Results 31 to 40 of about 6,054 (206)

Purine Nucleotide Availability Regulates mTORC1 Activity through the Rheb GTPase

Cell Reports, 2017
Pharmacologic agents that interfere with nucleotide metabolism constitute an important class of anticancer agents. Recent studies have demonstrated that mTOR complex 1 (mTORC1) inhibitors suppress de novo biosynthesis of pyrimidine and purine nucleotides.
Natasha Emmanuel, Shoba Ragunathan, Qin Shan, Fang Wang, Andreas Giannakou, Nanni Huser, Guixian Jin, Jeremy Myers, Robert T. Abraham, Keziban Unsal-Kacmaz   +9 more
doaj   +1 more source

Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase[S]

Journal of Lipid Research, 2010
Over a hundred proteins in eukaryotic cells carry a C-terminal CaaX box sequence, which targets them for posttranslational isoprenylation of the cysteine residue.
Julia M. Fres, Stefan Müller, Gerrit J.K. Praefcke   +2 more
doaj   +1 more source

Toward Multi(radio)metalated DNA: Enzymatic Polymerization of Metal‐Chelate‐Modified Deoxyribonucleoside Triphosphates

Angewandte Chemie, EarlyView.
This work presents the first enzymatic polymerization of defined metal‐chelator‐modified nucleotides that leverage polymerase fidelity for uniform (radio)metal loading with successful incorporation of five different metals: Ga, In, Tb, Lu, and Y.
Antonio A. W. L. Wong, François Bénard, David M. Perrin   +2 more
wiley   +2 more sources

Farnesylation of the Transducin G Protein Gamma Subunit Is a Prerequisite for Its Ciliary Targeting in Rod Photoreceptors

Frontiers in Molecular Neuroscience, 2018
Primary cilia are microtubule-based organelles, which protrude from the plasma membrane and receive a wide range of extracellular signals. Various cilia use G protein-coupled receptors (GPCRs) for the detection of these signals.
Celine Brooks, Joseph Murphy, Marycharmain Belcastro, Daniel Heller, Saravanan Kolandaivelu, Oleg Kisselev, Maxim Sokolov, Maxim Sokolov   +7 more
doaj   +1 more source

Protein farnesylation is upregulated in Alzheimer’s human brains and neuron-specific suppression of farnesyltransferase mitigates pathogenic processes in Alzheimer’s model mice

Acta Neuropathologica Communications, 2021
The pathogenic mechanisms underlying the development of Alzheimer’s disease (AD) remain elusive and to date there are no effective prevention or treatment for AD.
Angela Jeong, Shaowu Cheng, Rui Zhong, David A. Bennett, Martin O. Bergö, Ling Li   +5 more
doaj   +1 more source

Genetic and pharmacological modulation of lamin A farnesylation determines its function and turnover. [PDF]

Aging Cell
Hutchinson-Gilford Progeria syndrome (HGPS) is a severe premature ageing disorder caused by a 50 amino acid truncated (Δ50AA) and permanently farnesylated lamin A (LA) mutant called progerin.
Foo MXR, Ong PF, Yap ZX, Maric M, Bong CJS, Dröge P, Burke B, Dreesen O.   +7 more
europepmc   +2 more sources

Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria

Journal of Lipid Research, 2010
Hutchinson-Gilford progeria syndrome (HGPS) is caused by the accumulation of a farnesylated form of prelamin A (progerin). Previously, we showed that blocking protein farnesylation with a farnesyltransferase inhibitor (FTI) ameliorates the disease ...
Shao H. Yang, Sandy Y. Chang, Douglas A. Andres, H. Peter Spielmann, Stephen G. Young, Loren G. Fong   +5 more
doaj   +1 more source

Mechanisms of A-Type Lamin Targeting to Nuclear Ruptures Are Disrupted in LMNA- and BANF1-Associated Progerias

Cells, 2022
Mutations in the genes LMNA and BANF1 can lead to accelerated aging syndromes called progeria. The protein products of these genes, A-type lamins and BAF, respectively, are nuclear envelope (NE) proteins that interact and participate in various cellular ...
Rhiannon M. Sears, Kyle J. Roux
doaj   +1 more source

Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome

Journal of Lipid Research, 2009
Hutchinson-Gilford progeria syndrome (HGPS) is caused by the synthesis of a truncated prelamin A, commonly called progerin, that contains a carboxyl-terminal farnesyl lipid anchor.
Brandon S.J. Davies, Shao H. Yang, Emily Farber, Roger Lee, Suzanne B. Buck, Douglas A. Andres, H. Peter Spielmann, Brian J. Agnew, Fuyuhiko Tamanoi, Loren G. Fong, Stephen G. Young   +10 more
doaj   +1 more source

Lamin A-linked progerias: is farnesylation the be all and end all? [PDF]

, 2010
The Publisher's final version can be found by following the DOI link.HGPS (Hutchinson-Gilford progeria syndrome) is a severe childhood disorder that appears to mimic an accelerated aging process. The disease is most commonly caused by gene mutations that
Sue Shackleton, Smallwood, Dawn T., Shackleton, S, Dawn T. Smallwood   +3 more
core   +1 more source