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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Immunoglobulin superfamily, member 1'''<ref name="OMIM Entry 300137">{{cite web | title = Entry 300137: Immunoglobulin superfamily, member 1; IGSF1| url = http://omim.org/entry/300137| accessdate = }}</ref> is a plasma membrane glyco[[protein]] encoded by the ''IGSF1'' [[gene]],<ref name="pmid9521868">{{cite journal | vauthors = Mazzarella R, Pengue G, Jones J, Jones C, Schlessinger D | title = Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in Xq25 | journal = Genomics | volume = 48 | issue = 2 | pages = 157–62 | date = Mar 1998 | pmid = 9521868 | pmc =  | doi = 10.1006/geno.1997.5156 }}</ref><ref name="pmid9729118">{{cite journal | vauthors = Frattini A, Faranda S, Redolfi E, Allavena P, Vezzoni P | title = Identification and genomic organization of a gene coding for a new member of the cell adhesion molecule family mapping to Xq25 | journal = Gene | volume = 214 | issue = 1–2 | pages = 1–6 | date = Jul 1998 | pmid = 9729118 | pmc =  | doi = 10.1016/S0378-1119(98)00253-4 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: IGSF1 immunoglobulin superfamily, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3547| accessdate = }}</ref> which maps to the [[X chromosome]] in humans and other mammalian species.
| update_page = yes
| require_manual_inspection = no
| 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. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Immunoglobulin superfamily, member 1
| HGNCid = 5948
| Symbol = IGSF1
| AltSymbols =; IGCD1; IGDC1; INHBP; KIAA0364; MGC75490; PGSF2
| OMIM = 300137
| ECnumber = 
| Homologene = 1195
| MGIid = 2147913
| GeneAtlas_image1 = PBB_GE_IGSF1_207695_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0048186 |text = inhibin beta-A binding}} {{GNF_GO|id=GO:0048187 |text = inhibin beta-B binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3547
    | Hs_Ensembl = ENSG00000147255
    | Hs_RefseqProtein = NP_001546
    | Hs_RefseqmRNA = NM_001555
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 130235161
    | Hs_GenLoc_end = 130361358
    | Hs_Uniprot = 
    | Mm_EntrezGene = 209268
    | Mm_Ensembl = ENSMUSG00000031111
    | Mm_RefseqmRNA = NM_177591
    | Mm_RefseqProtein = NP_808259
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 46027171
    | Mm_GenLoc_end = 46042366
    | Mm_Uniprot = 
  }}
}}
'''Immunoglobulin superfamily, member 1''', also known as '''IGSF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IGSF1 immunoglobulin superfamily, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3547| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
IGSF1's function in normal cells is unresolved.  The protein is a member of the [[Immunoglobulin superfamily|immunoglobulin (Ig) superfamily]]. It was predicted to contain 12 Ig loops, a transmembrane domain, and a short cytoplasmic tail. However, during translation of the [[Protein biosynthesis|protein]], it is cleaved into [[N-terminus|amino-]] and [[C-terminus|carboxy-]]terminal domains (NTD and CTD, respectively).<ref name="pmid18981173">{{cite journal | vauthors = Robakis T, Bak B, Lin SH, Bernard DJ, Scheiffele P | title = An internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain protein | journal = The Journal of Biological Chemistry | volume = 283 | issue = 52 | pages = 36369–76 | date = Dec 2008 | pmid = 18981173 | pmc = 2662301 | doi = 10.1074/jbc.M807527200 }}</ref> Only the CTD is trafficked to the [[Cell membrane|plasma membrane]]. The NTD is trapped within the [[Endoplasmic reticulum|endoplasmic reticulum (ER)]]. Pathogenic mutations in the ''IGSF1'' gene block the transport of the CTD to the plasma membrane.
{{PBB_Summary
| section_title =
| summary_text = Members of the immunoglobulin (Ig) superfamily (see MIM 147100), which includes IGSF1, have a variety of functions, but all appear to play a role in cell recognition and the regulation of cell behavior.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: IGSF1 immunoglobulin superfamily, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3547| accessdate = }}</ref>
}}


