TRIM25: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Tripartite motif-containing protein 25''' is a [[protein]] that in humans is encoded by the ''TRIM25'' [[gene]].<ref name="pmid7789997">{{cite journal | vauthors = Inoue S, Orimo A, Matsuda Y, Inazawa J, Emi M, Nakamura Y, Hori T, Muramatsu M | title = Chromosome mapping of human (ZNF147) and mouse genes for estrogen-responsive finger protein (efp), a member of the RING finger family | journal = Genomics | volume = 25 | issue = 2 | pages = 581–3 | date = Jan 1995 | pmid = 7789997 | pmc =  | doi = 10.1016/0888-7543(95)80064-S }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIM25 tripartite motif-containing 25| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7706| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- 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 = Tripartite motif-containing 25
| HGNCid = 12932
| Symbol = TRIM25
| AltSymbols =; EFP; RNF147; Z147; ZNF147
| OMIM = 600453
| ECnumber = 
| Homologene = 48325
| MGIid = 102749
| GeneAtlas_image1 = PBB_GE_TRIM25_206911_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7706
    | Hs_Ensembl = ENSG00000121060
    | Hs_RefseqProtein = NP_005073
    | Hs_RefseqmRNA = NM_005082
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 52320269
    | Hs_GenLoc_end = 52346408
    | Hs_Uniprot = Q14258
    | Mm_EntrezGene = 217069
    | Mm_Ensembl = ENSMUSG00000000275
    | Mm_RefseqmRNA = NM_009546
    | Mm_RefseqProtein = NP_033572
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 88815523
    | Mm_GenLoc_end = 88836383
    | Mm_Uniprot = Q3U3X7
  }}
}}
'''Tripartite motif-containing 25''', also known as '''TRIM25''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRIM25 tripartite motif-containing 25| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7706| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the tripartite motif (TRIM) family grouping more than 70 TRIMs. TRIM proteins primarily function as [[ubiquitin ligases]] that regulate the innate response to infection.<ref name="pmid24015671">{{cite journal | vauthors = D'Cruz AA, Kershaw NJ, Chiang JJ, Wang MK, Nicola NA, Babon JJ, Gack MU, Nicholson SE | title = Crystal structure of the TRIM25 B30.2 (PRYSPRY) domain: a key component of antiviral signalling | journal = The Biochemical Journal | volume = 456 | issue = 2 | pages = 231–40 | year = 2013 | pmid = 24015671 | pmc = 4012390 | doi = 10.1042/BJ20121425 }}</ref> TRIM25 localizes to the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene.<ref name="entrez">{{cite web | title = Entrez Gene: TRIM25 tripartite motif-containing 25| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7706| accessdate = }}</ref>
}}


==References==
== Domain Architecture ==
{{reflist|2}}
 
==Further reading==
TRIM25 has an N-terminal RING domain, followed by a B-box type 1 domain, a B-box type 2 domain, a coiled-coil domain (CCD) and a C-terminal SPRY domain.  The RING domain coordinates two zinc atoms and is essential for recruiting [[ubiquitin-conjugating enzyme]]s. The function of the B-box domains is unknown. The CCD domain has been implicated in multimerization and other protein-protein interactions.<ref>{{cite journal | vauthors = Haik KG | title = Visual difficulties from video display terminals | journal = Southern Medical Journal | volume = 78 | issue = 7 | pages = 887–8 | date = Jul 1985 | pmc = | doi=10.1097/00007611-198507000-00031 | pmid=}}</ref> The SPRY domain is required for substrate recruitment.<ref>{{cite journal | vauthors = Pilka L, Trávník P, Dvorák M, Tesarík J, Ventruba P, Krejcí K, Soska J | title = [Delivery after intrauterine embryo transfer obtained by fertilization and oocyte culture in vitro] | journal = Ceskoslovenská Gynekologie | volume = 50 | issue = 7 | pages = 452–9 | date = Aug 1985 | pmid = 4042170 }}</ref>  The NMR chemical shifts for backbone of the PRYSPRY domain of TRIM25 is assigned based on triple-resonance experiments using uniformly isotopic labeled protein and  the secondary structure of the domain PRYSPRY domain of TRIM25 predicted based on the NMR assignments.<ref>{{Cite journal|last = Kong|first = Chen|last2 = Penumutchu|first2 = Srinivasa R.|last3 = Hung|first3 = Kuo-wei|last4 = Huang|first4 = Huiying|last5 = Lin|first5 = Tianwei|last6 = Yu|first6 = Chin|date = 2015-02-22|title = Backbone resonance assignments of the PRYSPRY domain of TRIM25|url = https://link.springer.com/article/10.1007/s12104-015-9599-x|journal = Biomolecular NMR Assignments|language = en|volume = 9|issue = 2|pages = 313–315|doi = 10.1007/s12104-015-9599-x|issn = 1874-2718}}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== TRIM25 functions ==
| citations =
 
