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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

AF4/FMR2 family, member 4

Top mentioned proteins: CAN, HAD, ACID, ATPase, V1a
Papers on AlF4
Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling.
Conti et al., Martinsried, Germany. In Mol Cell, Dec 2015
We determined the 2.1 Å resolution structure of MLEcore bound to a U10 RNA and ADP-AlF4.
Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion.
Lou et al., Chengdu, China. In J Cell Biol, Oct 2015
Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AlF4(-) but is monomeric with GDP.
The HAlF4 superacid fragmentation induced by an excess electron attachment.
Skurski et al., Gdańsk, Poland. In Phys Chem Chem Phys, Aug 2015
The initially formed (HAlF4)(-) anion of a dipole-bound nature undergoes an immediate structural reorganization driven by the (AlF4)(-) strongly-bound superhalogen anion formation.
A Developmental Framework for Graft Formation and Vascular Reconnection in Arabidopsis thaliana.
Meyerowitz et al., Cambridge, United Kingdom. In Curr Biol, Jun 2015
We propose an inter-tissue communication process that occurs at the graft junction and promotes vascular connection by tissue-specific auxin responses involving ABERRANT LATERAL ROOT FORMATION 4 (ALF4).
Does Interaction between the Motor and Regulatory Domains of the Myosin Head Occur during ATPase Cycle? Evidence from Thermal Unfolding Studies on Myosin Subfragment 1.
Levitsky et al., Moscow, Russia. In Plos One, 2014
To check this assumption, we applied differential scanning calorimetry (DSC) combined with temperature dependences of fluorescence to study changes in thermal unfolding and the domain structure of S1, which occur upon formation of the ternary complexes S1-ADP-AlF4- and S1-ADP-BeFx that mimic S1 ATPase intermediate states S1**-ADP-Pi and S1*-ATP, respectively.
Regulation of AMP-activated protein kinase signaling by AFF4 protein, member of AF4 (ALL1-fused gene from chromosome 4) family of transcription factors, in hypothalamic neurons.
Morikawa et al., Wakayama, Japan. In J Biol Chem, 2012
AFF4 may therefore help to maintain activation of AMPK downstream signaling under conditions of prolonged stimulation with ghrelin, such as during fasting.
Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes.
Goličnik, In Acta Chim Slov, 2010
AlFx and MgFx are identified as enzymatic analogues of phosphoryl transition state where both are able to form different coordination geometries within the enzyme active sites: trigonal bipyramidal (AlF3 and MgF3-) or octahedral (AlF4- or MgF42-).
Differential chromatin looping regulates CD4 expression in immature thymocytes.
Peterlin et al., San Francisco, United States. In Mol Cell Biol, 2008
In the absence of Runx1 on the silencer, P-TEFb interacts with the transcription complex, forming a different chromatin loop between the enhancer and the promoter, which leads to the expression of the CD4 gene
Ca2+ versus Mg2+ coordination at the nucleotide-binding site of the sarcoplasmic reticulum Ca2+-ATPase.
Nissen et al., Århus, Denmark. In J Mol Biol, 2007
To determine whether Ca2+ competes with Mg2+ and affects the nucleotide-binding site, we have subjected the AMPPCP and ADP:AlF4- bound forms to crystallographic analysis by anomalous difference Fourier maps, and we have compared AMPPCP-bound forms crystallized in the absence or in the presence of Mg2+.
The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling.
Davies et al., Oxford, United Kingdom. In Hum Mol Genet, 2007
Af4 functions as a positive regulator of Pol II transcription elongation factor b (P-TEFb) kinase and, in complex with MLL fusion partners Af9, Enl and Af10, as a mediator of histone H3-K79 methylation by recruiting Dot1 to elongating Pol II
Infertility with defective spermiogenesis in mice lacking AF5q31, the target of chromosomal translocation in human infant leukemia.
Nosaka et al., Tokyo, Japan. In Mol Cell Biol, 2005
AF5q31 (Aff4) is a transcriptional regulator in testicular somatic cells and is essential for male germ cell differentiation and survival.
Regulation of nuclear phospholipase C activity.
Cocco et al., Bologna, Italy. In Acta Biochim Pol, 2003
Whilst at the plasma membrane this PI-PLC is activated and regulated by Galphaq/alpha(11) and Gbetagamma subunits, there is yet no evidence that qalpha/alpha(11) is present within the nuclear compartment, neither GTP-gamma-S nor AlF4 can stimulate PI-PLCbeta1 activity in isolated nuclei.
Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A.
Sigler et al., New Haven, United States. In Nature, 2001
Here we describe the crystal structure at 2.0 A of rod transducin alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the GTPase-activating protein RGS9.
Heterotrimeric G proteins as fluoride targets in bone (review).
Susa, Basel, Switzerland. In Int J Mol Med, 1999
The resulting G alpha-GDP-AlF4- complex assumes an active state conformation, which resembles that of G alpha-GTP complex.
Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.
Gamblin et al., London, United Kingdom. In Nature, 1997
Here we report the crystal structure of RhoA and rhoGAP complexed with the transition-state analogue GDP.AlF4- at 1.65 A resolution.
An evaluation of strategies available for the identification of GTP-binding proteins required in intracellular signalling pathways.
Gregory et al., Adelaide, Australia. In Cell Signal, 1997
Approaches available for investigations in the first stage include the use of analogues of GTP and GDP, AlF4-, inhibitors of G-protein isoprenylation, bacterial toxins which covalently modify G-proteins, and the introduction of a purified GDP dissociation inhibitor, GDP exchange and/or GTP-ase activating protein.
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
Sprang et al., Dallas, United States. In Cell, 1997
We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 .
RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.
Blumer et al., Saint Louis, United States. In Nature, 1996
RGS1, RGS4 and GAIP (for G alpha-interacting protein) bind specifically and tightly to G alphai and G alpha0 in cell membranes treated with GDP and AlF4(-), and are GAPs for G alphai, G alpha0 and transducin alpha-subunits, but not for G alphas.
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis.
Sprang et al., Dallas, United States. In Science, 1994
High-resolution x-ray structures of the GTP gamma S and GDP.AlF4- complexes formed by the G protein Gi alpha 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues.
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