==References==
== Clinical Relevance ==
{{reflist|2}}
 
==Further reading==
Mutations in ''IGSF1'' cause a condition called IGSF1 deficiency syndrome<ref name="pmid23143598">{{cite journal | vauthors = Sun Y, Bak B, Schoenmakers N, van Trotsenburg AS, Oostdijk W, Voshol P, Cambridge E, White JK, le Tissier P, Gharavy SN, Martinez-Barbera JP, Stokvis-Brantsma WH, Vulsma T, Kempers MJ, Persani L, Campi I, Bonomi M, Beck-Peccoz P, Zhu H, Davis TM, Hokken-Koelega AC, Del Blanco DG, Rangasami JJ, Ruivenkamp CA, Laros JF, Kriek M, Kant SG, Bosch CA, Biermasz NR, Appelman-Dijkstra NM, Corssmit EP, Hovens GC, Pereira AM, den Dunnen JT, Wade MG, Breuning MH, Hennekam RC, Chatterjee K, Dattani MT, Wit JM, Bernard DJ | title = Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central hypothyroidism and testicular enlargement | journal = Nature Genetics | volume = 44 | issue = 12 | pages = 1375–81 | date = Dec 2012 | pmid = 23143598 | pmc = 3511587 | doi = 10.1038/ng.2453 }}</ref> or central hypothyroidism/testicular enlargement (CHTE<ref name="OMIM Entry 300888">{{cite web | title = Entry 300888: Hypothyroidism, central, and testicular enlargement; CHTE| url = http://omim.org/entry/300888| accessdate = }}</ref>). The condition, which affects an estimated 1:100,000 people,<ref name="pmid25002994">{{cite journal | vauthors = Joustra SD, van Trotsenburg AS, Sun Y, Losekoot M, Bernard DJ, Biermasz NR, Oostdijk W, Wit JM | title = IGSF1 deficiency syndrome: A newly uncovered endocrinopathy | journal = Rare Diseases | volume = 1 | issue = 1 | date = May 2013 | pmid = 25002994 | pmc = 3915563 | doi = 10.4161/rdis.24883 | pages=e24883}}</ref> is more common in males than females. Most affected males are discovered through neonatal screening for [[hypothyroidism]]. The extent of hypothyroidism is variable, but most male cases require treatment with thyroid hormone replacement. Males with IGSF1 deficiency exhibit enlarged testicles (also known as [[macroorchidism]]) and a delay in the development of secondary sexual characteristics. Post-pubertally, there is no evidence of impaired fertility in these men.
 
The ''IGSF1'' gene is also active in the brain and in the developing liver. It can also become reactivated in liver cancer (hepatocellular carcinoma).<ref name="pmid15735714">{{cite journal | vauthors = Patil MA, Chua MS, Pan KH, Lin R, Lih CJ, Cheung ST, Ho C, Li R, Fan ST, Cohen SN, Chen X, So S | title = An integrated data analysis approach to characterize genes highly expressed in hepatocellular carcinoma | journal = Oncogene | volume = 24 | issue = 23 | pages = 3737–47 | date = May 2005 | pmid = 15735714 | pmc =  | doi = 10.1038/sj.onc.1208479 }}</ref>
 