*{{cite journal  | author=Horie K, Urano T, Ikeda K, Inoue S |title=Estrogen-responsive RING finger protein controls breast cancer growth. |journal=J. Steroid Biochem. Mol. Biol. |volume=85 |issue= 2-5 |pages= 101-4 |year= 2003 |pmid= 12943693 |doi= }}
TRIM25 plays a key role in the [[RIG-I]] signaling pathway. RIG-I is a cytosolic [[pattern recognition receptor]] that senses viral RNA. Following RNA recognition, the [[caspase recruitment domain]] (CARD) of RIG-I undergoes K(63)-linked [[ubiquitination]] by TRIM25. The RING and SPRY domains of TRIM25 mediate its interaction with RIG-I. IFN production then follows by an intracellular signaling pathway involving [[IRF3]].<ref>{{cite journal | vauthors = Gack MU, Kirchhofer A, Shin YC, Inn KS, Liang C, Cui S, Myong S, Ha T, Hopfner KP, Jung JU | title = Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 43 | pages = 16743–8 | date = Oct 2008 | pmid = 18948594 | doi = 10.1073/pnas.0804947105 | pmc=2575490}}</ref>
*{{cite journal | author=Inoue S, Orimo A, Matsuda Y, ''et al.'' |title=Chromosome mapping of human (ZNF147) and mouse genes for estrogen-responsive finger protein (efp), a member of the RING finger family. |journal=Genomics |volume=25 |issue= 2 |pages= 581-3 |year= 1995 |pmid= 7789997 |doi=  }}
 
*{{cite journal | author=Inoue S, Orimo A, Hosoi T, ''et al.'' |title=Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 11117-21 |year= 1994 |pmid= 8248217 |doi= }}
== Viral escape ==
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
 
*{{cite journal  | author=Ikeda K, Inoue S, Orimo A, ''et al.'' |title=Multiple regulatory elements and binding proteins of the 5'-flanking region of the human estrogen-responsive finger protein (efp) gene. |journal=Biochem. Biophys. Res. Commun. |volume=236 |issue= 3 |pages= 765-71 |year= 1997 |pmid= 9245730 |doi= 10.1006/bbrc.1997.7046 }}
To avoid IFN production, the non structural protein ([[NS1]]) of [[influenza]] will interact with CCD domain of TRIM25 to block RIG-I ubiquitination. Some studies have shown that a deletion of the CCD domain of TRIM25 prevents the binding of NS1.<ref>{{cite journal | vauthors = Gack MU, Albrecht RA, Urano T, Inn KS, Huang IC, Carnero E, Farzan M, Inoue S, Jung JU, García-Sastre A | title = Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I | journal = Cell Host & Microbe | volume = 5 | issue = 5 | pages = 439–49 | date = May 2009 | pmid = 19454348 | doi = 10.1016/j.chom.2009.04.006 | pmc=2737813}}</ref> Without this ubiquitination, there won’t be IFN production.
*{{cite journal  | author=Ikeda K, Orimo A, Higashi Y, ''et al.'' |title=Efp as a primary estrogen-responsive gene in human breast cancer. |journal=FEBS Lett. |volume=472 |issue= 1 |pages= 9-13 |year= 2000 |pmid= 10781795 |doi= }}
 
