Zobrazeno 1 - 10
of 440
pro vyhledávání: '"Relaxin/insulin-like family peptide receptor 2"'
Autor:
John B. Furness, Praveen Praveen, Mohammed Akhter Hossain, Shuai Nie, Qinghao Ou, Ruslan V Pustovit, Jamie Jm Liew, Xiaozhou Zhang, Martina Kocan, Lalita Oparija-Rogenmozere, Mengjie Liu, Ada Koo, Ross A. D. Bathgate
Publikováno v:
ACS Pharmacol Transl Sci
[Image: see text] Insulin-like peptide 5 (INSL5), the natural ligand for the relaxin family peptide receptor 4 (RXFP4), is a gut hormone that is exclusively produced by colonic L-cells. We have recently developed an analogue of INSL5, INSL5-A13, that
Publikováno v:
Insect Molecular Biology. 29:309-319
Insulin-like peptides (ILPs) including insulin, insulin-like growth factor (IGF) and relaxin are evolutionarily conserved hormones in metazoans, and they are involved in diverse physiological processes. The migratory brown planthopper (BPH), Nilaparv
Autor:
Raymond S. Norton, Michela L. Mitchell, Jan Tytgat, John D. Wade, Briony E. Forbes, Feng Lin, Dorothy C.C. Wai, Carlie Delaine, Steve Peigneur, Mohammed Akhter Hossain, Ernesto Lopes Pinheiro-Junior, Andrew Blyth
Publikováno v:
Biomolecules
Biomolecules; Volume 11; Issue 12; Pages: 1785
Biomolecules, Vol 11, Iss 1785, p 1785 (2021)
Biomolecules; Volume 11; Issue 12; Pages: 1785
Biomolecules, Vol 11, Iss 1785, p 1785 (2021)
The role of insulin and insulin-like peptides (ILPs) in vertebrate animals is well studied. Numerous ILPs are also found in invertebrates, although there is uncertainty as to the function and role of many of these peptides. We have identified transcr
Autor:
Zhenjun Zhao, Wenli Li, Zhi-Chao Liu, Ye Bo, Xiao-Bing Ren, Qi Fan, Yubo Liu, Jianing Zhang, Ya-Na Li
Publikováno v:
Insects
Volume 12
Issue 9
Insects, Vol 12, Iss 784, p 784 (2021)
Volume 12
Issue 9
Insects, Vol 12, Iss 784, p 784 (2021)
In insects, trehalose accumulation is associated with the insulin/insulin-like growth factor signalling (IIS) pathway. However, whether insulin-like peptide is involved in the regulation of the trehalose metabolism during diapause termination remains
Publikováno v:
Frontiers in Physiology
Frontiers in Physiology, Vol 12 (2021)
Frontiers in Physiology, Vol 12 (2021)
Most insect species encode multiple insulin-like peptides (ILPs) that exhibit functional overlaps in mediating physiological processes such as development and reproduction. Why do they need multiple ILPs? To address this question, we tested a hypothe
Culex pipiens form pipiens and Cx. pipiens form molestus differ in their ability to produce eggs without a bloodmeal. Autogenous mosquitoes, such as the molestus bioform of Cx. pipiens, depend on nutrition acquired as larvae instead of a bloodmeal to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f25bd10b88a437b1823dc7103923614b
https://doi.org/10.1101/2021.06.20.449144
https://doi.org/10.1101/2021.06.20.449144
Publikováno v:
Endocrine Abstracts.
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 5259, p 5259 (2021)
International Journal of Molecular Sciences
Volume 22
Issue 10
International Journal of Molecular Sciences
Volume 22
Issue 10
The involvement of insulin/insulin-like growth factor signaling (IIS) pathways in the growth regulation of marine invertebrates remains largely unexplored. In this study, we used a fast-growing Pacific oyster (Crassostrea gigas) variety “Haida No.1
Autor:
Yasuo Nambo, Harutaka Murase, Noritoshi Kawate, Munkhtuul Tsogtgerel, M.A. Hannan, Fumio Sato
Publikováno v:
Theriogenology. 132:212-217
The peripheral blood concentrations of insulin-like peptide 3 (INSL3) have been detected in many mammalian species, but the level of INSL3 in horse remains unknown. The objectives were to develop a time-resolved fluorescence immunoassay (TRFIA) to de
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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In insects, the insulin receptor (InR) pathway is involved in regulating key physiological processes, including juvenile hormone (JH) synthesis, vitellogenin production, and oocyte growth. This raises the question about which ligand (or ligands) bind