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Gene Information

Gene symbol: GPHB5

Gene name: glycoprotein hormone beta 5

HGNC ID: 18055

Synonyms: ZLUT1, GPB5

Related Genes

# Gene Symbol Number of hits
1 GPHA2 1 hits
2 IL1B 1 hits
3 NFKB1 1 hits
4 TNF 1 hits
5 TSHB 1 hits
6 TSHR 1 hits

Related Sentences

# PMID Sentence
1 18433898 Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5).
2 18433898 Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR).
3 18433898 Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5.
4 18433898 Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate.
5 18433898 The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSH beta.
6 18433898 Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5).
7 18433898 Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR).
8 18433898 Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5.
9 18433898 Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate.
10 18433898 The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSH beta.
11 18433898 Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5).
12 18433898 Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR).
13 18433898 Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5.
14 18433898 Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate.
15 18433898 The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSH beta.
16 18433898 Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5).
17 18433898 Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR).
18 18433898 Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5.
19 18433898 Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate.
20 18433898 The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSH beta.
21 18433898 Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5).
22 18433898 Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR).
23 18433898 Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5.
24 18433898 Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate.
25 18433898 The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSH beta.
26 19095738 We found that nuclear factor-kappaB (NF-kappaB) markedly activated GPB5 transcription.
27 19095738 Disruption of the putative NF-kappaB-binding motifs in the GPB5 5'-flanking region silenced the GPB5 activation by p65.
28 19095738 Because NF-kappaB is known to associate with acute phase inflammatory cytokines, we examined whether TNFalpha or IL-1beta could regulate GPB5.
29 19095738 Both these cytokines activated GPB5 transcription by 2- to 3-fold, and their effects were abolished by the addition of MG132, a NF-kappaB inhibitor.
30 19095738 We found that nuclear factor-kappaB (NF-kappaB) markedly activated GPB5 transcription.
31 19095738 Disruption of the putative NF-kappaB-binding motifs in the GPB5 5'-flanking region silenced the GPB5 activation by p65.
32 19095738 Because NF-kappaB is known to associate with acute phase inflammatory cytokines, we examined whether TNFalpha or IL-1beta could regulate GPB5.
33 19095738 Both these cytokines activated GPB5 transcription by 2- to 3-fold, and their effects were abolished by the addition of MG132, a NF-kappaB inhibitor.
34 19095738 We found that nuclear factor-kappaB (NF-kappaB) markedly activated GPB5 transcription.
35 19095738 Disruption of the putative NF-kappaB-binding motifs in the GPB5 5'-flanking region silenced the GPB5 activation by p65.
36 19095738 Because NF-kappaB is known to associate with acute phase inflammatory cytokines, we examined whether TNFalpha or IL-1beta could regulate GPB5.
37 19095738 Both these cytokines activated GPB5 transcription by 2- to 3-fold, and their effects were abolished by the addition of MG132, a NF-kappaB inhibitor.
38 19095738 We found that nuclear factor-kappaB (NF-kappaB) markedly activated GPB5 transcription.
39 19095738 Disruption of the putative NF-kappaB-binding motifs in the GPB5 5'-flanking region silenced the GPB5 activation by p65.
40 19095738 Because NF-kappaB is known to associate with acute phase inflammatory cytokines, we examined whether TNFalpha or IL-1beta could regulate GPB5.
41 19095738 Both these cytokines activated GPB5 transcription by 2- to 3-fold, and their effects were abolished by the addition of MG132, a NF-kappaB inhibitor.