*{{cite journal  | author=Reymond A, Meroni G, Fantozzi A, ''et al.'' |title=The tripartite motif family identifies cell compartments. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2140-51 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140 }}
== References ==
*{{cite journal | author=Urano T, Saito T, Tsukui T, ''et al.'' |title=Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. |journal=Nature |volume=417 |issue= 6891 |pages= 871-5 |year= 2002 |pmid= 12075357 |doi= 10.1038/nature00826 }}
{{reflist|33em}}
*{{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=Shimada N, Suzuki T, Inoue S, ''et al.'' |title=Systemic distribution of estrogen-responsive finger protein (Efp) in human tissues. |journal=Mol. Cell. Endocrinol. |volume=218 |issue= 1-2 |pages= 147-53 |year= 2004 |pmid= 15130519 |doi= 10.1016/j.mce.2003.12.008 }}
== Further reading ==
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
{{refbegin|33em}}
*{{cite journal | author=Rush J, Moritz A, Lee KA, ''et al.'' |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94-101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046 }}
* {{cite journal | vauthors = Horie K, Urano T, Ikeda K, Inoue S | title = Estrogen-responsive RING finger protein controls breast cancer growth | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 85 | issue = 2-5 | pages = 101–4 | date = Jun 2003 | pmid = 12943693 | doi = 10.1016/S0960-0760(03)00209-7 }}
*{{cite journal | author=Suzuki T, Urano T, Tsukui T, ''et al.'' |title=Estrogen-responsive finger protein as a new potential biomarker for breast cancer. |journal=Clin. Cancer Res. |volume=11 |issue= 17 |pages= 6148-54 |year= 2005 |pmid= 16144914 |doi= 10.1158/1078-0432.CCR-05-0040 }}
* {{cite journal | vauthors = Inoue S, Orimo A, Hosoi T, Kondo S, Toyoshima H, Kondo T, Ikegami A, Ouchi Y, Orimo H, Muramatsu M | title = Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 90 | issue = 23 | pages = 11117–21 | date = Dec 1993 | pmid = 8248217 | pmc = 47933 | doi = 10.1073/pnas.90.23.11117 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Nakayama H, Sano T, Motegi A, ''et al.'' |title=Increasing 14-3-3 sigma expression with declining estrogen receptor alpha and estrogen-responsive finger protein expression defines malignant progression of endometrial carcinoma. |journal=Pathol. Int. |volume=55 |issue= 11 |pages= 707-15 |year= 2005 |pmid= 16271083 |doi= 10.1111/j.1440-1827.2005.01900.x }}
* {{cite journal | vauthors = Ikeda K, Inoue S, Orimo A, Sano M, Watanabe T, Tsutsumi K, Muramatsu M | title = Multiple regulatory elements and binding proteins of the 5'-flanking region of the human estrogen-responsive finger protein (efp) gene | journal = Biochemical and Biophysical Research Communications | volume = 236 | issue = 3 | pages = 765–71 | date = Jul 1997 | pmid = 9245730 | doi = 10.1006/bbrc.1997.7046 }}
*{{cite journal | author=Nakasato N, Ikeda K, Urano T, ''et al.'' |title=A ubiquitin E3 ligase Efp is up-regulated by interferons and conjugated with ISG15. |journal=Biochem. Biophys. Res. Commun. |volume=351 |issue= 2 |pages= 540-6 |year= 2007 |pmid= 17069755 |doi= 10.1016/j.bbrc.2006.10.061 }}
* {{cite journal | vauthors = Ikeda K, Orimo A, Higashi Y, Muramatsu M, Inoue S | title = Efp as a primary estrogen-responsive gene in human breast cancer | journal = FEBS Letters | volume = 472 | issue = 1 | pages = 9–13 | date = Apr 2000 | pmid = 10781795 | doi = 10.1016/S0014-5793(00)01421-6 }}
*{{cite journal | author=Nakajima A, Maruyama S, Bohgaki M, ''et al.'' |title=Ligand-dependent transcription of estrogen receptor alpha is mediated by the ubiquitin ligase EFP. |journal=Biochem. Biophys. Res. Commun. |volume=357 |issue= 1 |pages= 245-51 |year= 2007 |pmid= 17418098 |doi= 10.1016/j.bbrc.2007.03.134 }}
* {{cite journal | vauthors = Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A | title = The tripartite motif family identifies cell compartments | journal = The EMBO Journal | volume = 20 | issue = 9 | pages = 2140–51 | date = May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 }}
}}
* {{cite journal | vauthors = Urano T, Saito T, Tsukui T, Fujita M, Hosoi T, Muramatsu M, Ouchi Y, Inoue S | title = Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth | journal = Nature | volume = 417 | issue = 6891 | pages = 871–5 | date = Jun 2002 | pmid = 12075357 | doi = 10.1038/nature00826 }}
* {{cite journal | vauthors = Shimada N, Suzuki T, Inoue S, Kato K, Imatani A, Sekine H, Ohara S, Shimosegawa T, Sasano H | title = Systemic distribution of estrogen-responsive finger protein (Efp) in human tissues | journal = Molecular and Cellular Endocrinology | volume = 218 | issue = 1-2 | pages = 147–53 | date = Apr 2004 | pmid = 15130519 | doi = 10.1016/j.mce.2003.12.008 }}
* {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = Jan 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 }}
* {{cite journal | vauthors = Suzuki T, Urano T, Tsukui T, Horie-Inoue K, Moriya T, Ishida T, Muramatsu M, Ouchi Y, Sasano H, Inoue S | title = Estrogen-responsive finger protein as a new potential biomarker for breast cancer | journal = Clinical Cancer Research | volume = 11 | issue = 17 | pages = 6148–54 | date = Sep 2005 | pmid = 16144914 | doi = 10.1158/1078-0432.CCR-05-0040 }}
* {{cite journal | vauthors = Nakayama H, Sano T, Motegi A, Oyama T, Nakajima T | title = Increasing 14-3-3 sigma expression with declining estrogen receptor alpha and estrogen-responsive finger protein expression defines malignant progression of endometrial carcinoma | journal = Pathology International | volume = 55 | issue = 11 | pages = 707–15 | date = Nov 2005 | pmid = 16271083 | doi = 10.1111/j.1440-1827.2005.01900.x }}
* {{cite journal | vauthors = Nakasato N, Ikeda K, Urano T, Horie-Inoue K, Takeda S, Inoue S | title = A ubiquitin E3 ligase Efp is up-regulated by interferons and conjugated with ISG15 | journal = Biochemical and Biophysical Research Communications | volume = 351 | issue = 2 | pages = 540–6 | date = Dec 2006 | pmid = 17069755 | doi = 10.1016/j.bbrc.2006.10.061 }}
* {{cite journal | vauthors = Nakajima A, Maruyama S, Bohgaki M, Miyajima N, Tsukiyama T, Sakuragi N, Hatakeyama S | title = Ligand-dependent transcription of estrogen receptor alpha is mediated by the ubiquitin ligase EFP | journal = Biochemical and Biophysical Research Communications | volume = 357 | issue = 1 | pages = 245–51 | date = May 2007 | pmid = 17418098 | doi = 10.1016/j.bbrc.2007.03.134 }}
{{refend}}
{{refend}}


