GLTP

GLTP

Glycolipid transfer protein, also known as GLTP, is a human gene.cite web | title = Entrez Gene: GLTP glycolipid transfer protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51228| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. It is thought to be a cytoplasmic protein.cite web | title = Entrez Gene: GLTP glycolipid transfer protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51228| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Brown RE, Mattjus P |title=Glycolipid transfer proteins. |journal=Biochim. Biophys. Acta |volume=1771 |issue= 6 |pages= 746–60 |year= 2007 |pmid= 17320476 |doi= 10.1016/j.bbalip.2007.01.011
*cite journal | author=Abe A |title=Primary structure of glycolipid transfer protein from pig brain. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 9634–7 |year= 1990 |pmid= 2190982 |doi=
*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=Mattjus P, Pike HM, Molotkovsky JG, Brown RE |title=Charged membrane surfaces impede the protein-mediated transfer of glycosphingolipids between phospholipid bilayers. |journal=Biochemistry |volume=39 |issue= 5 |pages= 1067–75 |year= 2000 |pmid= 10653652 |doi=
*cite journal | author=Lin X, Mattjus P, Pike HM, "et al." |title=Cloning and expression of glycolipid transfer protein from bovine and porcine brain. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 5104–10 |year= 2000 |pmid= 10671554 |doi=
*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=Li XM, Malakhova ML, Lin X, "et al." |title=Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy. |journal=Biochemistry |volume=43 |issue= 31 |pages= 10285–94 |year= 2004 |pmid= 15287756 |doi= 10.1021/bi0495432
*cite journal | author=Malinina L, Malakhova ML, Teplov A, "et al." |title=Structural basis for glycosphingolipid transfer specificity. |journal=Nature |volume=430 |issue= 7003 |pages= 1048–53 |year= 2004 |pmid= 15329726 |doi= 10.1038/nature02856
*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
*cite journal | author=Rao CS, Lin X, Pike HM, "et al." |title=Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. |journal=Biochemistry |volume=43 |issue= 43 |pages= 13805–15 |year= 2004 |pmid= 15504043 |doi= 10.1021/bi0492197
*cite journal | author=Malakhova ML, Malinina L, Pike HM, "et al." |title=Point mutational analysis of the liganding site in human glycolipid transfer protein. Functionality of the complex. |journal=J. Biol. Chem. |volume=280 |issue= 28 |pages= 26312–20 |year= 2005 |pmid= 15901739 |doi= 10.1074/jbc.M500481200
*cite journal | author=Rao CS, Chung T, Pike HM, Brown RE |title=Glycolipid transfer protein interaction with bilayer vesicles: modulation by changing lipid composition. |journal=Biophys. J. |volume=89 |issue= 6 |pages= 4017–28 |year= 2006 |pmid= 16169991 |doi= 10.1529/biophysj.105.070631
*cite journal | author=Malinina L, Malakhova ML, Kanack AT, "et al." |title=The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure. |journal=PLoS Biol. |volume=4 |issue= 11 |pages= e362 |year= 2006 |pmid= 17105344 |doi= 10.1371/journal.pbio.0040362

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