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BET3 Bet3p

Bet3, Bet3p
TRAPPC3 is a component of the TRAPP complex, which is involved in tethering of transport vesicles to the cis-Golgi membrane (Turnbull et al., 2005 [PubMed 15692564]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CAN, YPT1, CIs, ACID, BET1
Papers on Bet3
A General, Practical Triethylborane-Catalyzed Reduction of Carbonyl Functions to Alcohols.
New
Huang et al., Shanghai, China. In Chemistry, Nov 2015
Mechanistic studies revealed a resting state of sodium triethylalkoxylborate that is the product of the reaction of BEt3 with sodium alkoxide.
Protonolysis and thermolysis reactions of functionalised NHC-carbene boranes and borates.
Wang et al., Edinburgh, United Kingdom. In Dalton Trans, 2014
A set of β-ketoimidazolium and β-ketoimidazolinium salts of the general formula [R(1)C(O)CH2{CH[NCR(3)CR(3)N(R(2))]}]X (R(1) = (t)Bu, naphth; R(2) = (i)Pr, Mes, (t)Bu; R(3) = H, Me, (H)2; X = Cl, Br) show contrasting reactivity with superhydride bases MHBEt3; two are reduced to chiral β-alcohol carbene-boranes R(1)CH(OH)CH2{C(BEt3)[NCR(3)CR(3)N(R(2))]} 2 (R(1) = (t)Bu; R(2) = (i)Pr, Mes; R(3) = H), two with bulky R(2) substituents are reduced to chiral β-borate imidazolium salts [R(1)CH(OBEt3)CH2{CH[NCR(3)CR(3)N(R(2))]}]X 3 (R(1) = (t)Bu, naphth; R(2) = Mes, (t)Bu; R(3) = H, Me; X = Cl, Br), and the two saturated heterocycle derivatives remain unreduced but form carbene-borane adducts R(1)C(O)CH2{C(BEt3)[NCR(3)CR(3)N(R(2))]} 4 (R(1) = (t)Bu, naphth; R(2) = Mes; R(3) = (H)2).
Bis[N,N'-diisopropylbenzamidinato(-)]silicon(II): Lewis acid/base reactions with triorganylboranes.
Tacke et al., Würzburg, Germany. In Chemistry, 2014
Reaction of the donor-stabilized silylene 1 (which is three-coordinate in the solid state and four-coordinate in solution) with BEt3 and BPh3 leads to the formation of the Lewis acid/base complexes 2 and 3, respectively, which are the first five-coordinate silicon compounds with an SiB bond.
Triethylborane-initiated radical chain fluorination: a synthetic method derived from mechanistic insight.
Lectka et al., Baltimore, United States. In J Org Chem, 2014
Furthermore, BEt3/O2 is a preferred initiator in industrial processes, as it is economical, is low in toxicity, and lends way to easier workup.
A trs20 mutation that mimics an SEDT-causing mutation blocks selective and non-selective autophagy: a model for TRAPP III organization.
Sacher et al., Montréal, Canada. In Traffic, 2013
Finally, we demonstrate that lipidated Bet3p is enriched in TRAPP III and that lipidation increases the efficiency of autophagy.
C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking.
Sacher et al., Montréal, Canada. In Mol Biol Cell, 2011
Two of the components, KIAA1012 and Bet3L, are mammalian homologues of Trs85p and Bet3p, respectively.
Exploring chromium(III)-alkyl bond homolysis with CpCr[(ArNCMe)2CH](R) complexes.
Smith et al., Kelowna, Canada. In J Am Chem Soc, 2011
Alternative synthetic routes to Cr(III)-R species using the previously reported Cr(II) compounds CpCr[(ArNCMe)2CH] and sources of R· radicals (e.g., BEt3 and air) were also explored.
The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.
Impact
Reinisch et al., New Haven, United States. In Cell, 2008
The multimeric membrane-tethering complexes TRAPPI and TRAPPII share seven subunits, of which four (Bet3p, Bet5p, Trs23p, and Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion.
Silica surface modification reactions with aluminum and boron alkyls and (alkyl) chlorides: reactivities and surface nanostructures.
Gunko et al., Charleston, United States. In J Nanosci Nanotechnol, 2008
Various silica pretreatments are utilized to alter the silica surface prior to reaction with AlEt3, AlEtxCl(3-x), BEt3, BCl3, and TiCl4.
Re-assessing the locations of components of the classical vesicle-mediated trafficking machinery in transfected Plasmodium falciparum.
Tilley et al., Melbourne, Australia. In Int J Parasitol, 2007
We have generated transgenic parasites expressing chimeric proteins and used immunofluorescence studies to determine the locations of plasmodial homologues of the COPII component, Sar1p, and the Golgi-docking protein, Bet3p.
mBET3 is required for the organization of the TRAPP complexes.
GeneRIF
Ferro-Novick et al., New Haven, United States. In Biochem Biophys Res Commun, 2006
Together our findings indicate that BET3 plays an important role in the organization of the TRAPP complexes in both mammalian cells and yeast.
Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.
GeneRIF
Veit et al., Berlin, Germany. In Proc Natl Acad Sci U S A, 2006
Bet3 has strong self-palmitoylating activity
Structure of the Bet3-Tpc6B core of TRAPP: two Tpc6 paralogs form trimeric complexes with Bet3 and Mum2.
GeneRIF
Heinemann et al., Berlin, Germany. In J Mol Biol, 2006
The crystal structure of human Bet3-Tpc6B heterodimer presented here represents a core sub-complex in the assembly of TRAPP.
mBet3p is required for homotypic COPII vesicle tethering in mammalian cells.
GeneRIF
Ferro-Novick et al., New Haven, United States. In J Cell Biol, 2006
mBet3p is required for the tethering and fusion of COPII vesicles to each other.
Syntheses, characterization, and X-ray crystal structures of beta-diketiminate group 13 hydrides, chlorides, and fluorides.
Schmidt et al., Göttingen, Germany. In Inorg Chem, 2006
Reduction of LGa(Me)Cl with LiH.BEt3 leads to the formation of LGa(Me)H (10).
Sigma-borane coordinated to nickel(0) and some related nickel(II) trihydride complexes.
García et al., Ecatepec, Mexico. In J Am Chem Soc, 2006
The reactions of the complexes [(dcype)NiH]2, 1, [(dippe)NiH]2, 2, and [(dtbpe)NiH]2, 3, with a mixture of BEt3 and Super-Hydride (LiHBEt3) afforded sigma-borane nickel(0) compounds of the type [(dcype)Ni(sigma-HBEt2)], 4, [(dippe)Ni(sigma-HBEt2)], 5, [(dtbpe)Ni(sigma-HBEt2)], 6, respectively, with the concomitant formation in each case of [(dcype)2Ni2)(H)3][BEt4], 7, [(dippe)2Ni2(H)3][BEt4], 8 and [(dtbpe)2Ni2(H)3][BEt4], 9, respectively.
Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p.
GeneRIF
Sacher et al., South Korea. In Traffic, 2005
Incorporated into the transport protein particle by Trs33.
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