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Latest revision as of 12:16, 15 September 2017

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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
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View/Edit Human

Tripartite motif-containing protein 25 is a protein that in humans is encoded by the TRIM25 gene.[1][2]

Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family grouping more than 70 TRIMs. TRIM proteins primarily function as ubiquitin ligases that regulate the innate response to infection.[3] TRIM25 localizes to the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene.[2]

Domain Architecture

TRIM25 has an N-terminal RING domain, followed by a B-box type 1 domain, a B-box type 2 domain, a coiled-coil domain (CCD) and a C-terminal SPRY domain. The RING domain coordinates two zinc atoms and is essential for recruiting ubiquitin-conjugating enzymes. The function of the B-box domains is unknown. The CCD domain has been implicated in multimerization and other protein-protein interactions.[4] The SPRY domain is required for substrate recruitment.[5] The NMR chemical shifts for backbone of the PRYSPRY domain of TRIM25 is assigned based on triple-resonance experiments using uniformly isotopic labeled protein and the secondary structure of the domain PRYSPRY domain of TRIM25 predicted based on the NMR assignments.[6]

TRIM25 functions

TRIM25 plays a key role in the RIG-I signaling pathway. RIG-I is a cytosolic pattern recognition receptor that senses viral RNA. Following RNA recognition, the caspase recruitment domain (CARD) of RIG-I undergoes K(63)-linked ubiquitination by TRIM25. The RING and SPRY domains of TRIM25 mediate its interaction with RIG-I. IFN production then follows by an intracellular signaling pathway involving IRF3.[7]

Viral escape

To avoid IFN production, the non structural protein (NS1) of influenza will interact with CCD domain of TRIM25 to block RIG-I ubiquitination. Some studies have shown that a deletion of the CCD domain of TRIM25 prevents the binding of NS1.[8] Without this ubiquitination, there won’t be IFN production.