== Animal Model ==
 
Mice lacking a functional ''Igsf1'' gene similarly exhibit hypothyroidism of central origin.<ref name="pmid23143598"/> The ''IGSF1'' gene is particularly active in the [[pituitary gland]]. The pituitary synthesizes and secretes [[Thyroid stimulating hormone|thyroid-stimulating hormone (TSH)]]. TSH, in turn, stimulates production of the [[thyroid hormone]]s, thyroxine and triiodothyronine, by the [[Thyroid|thyroid gland]]. TSH secretion is controlled by [[Thyrotropin-releasing hormone|thyrotropin-releasing hormone (TRH)]], which is released by neurons in the hypothalamus of the brain. In ''Igsf1'' deficient mice, the receptor for TRH is downregulated in the pituitary.<ref name="pmid23143598"/> This decrease could explain, at least in part, the central hypothyroidism observed in both humans and mice with IGSF1 deficiency. How the loss of IGSF1 causes a decrease in TRH receptors is presently unknown.
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Chapman SC, Woodruff TK | title = Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP) | journal = Molecular Endocrinology | volume = 15 | issue = 4 | pages = 668–79 | date = Apr 2001 | pmid = 11266516 | doi = 10.1210/me.15.4.668 }}
| citations =
* {{cite journal | vauthors = Tanaka S, Tatsumi K, Okubo K, Itoh K, Kawamoto S, Matsubara K, Amino N | title = Expression profile of active genes in the human pituitary gland | journal = Journal of Molecular Endocrinology | volume = 28 | issue = 1 | pages = 33–44 | date = Feb 2002 | pmid = 11854097 | doi = 10.1677/jme.0.0280033 }}
*{{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 = Bernard DJ, Burns KH, Haupt B, Matzuk MM, Woodruff TK | title = Normal reproductive function in InhBP/p120-deficient mice | journal = Molecular and Cellular Biology | volume = 23 | issue = 14 | pages = 4882–91 | date = Jul 2003 | pmid = 12832474 | doi=10.1128/mcb.23.14.4882-4891.2003 | pmc=162213}}
*{{cite journal  | author=Nagase T, Ishikawa K, Nakajima D, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 2 |pages= 141-50 |year= 1997 |pmid= 9205841 |doi=  }}
* {{cite journal | vauthors = Tajima T, Nakamura A, Ishizu K | title = A novel mutation of IGSF1 in a Japanese patient of congenital central hypothyroidism without macroorchidism | journal = Endocrine Journal | volume = 60 | issue = 2 | pages = 245–9 | year = 2013 | pmid = 23363888 | doi=10.1210/jc.2013-1224}}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
* {{cite journal | vauthors = Tajima T, Nakamura A, Ishizu K | title = A novel mutation of IGSF1 in a Japanese patient of congenital central hypothyroidism without macroorchidism | journal = Endocrine Journal | volume = 60 | issue = 2 | pages = E1682–91 | year = 2013 | pmid = 23363888 | doi = 10.1210/jc.2013-1224 }}
*{{cite journal  | author=Mazzarella R, Pengue G, Jones J, ''et al.'' |title=Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in Xq25. |journal=Genomics |volume=48 |issue= 2 |pages= 157-62 |year= 1998 |pmid= 9521868 |doi= 10.1006/geno.1997.5156 }}
* {{cite journal | vauthors = Joustra SD, Schoenmakers N, Persani L, Campi I, Bonomi M, Radetti G, Beck-Peccoz P, Zhu H, Davis TM, Sun Y, Corssmit EP, Appelman-Dijkstra NM, Heinen CA, Pereira AM, Varewijck AJ, Janssen JA, Endert E, Hennekam RC, Lombardi MP, Mannens MM, Bak B, Bernard DJ, Breuning MH, Chatterjee K, Dattani MT, Oostdijk W, Biermasz NR, Wit JM, van Trotsenburg AS | title = The IGSF1 deficiency syndrome: characteristics of male and female patients | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 98 | issue = 12 | pages = 4942–52 | date = Dec 2013 | pmid = 24108313 | doi = 10.1210/jc.2013-2743 }}
*{{cite journal  | author=Frattini A, Faranda S, Redolfi E, ''et al.'' |title=Identification and genomic organization of a gene coding for a new member of the cell adhesion molecule family mapping to Xq25. |journal=Gene |volume=214 |issue= 1-2 |pages= 1-6 |year= 1998 |pmid= 9729118 |doi=  }}
* {{cite journal | vauthors = Tajima T, Nakamura A, Morikawa S, Ishizu K | title = Neonatal screening and a new cause of congenital central hypothyroidism | journal = Annals of Pediatric Endocrinology & Metabolism | volume = 19 | issue = 3 | pages = 117–21 | date = Sep 2014 | pmid = 25346914 | doi = 10.6065/apem.2014.19.3.117 | pmc=4208260}}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
