Interferon gamma receptor 1

Interferon gamma receptor 1 (IFNGR1) also known as CD119 (Cluster of Differentiation 119), is a human gene.cite web | title = Entrez Gene: IFNGR1 interferon gamma receptor 1| url =| accessdate = ]

section_title =
summary_text = IFNGR1 encodes the ligand-binding chain (alpha) of the heterodimeric gamma interferon receptor, which is found on macrophages. IFNGR2 encodes the non-ligand-binding partner of the heterodimeric receptor.cite web | title = Entrez Gene: IFNGR1 interferon gamma receptor 1| url =| accessdate = ]

ee also

* Cluster of differentiation
* Interferon-gamma receptor


Further reading

citations =
*cite journal | author=Samuel CE |title=Antiviral actions of interferons. |journal=Clin. Microbiol. Rev. |volume=14 |issue= 4 |pages= 778–809, table of contents |year= 2002 |pmid= 11585785 |doi= 10.1128/CMR.14.4.778-809.2001
*cite journal | author=van Loon AP, Ozmen L, Fountoulakis M, "et al." |title=High-affinity receptor for interferon-gamma (IFN-gamma), a ubiquitous protein occurring in different molecular forms on human cells: blood monocytes and eleven different cell lines have the same IFN-gamma receptor protein. |journal=J. Leukoc. Biol. |volume=49 |issue= 5 |pages= 462–73 |year= 1991 |pmid= 1826725 |doi=
*cite journal | author=Le Coniat M, Alcaide-Loridan C, Fellous M, Berger R |title=Human interferon gamma receptor 1 (IFNGR1) gene maps to chromosome region 6q23-6q24. |journal=Hum. Genet. |volume=84 |issue= 1 |pages= 92–4 |year= 1990 |pmid= 2532616 |doi=
*cite journal | author=Novick D, Orchansky P, Revel M, Rubinstein M |title=The human interferon-gamma receptor. Purification, characterization, and preparation of antibodies. |journal=J. Biol. Chem. |volume=262 |issue= 18 |pages= 8483–7 |year= 1987 |pmid= 2954953 |doi=
*cite journal | author=Aguet M, Dembić Z, Merlin G |title=Molecular cloning and expression of the human interferon-gamma receptor. |journal=Cell |volume=55 |issue= 2 |pages= 273–80 |year= 1988 |pmid= 2971451 |doi=
*cite journal | author=Szente BE, Subramaniam PS, Johnson HM |title=Identification of IFN-gamma receptor binding sites for JAK2 and enhancement of binding by IFN-gamma and its C-terminal peptide IFN-gamma(95-133). |journal=J. Immunol. |volume=155 |issue= 12 |pages= 5617–22 |year= 1996 |pmid= 7499845 |doi=
*cite journal | author=Igarashi K, Garotta G, Ozmen L, "et al." |title=Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor. |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14333–6 |year= 1994 |pmid= 7514165 |doi=
*cite journal | author=Walter MR, Windsor WT, Nagabhushan TL, "et al." |title=Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor. |journal=Nature |volume=376 |issue= 6537 |pages= 230–5 |year= 1995 |pmid= 7617032 |doi= 10.1038/376230a0
*cite journal | author=Kotenko SV, Izotova LS, Pollack BP, "et al." |title=Interaction between the components of the interferon gamma receptor complex. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 20915–21 |year= 1995 |pmid= 7673114 |doi=
*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 | author=Tjoelker LW, Seyfried CE, Eddy RL, "et al." |title=Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. |journal=Biochemistry |volume=33 |issue= 11 |pages= 3229–36 |year= 1994 |pmid= 8136357 |doi=
*cite journal | author=Greenlund AC, Farrar MA, Viviano BL, Schreiber RD |title=Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). |journal=EMBO J. |volume=13 |issue= 7 |pages= 1591–600 |year= 1994 |pmid= 8156998 |doi=
*cite journal | author=Stüber D, Friedlein A, Fountoulakis M, "et al." |title=Alignment of disulfide bonds of the extracellular domain of the interferon gamma receptor and investigation of their role in biological activity. |journal=Biochemistry |volume=32 |issue= 9 |pages= 2423–30 |year= 1993 |pmid= 8443182 |doi=
*cite journal | author=Dalton DK, Pitts-Meek S, Keshav S, "et al." |title=Multiple defects of immune cell function in mice with disrupted interferon-gamma genes. |journal=Science |volume=259 |issue= 5102 |pages= 1739–42 |year= 1993 |pmid= 8456300 |doi=
*cite journal | author=Novelli F, Giovarelli M, Gentz R, "et al." |title=Modulation of interferon-gamma receptor during human T lymphocyte alloactivation. |journal=Eur. J. Immunol. |volume=23 |issue= 6 |pages= 1226–31 |year= 1993 |pmid= 8500521 |doi=
*cite journal | author=Newport MJ, Huxley CM, Huston S, "et al." |title=A mutation in the interferon-gamma-receptor gene and susceptibility to mycobacterial infection. |journal=N. Engl. J. Med. |volume=335 |issue= 26 |pages= 1941–9 |year= 1997 |pmid= 8960473 |doi=
*cite journal | author=Jouanguy E, Altare F, Lamhamedi S, "et al." |title=Interferon-gamma-receptor deficiency in an infant with fatal bacille Calmette-Guérin infection. |journal=N. Engl. J. Med. |volume=335 |issue= 26 |pages= 1956–61 |year= 1997 |pmid= 8960475 |doi=
*cite journal | author=Gerritsma JS, Gerritsen AF, De Ley M, "et al." |title=Interferon-gamma induces biosynthesis of complement components C2, C4 and factor H by human proximal tubular epithelial cells. |journal=Cytokine |volume=9 |issue= 4 |pages= 276–83 |year= 1997 |pmid= 9112336 |doi= 10.1006/cyto.1996.0164
*cite journal | author=Sogabe S, Stuart F, Henke C, "et al." |title=Neutralizing epitopes on the extracellular interferon gamma receptor (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex. |journal=J. Mol. Biol. |volume=273 |issue= 4 |pages= 882–97 |year= 1998 |pmid= 9367779 |doi= 10.1006/jmbi.1997.1336
*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=