References

  1. ↑ Inoue S, Orimo A, Matsuda Y, Inazawa J, Emi M, Nakamura Y, Hori T, Muramatsu M (Jan 1995). "Chromosome mapping of human (ZNF147) and mouse genes for estrogen-responsive finger protein (efp), a member of the RING finger family". Genomics. 25 (2): 581–3. doi:10.1016/0888-7543(95)80064-S. PMID 7789997.
  2. ↑ 2.0 2.1 "Entrez Gene: TRIM25 tripartite motif-containing 25".
  3. ↑ D'Cruz AA, Kershaw NJ, Chiang JJ, Wang MK, Nicola NA, Babon JJ, Gack MU, Nicholson SE (2013). "Crystal structure of the TRIM25 B30.2 (PRYSPRY) domain: a key component of antiviral signalling". The Biochemical Journal. 456 (2): 231–40. doi:10.1042/BJ20121425. PMC 4012390. PMID 24015671.
  4. ↑ Haik KG (Jul 1985). "Visual difficulties from video display terminals". Southern Medical Journal. 78 (7): 887–8. doi:10.1097/00007611-198507000-00031.
  5. ↑ Pilka L, Trávník P, Dvorák M, Tesarík J, Ventruba P, Krejcí K, Soska J (Aug 1985). "[Delivery after intrauterine embryo transfer obtained by fertilization and oocyte culture in vitro]". Ceskoslovenská Gynekologie. 50 (7): 452–9. PMID 4042170.
  6. ↑ Kong, Chen; Penumutchu, Srinivasa R.; Hung, Kuo-wei; Huang, Huiying; Lin, Tianwei; Yu, Chin (2015-02-22). "Backbone resonance assignments of the PRYSPRY domain of TRIM25". Biomolecular NMR Assignments. 9 (2): 313–315. doi:10.1007/s12104-015-9599-x. ISSN 1874-2718.
  7. ↑ Gack MU, Kirchhofer A, Shin YC, Inn KS, Liang C, Cui S, Myong S, Ha T, Hopfner KP, Jung JU (Oct 2008). "Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction". Proceedings of the National Academy of Sciences of the United States of America. 105 (43): 16743–8. doi:10.1073/pnas.0804947105. PMC 2575490. PMID 18948594.
  8. ↑ Gack MU, Albrecht RA, Urano T, Inn KS, Huang IC, Carnero E, Farzan M, Inoue S, Jung JU, García-Sastre A (May 2009). "Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I". Cell Host & Microbe. 5 (5): 439–49. doi:10.1016/j.chom.2009.04.006. PMC 2737813. PMID 19454348.

Further reading

  • Horie K, Urano T, Ikeda K, Inoue S (Jun 2003). "Estrogen-responsive RING finger protein controls breast cancer growth". The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 101–4. doi:10.1016/S0960-0760(03)00209-7. PMID 12943693.
  • Inoue S, Orimo A, Hosoi T, Kondo S, Toyoshima H, Kondo T, Ikegami A, Ouchi Y, Orimo H, Muramatsu M (Dec 1993). "Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein". Proceedings of the National Academy of Sciences of the United States of America. 90 (23): 11117–21. doi:10.1073/pnas.90.23.11117. PMC 47933. PMID 8248217.
  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Ikeda K, Inoue S, Orimo A, Sano M, Watanabe T, Tsutsumi K, Muramatsu M (Jul 1997). "Multiple regulatory elements and binding proteins of the 5'-flanking region of the human estrogen-responsive finger protein (efp) gene". Biochemical and Biophysical Research Communications. 236 (3): 765–71. doi:10.1006/bbrc.1997.7046. PMID 9245730.
  • Ikeda K, Orimo A, Higashi Y, Muramatsu M, Inoue S (Apr 2000). "Efp as a primary estrogen-responsive gene in human breast cancer". FEBS Letters. 472 (1): 9–13. doi:10.1016/S0014-5793(00)01421-6. PMID 10781795.
  • Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". The EMBO Journal. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
  • Urano T, Saito T, Tsukui T, Fujita M, Hosoi T, Muramatsu M, Ouchi Y, Inoue S (Jun 2002). "Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth". Nature. 417 (6891): 871–5. doi:10.1038/nature00826. PMID 12075357.
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