Abstract
Defects in homeostatic regulation of cholesterol and fatty acids are associated with major cardiometabolic risk factors that are prevalent in type 2 diabetes and atherosclerotic cardiovascular disease. Regulatory input is found at many levels; however, recent findings have revealed p...
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PMID: 21461683
PDF is available here.
Abstract
We review recent reports that miRNAs are key modulators of cellular senescence, and we examine their influence upon specific senescence-regulatory proteins. We discuss evidence that dysregulation of miRNA-governed senescence programs underlies age-associated diseases, including cancer....
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PMID: 21592610
PDF is available here.
Wei Jiang,
En Yi Wen,
Min Gong,
Yuan Shi,
Li Chen,
Yang Bi,
Yun Zhang,
Yong Fang Liu,
Jie Chen,
Ping Qu,
You Xue Liu,
Xiao Ping Wei and
Ting Yu Li
Abstract
We studied the mRNA expression patterns of 6 RA receptors in the postnatal rat cerebral cortex and white matter at 1, 3, 7, 10, 14, 21, 28, and 35days. We found that RARβ, RXRα and RXRβ mRNA levels gradually increased during postnatal development. RARα presented a nearly unimodal trend, but RAR...
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PMID: 21241670
PDF is available here.
Abstract
We show here that IL-17 enhanced the stability of chemokine CXCL1 mRNA and other mRNAs through a pathway that involved the adaptor Act1, the adaptors TRAF2 or TRAF5 and the splicing factor SF2 (also known as alternative splicing factor (ASF)). TRAF2 and TRAF5 were necessary for IL-17 to signal the s...
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PMID: 21822258
PDF is available here.
Abstract
We describe methodology for studying the role of bacterial ribosome modification in the regulation of gene expression. Ribosomal components modification influences translation efficiencies of certain mRNAs. Proteome analysis allows us to identify cellular protein composition change caused by ribosom...
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PMID: 21460884
PDF is available here.
Abstract
We demonstrate using co-immunoprecipitation approaches that Ccr4-Not subunits interact with Hmt1, the budding yeast ortholog of PRMT1. Furthermore, using genetic and biochemical approaches, we demonstrate that Ccr4-Not physically and functionally interacts with the heterogenous nuclear ribonucleopro...
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PMID: 21464899
PDF is available here.
Abstract
Star-PAP is a poly (A) polymerase (PAP) that is putatively required for 3'-end cleavage and polyadenylation of a select set of pre-messenger RNAs (mRNAs), including heme oxygenase (HO-1) mRNA. To investigate the underlying mechanism, the cleavage and polyadenylation of pre-mRNA was reconstituted wit...
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PMID: 21102410
PDF is available here.
Abstract
We have established a method for analyzing base-methylated cytosines in RNA using bisulfite sequencing. Treatment of RNA with bisulfite causes the chemical deamination of nonmethylated cytosines to uracil, while methylated cytosines remain unaffected. cDNA synthesis followed by polymerase chain reac...
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PMID: 20889702
PDF is available here.
Abstract
We have identified in silico a set of miRNAs that control helicase gene expression by regulating its mRNA stability and translation in rice. Our analysis revealed that several rice helicases have distinct miRNA specificities. Such analyses will be a prerequisite to refining our understanding of targ...
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PMID: 20953156
PDF is available here.
Abstract
HuR, an ubiquitously expressed member of the Hu family, selectively binds and stabilizes ARE-containing mRNAs encoding proto-oncogenes, cell cycle regulators, cytokines and growth factors. The mechanism of HuR stabilization on target mRNAs is believed to be mediated through competition with destabil...
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PMID: 20712017
PDF is available here.
Abstract
We expand the number of TGFbeta/BMP-regulated miRNAs (T/B-miRs) to 20. Of interest, a majority of T/B-miRs contain a consensus sequence (R-SBE) within the stem region of the primary transcripts of T/B-miRs (pri-T/B-miRs). Here, we demonstrate that Smads directly bind the R-SBE. Mutation of the R-SBE...
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PMID: 20705240
PDF is available here.
Geng Wang,
Hsiao-Wen Chen,
Yavuz Oktay,
Jin Zhang,
Eric L Allen,
Geoffrey M Smith,
Kelly C Fan,
Jason S Hong,
Samuel W French,
J Michael McCaffery,
Robert N Lightowlers,
Herbert C Morse,
Carla M Koehler and
Michael A Teitell
Abstract
We localized polynucleotide phosphorylase (PNPASE), a 3' --> 5' exoribonuclease and poly-A polymerase, in the mitochondrial intermembrane space, a location lacking resident RNAs. Here, we show a new role for PNPASE in regulating the import of nuclear-encoded RNAs into the mitochondrial matrix. PNPAS...
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PMID: 20691904
PDF is available here.
Abstract
We show that Hsp90 is required for Ago2 to receive the small interfering RNA (siRNA) duplex from the RNA-induced silencing complex-loading complex in RNAi, suggesting a model where Hsp90 modifies Ago2 conformation to accommodate the siRNA duplex....
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PMID: 20639883
PDF is available here.
Abstract
We describe the effects of prolonged alpha1A-AR and PKC activity on human ether-a-go-go-related gene (HERG) K(+) channels (Kv11.1) expressed in a heterologous expression system. Stimulation of alpha1A-AR with phenylephrine or direct activation of PKC with phorbol ester increased HERG channel protein...
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PMID: 20463060
PDF is available here.
Abstract
We review the current status and potential functions of miRNAs in protozoan, helminths, and arthropods, and propose some perspectives for future studies....
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PMID: 20532562
PDF is available here.
Abstract
We present evidence supporting a role for heteronuclear ribonucleoprotein A1 (hnRNP A1) as a negative regulator of let-7a. HnRNP A1 binds the conserved terminal loop of pri-let-7a-1 and inhibits its processing by Drosha. Levels of mature let-7a negatively correlate with hnRNP A1 levels in somatic ce...
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PMID: 20639884
PDF is available here.
Abstract
We found that SIRT1 protein levels were much higher in mouse embryonic stem cells (mESCs) than in differentiated tissues. miRNAs post-transcriptionally downregulated SIRT1 during mESC differentiation and maintained low levels of SIRT1 expression in differentiated tissues. Specifically, miR-181a and...
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PMID: 20634564
PDF is available here.
Abstract
Our current findings uncover a novel mechanism by which AMPK protects against hypercholesterolemia-mediated endothelial dysfunction....
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PMID: 20395595
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
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PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
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PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
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PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
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PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
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PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.
Abstract
We show that neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneDelta1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the p...
|
PMID: 20507976
PDF is available here.
Abstract
We apply a genomic approach to determine the presence of m(1)A58 hypomodified tRNAs in human cell lines and show how A58 hypomodification affects stability and involvement of tRNAs in translation. Our microarray-based method detects the presence of m(1)A58 hypomodified tRNA species on the basis of t...
|
PMID: 20484468
PDF is available here.