Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Linlong Xue"'
Autor:
Meizhong Jin, Linlong Xue, Sharon A. Townson, Alan C. Rigby, Siminia Grigoriu, Kathryn M. Luly, Earl W. May, Alex Yuzhakov, Cindy C. Benod, Michelle L. Stewart, Alan S. Mann, Mark J. Mulvihill, Anna Kohlmann, Nicholas Perl, Jason T. Lowe, Jonah Simon, Alec D Silver, Gregory L. Verdine, Roy M. Pollock, Minyun Zhou, Seung-Joo Lee
Publikováno v:
Molecular Cancer Research. 18:B37-B37
Activating mutations in RAS proteins occur in ~1/3 of human cancers. These mutations impair the ability of the protein to hydrolyze GTP to GDP. As a result, mutant RAS proteins exist predominantly in the GTP-bound state, which directly activates aber
Autor:
Earl W. May, Meizhong Jin, Gizem Akcay, Anna Kohlmann, Sharon A. Townson, Linlong Xue, Alexander Yuzhakov, Cindy C. Benod, Ganesh Iyer, Alec D Silver, Alan S. Mann, Nicholas Perl, Minyun Zhou
Publikováno v:
Molecular Cancer Research. 18:A06-A06
RAS proteins are small GTPases involved in cell proliferation, survival, and differentiation, and are mutationally activated in about a third of all human cancers. These mutations drive cancer by impairing GTPase activity so that the RAS protein is f
Autor:
Stuart L. Schreiber, Michael Foley, Andrew Germain, Willmen Youngsaye, Timothy A. Lewis, Lawrence MacPherson, Michelle Palmer, Marek M. Nagiec, Christina Scherer, Han-Je Kim, Partha P. Nag, Michel Weïwer, BenjaminZ. Stanton, Chris Dockendorff, Melissa Bennion, Amal Ting, Jose Perez, Sara J. Buhrlage, Linlong Xue
Publikováno v:
ACS Medicinal Chemistry Letters
Macrocyclic Hedgehog (Hh) pathway inhibitors have been discovered with improved potency and maximal inhibition relative to the previously reported macrocycle robotnikinin. Analogues were prepared using a modular and efficient build-couple-pair (BCP)
Publikováno v:
Cell. 117(6):761-771
RPE65 is essential for the biosynthesis of 11-cis-retinal, the chromophore of rhodopsin. Here, we show that the membrane-associated form (mRPE65) is triply palmitoylated and is a chaperone for all-trans-retinyl esters, allowing their entry into the v
Publikováno v:
Biochemistry. 42:12805-12812
Lecithin retinol acyltransferase (LRAT) catalyzes the reversible esterification of vitamin A using lecithin as the acyl donor. LRAT is the founder member of a new class of enzymes, which include class II tumor suppressors, proteins essential for deve
Autor:
Huifen Faye Wang, Qinmi Wang, Grazyna D. Szklarz, Tammy L. Domanski, Linlong Xue, James R. Halpert, Maria Almira Correia
Publikováno v:
Chemical Research in Toxicology. 14:483-491
The major human liver drug-metabolizing cytochrome P450 enzymes P450 3A4 and P450 3A5 share >85% amino acid sequence identity yet exhibit different regioselectivity toward aflatoxin B(1) (AFB(1)) biotransformation [Gillam et al. (1995) Arch. Biochem.
Publikováno v:
Biochemistry. 45(35)
Lecithin retinol acyl transferase (LRAT) has the essential role of catalyzing the transfer of an acyl group from the sn-1 position of lecithin to vitamin A to generate all-trans-retinyl esters (tREs). In vitro studies had shown previously that LRAT a
Autor:
Robert R. Rando, Linlong Xue
Publikováno v:
Biochemistry. 43(20)
Lecithin-retinol acyltransferase (LRAT) catalyzes the transfer of an acyl moiety from the sn-1 position of lecithin to vitamin A, generating all-trans-retinyl esters. LRAT is a unique enzyme and is the founder member of an expanding group of proteins
Publikováno v:
Biochemistry. 42(20)
Lecithin retinol acyltransferase (LRAT) catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester, an essential reaction in the vertebrate visual cycle. Since all-trans-retinyl esters are the substrates for the isomerization reac
Publikováno v:
Archives of biochemistry and biophysics. 409(1)
CYP3A9 is an estrogen-inducible ortholog of human liver CYP3A4 with 76.5% sequence identity to CYP3A4. Unlike CYP3A4, it is a very poor testosterone 6beta- and 2beta-hydroxylase, but a relatively better catalyst of progesterone monohydroxylation larg