* {{cite journal | vauthors = Reynaert N, Braat E, de Zegher F | title = Congenital nystagmus and central hypothyroidism | journal = International Journal of Pediatric Endocrinology | volume = 2015 | issue = 1 | pages = 7 | year = 2015 | pmid = 25780367 | doi = 10.1186/s13633-015-0003-5 | pmc=4360929}}
*{{cite journal  | author=Chapman SC, Woodruff TK |title=Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP). |journal=Mol. Endocrinol. |volume=15 |issue= 4 |pages= 668-79 |year= 2001 |pmid= 11266516 |doi= }}
*{{cite journal  | author=Gui Y, Murphy LJ |title=Insulin-like growth factor (IGF)-binding protein-3 (IGFBP-3) binds to fibronectin (FN): demonstration of IGF-I/IGFBP-3/fn ternary complexes in human plasma. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 5 |pages= 2104-10 |year= 2001 |pmid= 11344214 |doi=  }}
*{{cite journal  | author=Kushlinskii NE, Britvin TA, Polyakova GA, ''et al.'' |title=Soluble Fas antigen (sFAS) in the serum from patients with adrenal tumors. |journal=Bull. Exp. Biol. Med. |volume=132 |issue= 4 |pages= 990-2 |year= 2002 |pmid= 11782802 |doi=  }}
*{{cite journal | author=Tanaka S, Tatsumi K, Okubo K, ''et al.'' |title=Expression profile of active genes in the human pituitary gland. |journal=J. Mol. Endocrinol. |volume=28 |issue= 1 |pages= 33-44 |year= 2002 |pmid= 11854097 |doi= }}
*{{cite journal | author=Aschkenazi S, Straszewski S, Verwer KM, ''et al.'' |title=Differential regulation and function of the Fas/Fas ligand system in human trophoblast cells. |journal=Biol. Reprod. |volume=66 |issue= 6 |pages= 1853-61 |year= 2003 |pmid= 12021072 |doi= }}
*{{cite journal  | author=Nat R, Radu E, Regalia T, Popescu LM |title=Apoptosis in human embryo development: 3. Fas-induced apoptosis in brain primary cultures. |journal=J. Cell. Mol. Med. |volume=5 |issue= 4 |pages= 417-28 |year= 2002 |pmid= 12067476 |doi=  }}
*{{cite journal | author=Fujita T, Maruyama M, Araya J, ''et al.'' |title=Hydrogen peroxide induces upregulation of Fas in human airway epithelial cells via the activation of PARP-p53 pathway. |journal=Am. J. Respir. Cell Mol. Biol. |volume=27 |issue= 5 |pages= 542-52 |year= 2002 |pmid= 12397013 |doi= }}
*{{cite journal  | author=Albertine KH, Soulier MF, Wang Z, ''et al.'' |title=Fas and fas ligand are up-regulated in pulmonary edema fluid and lung tissue of patients with acute lung injury and the acute respiratory distress syndrome. |journal=Am. J. Pathol. |volume=161 |issue= 5 |pages= 1783-96 |year= 2002 |pmid= 12414525 |doi=  }}
*{{cite journal | author=Nakayama M, Kikuno R, Ohara O |title=Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. |journal=Genome Res. |volume=12 |issue= 11 |pages= 1773-84 |year= 2003 |pmid= 12421765 |doi= 10.1101/gr.406902 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Ivanov VN, Lopez Bergami P, Maulit G, ''et al.'' |title=FAP-1 association with Fas (Apo-1) inhibits Fas expression on the cell surface. |journal=Mol. Cell. Biol. |volume=23 |issue= 10 |pages= 3623-35 |year= 2003 |pmid= 12724420 |doi=  }}
*{{cite journal | author=Bilinska M, Frydecka I, Podemski R, Gruszka E |title=Fas expression on T cells and sFas in relapsing-remitting multiple sclerosis. |journal=Acta Neurol. Scand. |volume=107 |issue= 6 |pages= 387-93 |year= 2003 |pmid= 12757469 |doi= }}
*{{cite journal  | author=Strauss G, Knape I, Melzner I, Debatin KM |title=Constitutive caspase activation and impaired death-inducing signaling complex formation in CD95-resistant, long-term activated, antigen-specific T cells. |journal=J. Immunol. |volume=171 |issue= 3 |pages= 1172-82 |year= 2003 |pmid= 12874203 |doi=  }}
*{{cite journal | author=Marsik C, Halama T, Cardona F, ''et al.'' |title=Regulation of Fas (APO-1, CD95) and Fas ligand expression in leukocytes during systemic inflammation in humans. |journal=Shock |volume=20 |issue= 6 |pages= 493-6 |year= 2004 |pmid= 14625471 |doi= 10.1097/01.shk.0000097248.97298.ea }}
}}
{{refend}}
{{refend}}


