| 词条 | RDH16 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| 释义 |
Model organisms
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty four tests were carried out on mutant mice, but no significant abnormalities were observed.[4] References1. ^1 {{cite web | title = Retinol dehydrogenase 16 (all-trans)| url = https://www.ncbi.nlm.nih.gov/gene/8608| accessdate = 2011-12-06}} 2. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBZG/salmonella-challenge/ |title=Salmonella infection data for Rdh16 |publisher=Wellcome Trust Sanger Institute}} 3. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBZG/citrobacter-challenge/ |title=Citrobacter infection data for Rdh16 |publisher=Wellcome Trust Sanger Institute}} 4. ^1 2 {{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }} 5. ^Mouse Resources Portal, Wellcome Trust Sanger Institute. 6. ^{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Rdh16 |title=International Knockout Mouse Consortium}} 7. ^{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362960 |title=Mouse Genome Informatics}} 8. ^{{Cite journal| last1 = Skarnes |first1 =W. C.| doi = 10.1038/nature10163 | last2 = Rosen | first2 = B.| last3 = West | first3 = A. P.| last4 = Koutsourakis | first4 = M.| last5 = Bushell | first5 = W.| last6 = Iyer | first6 = V.| last7 = Mujica | first7 = A. O.| last8 = Thomas | first8 = M.| last9 = Harrow | first9 = J.| last10 = Cox | first10 = T.| last11 = Jackson | first11 = D.| last12 = Severin | first12 = J.| last13 = Biggs | first13 = P.| last14 = Fu | first14 = J.| last15 = Nefedov | first15 = M.| last16 = De Jong | first16 = P. J.| last17 = Stewart | first17 = A. F.| last18 = Bradley | first18 = A. | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc =3572410 }} 9. ^{{cite journal |author=Dolgin E |title=Mouse library set to be knockout |journal=Nature |volume=474 |issue=7351 |pages=262–3 |date=June 2011 |pmid=21677718 |doi=10.1038/474262a }} 10. ^{{cite journal |vauthors=Collins FS, Rossant J, Wurst W |title=A mouse for all reasons |journal=Cell |volume=128 |issue=1 |pages=9–13 |date=January 2007 |pmid=17218247 |doi=10.1016/j.cell.2006.12.018 }} 11. ^{{cite journal|vauthors=van der Weyden L, White JK, Adams DJ, Logan DW | title=The mouse genetics toolkit: revealing function and mechanism. | journal=Genome Biol | year= 2011 | volume= 12 | issue= 6 | pages= 224 | pmid=21722353 | doi=10.1186/gb-2011-12-6-224 | pmc=3218837}} Further reading
| last1 = Persson | first1 = B. | last2 = Kallberg | first2 = Y. | last3 = Bray | first3 = J. E. | last4 = Bruford | first4 = E. | last5 = Dellaporta | first5 = S. L. | last6 = Favia | first6 = A. D. | last7 = Duarte | first7 = R. G. | last8 = Jörnvall | first8 = H. | last9 = Kavanagh | first9 = K. L. | last10 = Kedishvili | doi = 10.1016/j.cbi.2008.10.040 | first10 = N. | last11 = Kisiela | first11 = M. | last12 = Maser | first12 = E. | last13 = Mindnich | first13 = R. | last14 = Orchard | first14 = S. | last15 = Penning | first15 = T. M. | last16 = Thornton | first16 = J. M. | last17 = Adamski | first17 = J. | last18 = Oppermann | first18 = U. | title = The SDR (Short-Chain Dehydrogenase/Reductase and Related Enzymes) Nomenclature Initiative | journal = Chemico-Biological Interactions | volume = 178 | issue = 1–3 | pages = 94–98 | year = 2009 | pmid = 19027726 | pmc =2896744 }}
| last1 = Lapshina | first1 = E. A. | last2 = Belyaeva | first2 = O. V. | last3 = Chumakova | first3 = O. V. | last4 = Kedishvili | first4 = N. Y. | title = Differential Recognition of the Free versus Bound Retinol by Human Microsomal Retinol/Sterol Dehydrogenases: Characterization of the Holo-CRBP Dehydrogenase Activity of RoDH-4† | doi = 10.1021/bi026836r | journal = Biochemistry | volume = 42 | issue = 3 | pages = 776–784 | year = 2003 | pmid = 12534290 | pmc = }}
| last1 = Cain | first1 = J. M. | last2 = Zaino | first2 = R. | last3 = Shearer | first3 = D. | last4 = Bennett | first4 = R. A. | last5 = Olt | first5 = G. | last6 = Weisz | first6 = J. | title = Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria | journal = American Journal of Obstetrics and Gynecology | volume = 186 | issue = 4 | pages = 675–683 | year = 2002 | pmid = 11967490 | doi=10.1067/mob.2002.122127 }}{{refend}}{{gene-12-stub}} 2 : Human proteins|Genes mutated in mice |
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