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{{Infobox_gene}}
{{PBB_Controls
'''Inhibin, beta A''', also known as '''INHBA''', is a [[protein]] which in humans is encoded by the ''INHBA'' [[gene]].<ref name="pmid3345731">{{cite journal |vauthors=Burger HG, Igarashi M | title = Inhibin: definition and nomenclature, including related substances | journal = Endocrinology | volume = 122 | issue = 4 | pages = 1701–2 | date=April 1988| pmid = 3345731 | doi = 10.1210/endo-122-4-1701| url = | issn = }}</ref> INHBA is a subunit of both [[activin and inhibin]], two closely related glycoproteins with opposing biological effects.
| update_page = yes
 
| require_manual_inspection = no
== Function ==
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The inhibin beta A subunit joins the alpha subunit to form a pituitary [[follicle-stimulating hormone|FSH]] secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.<ref>{{cite web | title = Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3624| accessdate = }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_INHBA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nys.
| PDB = {{PDB2|1nys}}, {{PDB2|1nyu}}, {{PDB2|1s4y}}, {{PDB2|2arp}}, {{PDB2|2arv}}, {{PDB2|2b0u}}, {{PDB2|2p6a}}
| Name = Inhibin, beta A (activin A, activin AB alpha polypeptide)
| HGNCid = 6066
| Symbol = INHBA
| AltSymbols =; EDF; FRP
| OMIM = 147290
| ECnumber = 
| Homologene = 1653
| MGIid = 96570
| GeneAtlas_image1 = PBB_GE_INHBA_210511_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_INHBA_204926_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0017106 |text = activin inhibitor activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0048184 |text = follistatin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0043509 |text = activin A complex}} {{GNF_GO|id=GO:0043512 |text = inhibin A complex}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030218 |text = erythrocyte differentiation}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0042326 |text = negative regulation of phosphorylation}} {{GNF_GO|id=GO:0042541 |text = hemoglobin biosynthetic process}} {{GNF_GO|id=GO:0045077 |text = negative regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0045578 |text = negative regulation of B cell differentiation}} {{GNF_GO|id=GO:0045648 |text = positive regulation of erythrocyte differentiation}} {{GNF_GO|id=GO:0045650 |text = negative regulation of macrophage differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046881 |text = positive regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0046882 |text = negative regulation of follicle-stimulating hormone secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3624
    | Hs_Ensembl = ENSG00000122641
    | Hs_RefseqProtein = NP_002183
    | Hs_RefseqmRNA = NM_002192
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 41695126
    | Hs_GenLoc_end = 41709231
    | Hs_Uniprot = P08476
    | Mm_EntrezGene = 16323
    | Mm_Ensembl = ENSMUSG00000041324
    | Mm_RefseqmRNA = NM_008380
    | Mm_RefseqProtein = NP_032406
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 15805370
    | Mm_GenLoc_end = 15818147
    | Mm_Uniprot = Q3UXL8
  }}
}}
'''Inhibin, beta A (activin A, activin AB alpha polypeptide)''', also known as '''INHBA''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
INHBA has been shown to [[Protein-protein interaction|interact]] with [[ACVR2A]].<ref name=pmid10746731>{{cite journal |last=Lewis |first=K A |authorlink= |author2=Gray P C |author3=Blount A L |author4=MacConell L A |author5=Wiater E |author6=Bilezikjian L M |author7=Vale W  |date=March 2000|title=Betaglycan binds inhibin and can mediate functional antagonism of activin signalling |journal=[[Nature (journal)|Nature]] |volume=404 |issue=6776 |pages=411–4 |publisher= |location = ENGLAND| issn = 0028-0836| pmid = 10746731 |doi = 10.1038/35006129 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9202237>{{cite journal |last=Martens |first=J W |authorlink= |author2=de Winter J P |author3=Timmerman M A |author4=McLuskey A |author5=van Schaik R H |author6=Themmen A P |author7=de Jong F H  |date=July 1997|title=Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells |journal=[[Endocrinology (journal)|Endocrinology]] |volume=138 |issue=7 |pages=2928–36 |publisher= |location = UNITED STATES| issn = 0013-7227| pmid = 9202237 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1210/endo.138.7.5250 }}</ref>
| section_title =  
| summary_text = The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.<ref>{{cite web | title = Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3624| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal | author=Munz B, Hübner G, Tretter Y, ''et al.'' |title=A novel role of activin in inflammation and repair. |journal=J. Endocrinol. |volume=161 |issue= 2 |pages= 187-93 |year= 1999 |pmid= 10320815 |doi=  }}
