ライフサイエンスコーパス: follitropin

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1 a manner that explains how substitutions in follitropin and thyrotropin receptors distant from their

2 assembly of human choriogonadotropin, human follitropin, and human thyrotropin heterodimers occurs i

3 r with the pituitary hormones lutropin (LH), follitropin, and thyrotropin constitute the family of gl

4 We assembled models of lutropin, follitropin, and thyrotropin receptors by aligning model

5 e the hormone to distinguish lutropin (LHR), follitropin, and thyrotropin receptors.

6 sequence during the divergence of lutropins, follitropins, and thyrotropins and the speciation of tel

7 etically fused to either the common alpha or follitropin beta subunits, O-glycosylation was observed.

8 ides of hFSHR ECD primary sequence abolished follitropin binding primarily in the region of amino aci

9 (CG), thyrotropin (TSH), lutropin (LH), and follitropin (FSH) are heterodimers, composed of a common

10 the secretion profiles of lutropin (LH) and follitropin (FSH) differ.

11 Lutropin (LH) and follitropin (FSH) receptors belong to a group of leucine

12 Human thyrotropin (TSH), luteotropin (LH), follitropin (FSH), and chorionic gonadotropin are member

13 ontiguous residues of the lutropin (LHR) and follitropin (FSHR) receptors that dictate their rates of

14 human chorionic gonadotropin (hCG) and human follitropin (hFSH), that exhibit activity unique to a th

15 ptor (rFSHR) internalize agonist (i.e. human follitropin, hFSH) at a rate similar to that of other ag

16 pin (CG) and the anterior pituitary hormones follitropin, lutropin, and thyrotropin.

17 Follitropin, or follicle-stimulating hormone (FSH) recep

18 mutations of the structurally related human follitropin receptor (hFSHR) have been identified.

19 We have previously shown that the rat follitropin receptor (rFSHR) expressed in transfected ce

20 kidney (293) cells transfected with the rat follitropin receptor (rFSHR) internalize agonist (i.e. h

21 The rat follitropin receptor (rFSHR) is an unusual G protein-cou

22 acid sequences of the human (h) and rat (r) follitropin receptors (FSHR) are approximately 89% ident

23 e short SSDs in marmoset lutropin and salmon follitropin receptors have KH domain folds.

24 HRs, but not the closely related lutropin or follitropin receptors, exhibit persistent cAMP signaling

25 o to its ability to distinguish lutropin and follitropin receptors.

26 all vertebrate hormones except some teleost follitropins (teFSH), wherein it is latched to a cystein

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