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Latest revision as of 05:42, 12 January 2019

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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

Immunoglobulin superfamily, member 1[1] is a plasma membrane glycoprotein encoded by the IGSF1 gene,[2][3][4] which maps to the X chromosome in humans and other mammalian species.

Function

IGSF1's function in normal cells is unresolved. The protein is a member of the immunoglobulin (Ig) superfamily. It was predicted to contain 12 Ig loops, a transmembrane domain, and a short cytoplasmic tail. However, during translation of the protein, it is cleaved into amino- and carboxy-terminal domains (NTD and CTD, respectively).[5] Only the CTD is trafficked to the plasma membrane. The NTD is trapped within the endoplasmic reticulum (ER). Pathogenic mutations in the IGSF1 gene block the transport of the CTD to the plasma membrane.

Clinical Relevance

Mutations in IGSF1 cause a condition called IGSF1 deficiency syndrome[6] or central hypothyroidism/testicular enlargement (CHTE[7]). The condition, which affects an estimated 1:100,000 people,[8] is more common in males than females. Most affected males are discovered through neonatal screening for hypothyroidism. The extent of hypothyroidism is variable, but most male cases require treatment with thyroid hormone replacement. Males with IGSF1 deficiency exhibit enlarged testicles (also known as macroorchidism) and a delay in the development of secondary sexual characteristics. Post-pubertally, there is no evidence of impaired fertility in these men.

The IGSF1 gene is also active in the brain and in the developing liver. It can also become reactivated in liver cancer (hepatocellular carcinoma).[9]

Animal Model

Mice lacking a functional Igsf1 gene similarly exhibit hypothyroidism of central origin.[6] The IGSF1 gene is particularly active in the pituitary gland. The pituitary synthesizes and secretes thyroid-stimulating hormone (TSH). TSH, in turn, stimulates production of the thyroid hormones, thyroxine and triiodothyronine, by the thyroid gland. TSH secretion is controlled by thyrotropin-releasing hormone (TRH), which is released by neurons in the hypothalamus of the brain. In Igsf1 deficient mice, the receptor for TRH is downregulated in the pituitary.[6] This decrease could explain, at least in part, the central hypothyroidism observed in both humans and mice with IGSF1 deficiency. How the loss of IGSF1 causes a decrease in TRH receptors is presently unknown.

References

  1. ↑ "Entry 300137: Immunoglobulin superfamily, member 1; IGSF1".
  2. ↑ Mazzarella R, Pengue G, Jones J, Jones C, Schlessinger D (Mar 1998). "Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in Xq25". Genomics. 48 (2): 157–62. doi:10.1006/geno.1997.5156. PMID 9521868.
  3. ↑ Frattini A, Faranda S, Redolfi E, Allavena P, Vezzoni P (Jul 1998). "Identification and genomic organization of a gene coding for a new member of the cell adhesion molecule family mapping to Xq25". Gene. 214 (1–2): 1–6. doi:10.1016/S0378-1119(98)00253-4. PMID 9729118.
  4. ↑ "Entrez Gene: IGSF1 immunoglobulin superfamily, member 1".
  5. ↑ Robakis T, Bak B, Lin SH, Bernard DJ, Scheiffele P (Dec 2008). "An internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain protein". The Journal of Biological Chemistry. 283 (52): 36369–76. doi:10.1074/jbc.M807527200. PMC 2662301. PMID 18981173.
  6. ↑ 6.0 6.1 6.2 Sun Y, Bak B, Schoenmakers N, van Trotsenburg AS, Oostdijk W, Voshol P, Cambridge E, White JK, le Tissier P, Gharavy SN, Martinez-Barbera JP, Stokvis-Brantsma WH, Vulsma T, Kempers MJ, Persani L, Campi I, Bonomi M, Beck-Peccoz P, Zhu H, Davis TM, Hokken-Koelega AC, Del Blanco DG, Rangasami JJ, Ruivenkamp CA, Laros JF, Kriek M, Kant SG, Bosch CA, Biermasz NR, Appelman-Dijkstra NM, Corssmit EP, Hovens GC, Pereira AM, den Dunnen JT, Wade MG, Breuning MH, Hennekam RC, Chatterjee K, Dattani MT, Wit JM, Bernard DJ (Dec 2012). "Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central hypothyroidism and testicular enlargement". Nature Genetics. 44 (12): 1375–81. doi:10.1038/ng.2453. PMC 3511587. PMID 23143598.
  7. ↑ "Entry 300888: Hypothyroidism, central, and testicular enlargement; CHTE".
  8. ↑ Joustra SD, van Trotsenburg AS, Sun Y, Losekoot M, Bernard DJ, Biermasz NR, Oostdijk W, Wit JM (May 2013). "IGSF1 deficiency syndrome: A newly uncovered endocrinopathy". Rare Diseases. 1 (1): e24883. doi:10.4161/rdis.24883. PMC 3915563. PMID 25002994.
  9. ↑ Patil MA, Chua MS, Pan KH, Lin R, Lih CJ, Cheung ST, Ho C, Li R, Fan ST, Cohen SN, Chen X, So S (May 2005). "An integrated data analysis approach to characterize genes highly expressed in hepatocellular carcinoma". Oncogene. 24 (23): 3737–47. doi:10.1038/sj.onc.1208479. PMID 15735714.

Further reading


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