Evaluating chalcogen heteroatoms in conjugated polymers for organic electronics

Kobilka, Brandon M.

doi:10.31274/etd-180810-544

Cited by 2 publications

(2 citation statements)

References 101 publications

(107 reference statements)

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“…Our data support and considerably expand previous findings obtained with truncated /?Zadrenergic receptors [24]. In this case, coinjection into Xenopus oocytes of mRNAs coding for two fragmented @2-adrenergic receptors ('split' within the i3 loop) resulted in the appearance of specific adrenergic binding sites.…”

Section: Agonist Binding Studiessupporting

confidence: 90%

Reconstitution of functional muscarinic receptors by co‐expression of amino‐ and carboxyl‐terminal receptor fragments

Maggio¹,

Vogel²,

Wess³

1993

FEBS Letters

118

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Truncated m2 and m3 muscarinic receptors (referred to as m2-and m3-trunc), containing transmembrane domains I-V and the N-terminal portion of the third cytoplasmic loop, were co-expressed in COS-7 cells with the corresponding C-terminal receptor fragments (referred to as m2-and m3-tail; containing transmembrane domains VI and VII). Expression of any of these four polypeptides alone did not result in any detectable ["H]N-methylscopolamine (['HINMS) binding activity. However, specific ['H]NMS binding sites were observed after co-expression of m2-trunc with m2-tail and m3-trunc with m3-tail. These sites displayed ligand binding properties similar to those of the two wild-type receptors. The 'reconstituted' m3-trunc/m3-tail receptor was also able to stimulate agonist-dependent phosphatidyl inositol hydrolysis in a fashion similar to the wild-type m3 receptor, whereas all other polypeptide combinations were inactive. These data suggest that muscarinic receptors are assembled in a fashion analogous to two-subunit receptors.

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Section: Agonist Binding Studiessupporting

confidence: 90%

Reconstitution of functional muscarinic receptors by co‐expression of amino‐ and carboxyl‐terminal receptor fragments

Maggio¹,

Vogel²,

Wess³

1993

FEBS Letters

118

View full text Add to dashboard Cite

show abstract

“…RSS protein may increase the binding affinity of the receptor to 5-HT and/or sensitize one of the steps of the signal transduction which activates PLC. Actually, there are several reports suggesting a requirement for cofactors for membrane insertion and posttranslational activation of G protein-coupled receptors [26][27][28]. Moreover, some proteins which markedly affect G protein activity or receptor-G protein coupling have been identified.…”

Section: Putative Cellular Function Of Rss Proteinmentioning

confidence: 99%