External links


update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes

Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Interferon-gamma receptor — protein Name= interferon gamma receptor 1 caption= width= HGNCid=5439 Symbol=IFNGR1 AltSymbols=IFNGR EntrezGene=3459 OMIM=107470 RefSeq=NM 000416 UniProt=P15260 PDB= ECnumber= Chromosome=6 Arm=q Band=23 LocusSupplementaryData= q24protein… …   Wikipedia

  • Interferon-gamma — (IFN γ) is a dimerized soluble cytokine that is the only member of the type II class of interferons.cite journal | author = Gray PW, Goeddel DV | title = Structure of the human immune interferon gene | journal = Nature | volume = 298 | issue =… …   Wikipedia

  • Interferon — Interféron Pour les articles homonymes, voir IFN. Les Interférons (IFN) sont des protéines (glycoprotéines de la famille des cytokines) naturellement produites par les cellules du système immunitaire, mais également par d autres types cellulaires …   Wikipédia en Français

  • Interféron — Pour les articles homonymes, voir IFN. Les interférons (IFN) sont des protéines (glycoprotéines de la famille des cytokines). Ils sont naturellement produits par les cellules du système immunitaire, mais également par d autres types cellulaires… …   Wikipédia en Français

  • Interferon — Interferons (IFNs) are natural proteins produced by the cells of the immune system of most vertebrates in response to challenges by foreign agents such as viruses, parasites and tumor cells. Interferons belong to the large class of glycoproteins… …   Wikipedia

  • Interferon type II — A sole member makes up the type II IFNs that is called IFN γ (gamma). Mature IFN γ is an anti parallel homodimer, which binds to the IFN γ receptor (IFNGR) complex to elicit a signal within its target cell. IFNGR is made up of two subunits each… …   Wikipedia

  • Receptor (biochemistry) — For other uses, see Receptor (disambiguation). In biochemistry, a receptor is a molecule found on the surface of a cell, which receives specific chemical signals from neighbouring cells or the wider environment within an organism. These signals… …   Wikipedia

  • Type II cytokine receptor — Type II cytokine receptors are transmembrane proteins that are expressed on the surface of certain cells, which bind and respond to a select group of cytokines. These receptors are similar to type I cytokine receptors except they do not possess… …   Wikipedia

  • Cytokine receptor — Key steps of the JAK STAT pathway for type 1 and 2 cytokine receptors …   Wikipedia

  • Peroxisome proliferator-activated receptor gamma — PDB rendering based on 1fm6 …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”

We are using cookies for the best presentation of our site. Continuing to use this site, you agree with this.