*{{cite journal   |vauthors=Munz B, Hübner G, Tretter Y, etal |title=A novel role of activin in inflammation and repair. |journal=J. Endocrinol. |volume=161 |issue= 2 |pages= 187–93 |year= 1999 |pmid= 10320815 |doi=10.1677/joe.0.1610187 }}
*{{cite journal  | author=Welt C, Sidis Y, Keutmann H, Schneyer A |title=Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 724-52 |year= 2002 |pmid= 12324653 |doi=  }}
*{{cite journal  |vauthors=Welt C, Sidis Y, Keutmann H, Schneyer A |title=Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 724–52 |year= 2002 |pmid= 12324653 |doi=  }}
*{{cite journal  | author=Shav-Tal Y, Zipori D |title=The role of activin a in regulation of hemopoiesis. |journal=Stem Cells |volume=20 |issue= 6 |pages= 493-500 |year= 2003 |pmid= 12456957 |doi= }}
*{{cite journal  |vauthors=Shav-Tal Y, Zipori D |title=The role of activin a in regulation of hemopoiesis. |journal=Stem Cells |volume=20 |issue= 6 |pages= 493–500 |year= 2003 |pmid= 12456957 |doi=10.1634/stemcells.20-6-493  }}
*{{cite journal | author=Reis FM, Luisi S, Carneiro MM, ''et al.'' |title=Activin, inhibin and the human breast. |journal=Mol. Cell. Endocrinol. |volume=225 |issue= 1-2 |pages= 77-82 |year= 2005 |pmid= 15451571 |doi= 10.1016/j.mce.2004.02.016 }}
*{{cite journal   |vauthors=Reis FM, Luisi S, Carneiro MM, etal |title=Activin, inhibin and the human breast. |journal=Mol. Cell. Endocrinol. |volume=225 |issue= 1–2 |pages= 77–82 |year= 2005 |pmid= 15451571 |doi= 10.1016/j.mce.2004.02.016 }}
*{{cite journal | author=Shao L, Frigon NL, Young AL, ''et al.'' |title=Effect of activin A on globin gene expression in purified human erythroid progenitors. |journal=Blood |volume=79 |issue= 3 |pages= 773-81 |year= 1992 |pmid= 1310063 |doi=  }}
*{{cite journal   |vauthors=Shao L, Frigon NL, Young AL, etal |title=Effect of activin A on globin gene expression in purified human erythroid progenitors |journal=Blood |volume=79 |issue= 3 |pages= 773–81 |year= 1992 |pmid= 1310063 |doi=  }}
*{{cite journal  | author=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase. |journal=Cell |volume=65 |issue= 6 |pages= 973-82 |year= 1991 |pmid= 1646080 |doi=  }}
*{{cite journal  |vauthors=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase |journal=Cell |volume=65 |issue= 6 |pages= 973–82 |year= 1991 |pmid= 1646080 |doi=10.1016/0092-8674(91)90549-E }}
*{{cite journal | author=Tanimoto K, Handa S, Ueno N, ''et al.'' |title=Structure and sequence analysis of the human activin beta A subunit gene. |journal=DNA Seq. |volume=2 |issue= 2 |pages= 103-10 |year= 1992 |pmid= 1777673 |doi=  }}
*{{cite journal   |vauthors=Tanimoto K, Handa S, Ueno N, etal |title=Structure and sequence analysis of the human activin beta A subunit gene |journal=DNA Seq. |volume=2 |issue= 2 |pages= 103–10 |year= 1992 |pmid= 1777673 |doi=10.3109/10425179109039678 }}
*{{cite journal  | author=Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH |title=Activin B: precursor sequences, genomic structure and in vitro activities. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1352-8 |year= 1990 |pmid= 2575216 |doi=  }}
*{{cite journal  |vauthors=Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH |title=Activin B: precursor sequences, genomic structure and in vitro activities |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1352–8 |year= 1990 |pmid= 2575216 |doi=10.1210/mend-3-9-1352 }}
*{{cite journal | author=Barton DE, Yang-Feng TL, Mason AJ, ''et al.'' |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice. |journal=Genomics |volume=5 |issue= 1 |pages= 91-9 |year= 1989 |pmid= 2767687 |doi=  }}
*{{cite journal   |vauthors=Barton DE, Yang-Feng TL, Mason AJ, etal |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice |journal=Genomics |volume=5 |issue= 1 |pages= 91–9 |year= 1989 |pmid= 2767687 |doi=10.1016/0888-7543(89)90091-8 }}
*{{cite journal | author=Murata M, Eto Y, Shibai H, ''et al.'' |title=Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2434-8 |year= 1988 |pmid= 3267209 |doi=  }}
*{{cite journal   |vauthors=Murata M, Eto Y, Shibai H, etal |title=Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2434–8 |year= 1988 |pmid= 3267209 |doi=10.1073/pnas.85.8.2434  | pmc=280011 |bibcode=1988PNAS...85.2434M }}
*{{cite journal  | author=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances. |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701-2 |year= 1988 |pmid= 3345731 |doi=  }}
