Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor

scientific article

Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor is …
instance of (P31):
scholarly articleQ13442814

External links are
P819ADS bibcode2007PNAS..10411945P
P356DOI10.1073/PNAS.0704348104
P932PMC publication ID1924551
P698PubMed publication ID17609376
P5875ResearchGate publication ID6229122

P2093author name stringDaniel DiMaio
Anne P B Edwards
Lisa L Freeman-Cook
Jennifer B Ptacek
P2860cites workThe BPV-1 E5 protein, the 16 kDa membrane pore-forming protein and the PDGF receptor exist in a complex that is dependent on hydrophobic transmembrane interactionsQ24337640
A transmembrane helix dimer: structure and implicationsQ27735013
Selection and characterization of small random transmembrane proteins that bind and activate the platelet-derived growth factor beta receptor.Q30341383
Motifs of serine and threonine can drive association of transmembrane helicesQ30819513
Specific locations of hydrophilic amino acids in constructed transmembrane ligands of the platelet-derived growth factor beta receptorQ31135195
The platelet-derived growth factor beta receptor as a target of the bovine papillomavirus E5 proteinQ33180948
Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor beta receptorQ33575831
The organizing principle in the formation of the T cell receptor-CD3 complex.Q34167740
Sequence specificity in the dimerization of transmembrane alpha-helicesQ34279030
Polar residues drive association of polyleucine transmembrane helicesQ34449670
Polar side chains drive the association of model transmembrane peptidesQ34630825
Multiple transmembrane amino acid requirements suggest a highly specific interaction between the bovine papillomavirus E5 oncoprotein and the platelet-derived growth factor beta receptorQ35000599
Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 proteinQ36318177
Folding and stability of alpha-helical integral membrane proteinsQ36472824
The bovine papillomavirus type 1 E5 transforming protein specifically binds and activates the beta-type receptor for the platelet-derived growth factor but not other related tyrosine kinase-containing receptors to induce cellular transformationQ36622401
Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cellsQ37119249
The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residuesQ38338136
Identification of the transmembrane dimer interface of the bovine papillomavirus E5 proteinQ40794484
Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming proteinQ41080345
Transmembrane helical interactions and the assembly of the T cell receptor complexQ41727804
Structural models of the bovine papillomavirus E5 protein.Q52229470
Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.Q54577274
Membrane protein association by potential intrarnembrane charge pairsQ59054338
Membrane protein folding and oligomerization: the two-stage modelQ67662788
Interhelical hydrogen bonding drives strong interactions in membrane proteinsQ73402358
Asparagine-mediated self-association of a model transmembrane helixQ73402361
P433issue29
P407language of work or nameEnglishQ1860
P921main subjecttransmembrane proteinQ424204
Platelet derived growth factor receptor, beta polypeptideQ21983261
P304page(s)11945-11950
P577publication date2007-07-03
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titlePacking contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor
P478volume104

Reverse relations

cites work (P2860)
Q37189482A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor β receptor into an inhibitor
Q33482628Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet-derived growth factor beta receptor
Q39113585Compensatory mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor β receptor reveal a complex direct transmembrane interaction
Q33530296Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor.
Q33768327Construction and maintenance of randomized retroviral expression libraries for transmembrane protein engineering
Q37475038De novo selection of oncogenes
Q35161709Mapping the homodimer interface of an optimized, artificial, transmembrane protein activator of the human erythropoietin receptor
Q92265666Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them
Q34754347The E5 proteins
Q37319770The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango
Q35151120Viral miniproteins

Search more.