idno><date when="1996" year="1996">1996</date><idno type="doi">10.1016/0898-6568(95)02033-0</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-X9RJQXRQ-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000A07</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000A07</idno><idno type="wicri:Area/Istex/Curation">000A07</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">SH2 domain protein interaction and possibilities for pharmacological intervention</title><author><name sortKey="Beattie, J" sort="Beattie, J" uniqKey="Beattie J" first="J" last="Beattie">J. Beattie</name><affiliation wicri:level="1"><mods:affiliation>Hannah Research Institute, Ayr KA6 5HL, UK</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Hannah Research Institute, Ayr KA6 5HL</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cellular Signalling</title><title level="j" type="abbrev">CLS</title><idno type="ISSN">0898-6568</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">8</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="75">75</biblScope><biblScope unit="page" to="86">86</biblScope></imprint><idno type="ISSN">0898-6568</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0898-6568</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Arginine residue</term><term>Beattie</term><term>Binding site</term><term>Binding sites</term><term>Binding specificity</term><term>Biochemistry</term><term>Biol</term><term>Biological signal</term><term>Cell lysates</term><term>Cell membrane</term><term>Chem</term><term>Crystal structure</term><term>Cytokine receptors</term><term>Cytoplasmic</term><term>Cytoplasmic domain</term><term>Cytoplasmic region</term><term>Cytoplasmic tyrosine kinases</term><term>Cytosolic</term><term>Cytosolic domain</term><term>Cytosolic region</term><term>Domain</term><term>Domain fusion protein</term><term>Domain interaction</term><term>Domain manipulation</term><term>Domain protein</term><term>Domain proteins</term><term>Domain transcription factors</term><term>Enzyme activity</term><term>Functional aspects</term><term>Functional data</term><term>Hamster polyoma middle</term><term>Homology domain</term><term>Important role</term><term>Kinase</term><term>Kinase domains</term><term>Large body</term><term>Maximal stimulation</term><term>Methylene group</term><term>Mitogenic response</term><term>Mitogenic signal</term><term>Pawson</term><term>Pdgf</term><term>Pdgf receptor</term><term>Peptide</term><term>Peptide analogues</term><term>Peptide binding</term><term>Peptide binding specificities</term><term>Peptide interactions</term><term>Peptide sequences</term><term>Peptide target sequence</term><term>Peptide target sequences</term><term>Pharmacological intervention</term><term>Phosphatase</term><term>Phosphate group</term><term>Phosphorylate sequences</term><term>Phosphorylated</term><term>Phosphorylation</term><term>Phosphotyrosine</term><term>Pi3k</term><term>Protein</term><term>Protein engagement</term><term>Protein peptide</term><term>Protein targets</term><term>Protein tyrosine kinases</term><term>Protein tyrosine phosphatase</term><term>Rate constants</term><term>Reagent</term><term>Recent studies</term><term>Receptor</term><term>Receptor autophosphorylation</term><term>Receptor engagement</term><term>Recognition motifs</term><term>Recognition properties</term><term>Residue</term><term>Same group</term><term>Schlessinger</term><term>Shoelson</term><term>Signal transducers</term><term>Signal transduction</term><term>Signal transduction proteins</term><term>Subsequent work</term><term>Target interaction</term><term>Target molecules</term><term>Target protein</term><term>Target sequence</term><term>Target sequences</term><term>Tetrahedron lett</term><term>Transcription</term><term>Transcription factor</term><term>Transcription factors</term><term>Transduction</term><term>Tyrosine</term><term>Tyrosine kinases</term><term>Tyrosine phosphatases</term><term>Tyrosine phosphorylation</term><term>Tyrosine residues</term><term>Vivo binding site</term><term>Widespread distribution</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: SH2 domain containing proteins play a key role in the process of intracellular transmission of signalling events initiated at the cell surface. As a pre-requisite in the fulfilment of this function, these proteins bind to a variety of phospho-tyrosine (pY) containing target molecules. Delineation of these binding sites as essentially short linear peptides (both structurally and functionally) has led to the suggestion that the activity of these signalling complexes may be manipulated by the development of relatively simple peptide reagents. This review examines the range of possibilities open to this approach and the extent to which positive results have already been realised.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000A07 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Curation/biblio.hfd -nk 000A07 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Curation
|type= RBID
|clé= ISTEX:203FB781EE6393486E02461E6B9C06B0D3FB0DE9
|texte= SH2 domain protein interaction and possibilities for pharmacological intervention
}}
| This area was generated with Dilib version V0.6.33. |  |