*{{cite journal  |vauthors=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701–2 |year= 1988 |pmid= 3345731 |doi=10.1210/endo-122-4-1701 }}
*{{cite journal  | author=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957-64 |year= 1986 |pmid= 3754442 |doi=  }}
*{{cite journal  |vauthors=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957–64 |year= 1986 |pmid= 3754442 |doi=10.1016/0006-291X(86)91021-1 }}
*{{cite journal | author=Stewart AG, Milborrow HM, Ring JM, ''et al.'' |title=Human inhibin genes. Genomic characterisation and sequencing. |journal=FEBS Lett. |volume=206 |issue= 2 |pages= 329-34 |year= 1986 |pmid= 3758355 |doi=  }}
*{{cite journal   |vauthors=Stewart AG, Milborrow HM, Ring JM, etal |title=Human inhibin genes. Genomic characterisation and sequencing |journal=FEBS Lett. |volume=206 |issue= 2 |pages= 329–34 |year= 1986 |pmid= 3758355 |doi=10.1016/0014-5793(86)81006-7 }}
*{{cite journal | author=Sumitomo S, Inouye S, Liu XJ, ''et al.'' |title=The heparin binding site of follistatin is involved in its interaction with activin. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 1-9 |year= 1995 |pmid= 7887917 |doi= 10.1006/bbrc.1995.1297 }}
*{{cite journal   |vauthors=Sumitomo S, Inouye S, Liu XJ, etal |title=The heparin binding site of follistatin is involved in its interaction with activin |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 1–9 |year= 1995 |pmid= 7887917 |doi= 10.1006/bbrc.1995.1297 }}
*{{cite journal  | author=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308-13 |year= 1995 |pmid= 7890768 |doi=  }}
*{{cite journal  |vauthors=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308–13 |year= 1995 |pmid= 7890768 |doi=10.1074/jbc.270.11.6308 }}
*{{cite journal  | author=Mason AJ |title=Functional analysis of the cysteine residues of activin A. |journal=Mol. Endocrinol. |volume=8 |issue= 3 |pages= 325-32 |year= 1994 |pmid= 8015550 |doi= }}
*{{cite journal  | author=Mason AJ |title=Functional analysis of the cysteine residues of activin A |journal=Mol. Endocrinol. |volume=8 |issue= 3 |pages= 325–32 |year= 1994 |pmid= 8015550 |doi=10.1210/me.8.3.325  }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Nishihara T, Okahashi N, Ueda N |title=Activin A induces apoptotic cell death. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 985-91 |year= 1994 |pmid= 8267637 |doi= 10.1006/bbrc.1993.2576 }}
*{{cite journal  |vauthors=Nishihara T, Okahashi N, Ueda N |title=Activin A induces apoptotic cell death |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 985–91 |year= 1994 |pmid= 8267637 |doi= 10.1006/bbrc.1993.2576 }}
*{{cite journal | author=ten Dijke P, Ichijo H, Franzén P, ''et al.'' |title=Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity. |journal=Oncogene |volume=8 |issue= 10 |pages= 2879-87 |year= 1993 |pmid= 8397373 |doi=  }}
*{{cite journal   |vauthors=ten Dijke P, Ichijo H, Franzén P, etal |title=Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity |journal=Oncogene |volume=8 |issue= 10 |pages= 2879–87 |year= 1993 |pmid= 8397373 |doi=  }}
*{{cite journal | author=Tanimoto K, Yoshida E, Mita S, ''et al.'' |title=Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32760-9 |year= 1997 |pmid= 8955111 |doi=  }}
*{{cite journal   |vauthors=Tanimoto K, Yoshida E, Mita S, etal |title=Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32760–9 |year= 1997 |pmid= 8955111 |doi=10.1074/jbc.271.51.32760 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{TGFβ receptor superfamily modulators}}
{{WikiDoc Sources}}
{{PDB Gallery|geneid=3624}}
 
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{{PBB_Controls
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[[sr:INHBB]]

Latest revision as of 00:41, 24 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene.[1] INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

Function

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.[2]

Interactions

INHBA has been shown to interact with ACVR2A.[3][4]

References

  1. ↑ Burger HG, Igarashi M (April 1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
  2. ↑ "Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)".
  3. ↑ Lewis, K A; Gray P C; Blount A L; MacConell L A; Wiater E; Bilezikjian L M; Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. ENGLAND. 404 (6776): 411–4. doi:10.1038/35006129. ISSN 0028-0836. PMID 10746731.
  4. ↑ Martens, J W; de Winter J P; Timmerman M A; McLuskey A; van Schaik R H; Themmen A P; de Jong F H (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". Endocrinology. UNITED STATES. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. ISSN 0013-7227. PMID 9202237.

Further reading


sr:INHBB

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