A putative molecular-activation switch in the transmembrane domain of erbB2.

scientific article

A putative molecular-activation switch in the transmembrane domain of erbB2. is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2002PNAS...9915937F
P356DOI10.1073/PNAS.252640799
P932PMC publication ID138543
P698PubMed publication ID12461170
P5875ResearchGate publication ID11009784

P50authorJoseph SchlessingerQ2908140
Sarel J FleishmanQ41625606
Nir Ben-TalQ47333803
P2860cites workG to A polymorphism at amino acid codon 655 of the human erbB-2/HER2 geneQ40507769
A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signalingQ40673334
Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domainQ40782870
Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformationQ42803794
Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185.Q42811529
The single transmembrane domains of ErbB receptors self-associate in cell membranesQ43821697
A point mutation in the neu oncogene mimics ligand induction of receptor aggregationQ44611984
Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions.Q52081092
Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk.Q53412908
Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptorQ57103722
A Novel Scoring Function for Predicting the Conformations of Tightly Packed Pairs of Transmembrane α-HelicesQ57207133
Neu receptor dimerizationQ59087928
A transmembrane helix dimer: structure and implicationsQ27735013
Cell signaling by receptor tyrosine kinasesQ27860474
Signal transduction by receptors with tyrosine kinase activityQ27860624
Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helicesQ28298420
ErbB-2 is a common auxiliary subunit of NDF and EGF receptors: implications for breast cancerQ28678776
The GxxxG motif: a framework for transmembrane helix-helix associationQ30839523
Receptor signaling: when dimerization is not enoughQ33723925
ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signalingQ33886341
A subdomain in the transmembrane domain is necessary for p185neu* activationQ33937484
The epidermal growth factor receptor family as a central element for cellular signal transduction and diversificationQ34249785
Helix to helix packing in proteinsQ34283185
Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinaseQ34769307
Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 geneQ36851389
A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerizationQ37878779
Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signalingQ40015717
An EcoRI polymorphism at the insulin receptor locus on a fragment comprising exons 4 to 8.Q40507764
P433issue25
P407language of work or nameEnglishQ1860
P921main subjecttransmembrane proteinQ424204
P304page(s)15937-15940
P577publication date2002-12-02
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleA putative molecular-activation switch in the transmembrane domain of erbB2.
P478volume99

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cites work (P2860)
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