Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization

scientific article published on 01 October 1996

Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.271.40.24482
P698PubMed publication ID8798708

P2093author name stringA Gertler
J Grosclaude
S Nir
C J Strasburger
J Djiane
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Extracellular domain of prolactin receptor from bovine mammary gland: expression in Escherichia coli, purification and characterization of its interaction with lactogenic hormonesQ38298335
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Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interactionQ46931184
Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensorsQ67711120
Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissueQ67957999
Water-soluble prolactin receptors from porcine mammary glandQ69764025
Differential Biological Activities between Mono- and Bivalent Fragments of Anti-Prolactin Receptor AntibodiesQ70190556
Binding sites of human growth hormone and ovine and bovine prolactins in the mammary gland and the liver of lactating dairy cowQ70191038
Receptors for lactogenic hormones in the ovine corpus luteum. I: A major discrepancy in the specific binding of radiolabelled ovine prolactin and human growth hormoneQ70356065
Human growth hormone but not ovine or bovine growth hormones exhibits galactopoietic prolactin-like activity in organ culture from bovine lactating mammary glandQ71239934
Comparison of a structural and a functional epitopeQ71601556
Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activationQ72871521
P433issue40
P407language of work or nameEnglishQ1860
P304page(s)24482-24491
P577publication date1996-10-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleReal-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization
P478volume271

Reverse relations

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