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7 documents found
1: Title: Analysis of SRrp86-regulated alternative splicing: control of c-Jun and IκBβ activity.
Authors: Solis, Amanda S, et.al. .
Journal: RNA biology (Rna Biol), Vol. 7 (4): 486-94, 2010 Jul-Aug .
Snippet: Previous work led to the hypothesis that SRrp86, a related member of the SR protein superfamily, can interact with and modulate the activity of other SR proteins.
Affiliation: Department of Biological Sciences, Vanderbilt University, Nashville, TN USA. .
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2: Title: The splicing regulatory protein p18SRP is down-regulated in Alzheimer's disease brain.
Authors: Heese, Klaus, et.al. .
Journal: Journal of molecular neuroscience : MN (J Mol Neurosci), Vol. 24 (2): 269-76, 2004 .
Snippet: Using bioinformatics, the yeast two-hybrid-system, reverse transcription polymerase chain reaction, and fluorescence microscopy analysis, we demonstrate here that the new putative splicing regulatory protein p18SRP is a lysine-rich zinc finger domain-containing protein that interacts with the serine-arginine (SR)-rich splicing regulatory protein SRrp86.
Affiliation: BF Research Institute, c/o National Cardiovascular Center, Suita, Osaka 565-0873, Japan. heesek@silver.ocn.ne.jp .
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3: Title: Regulation of alternative splicing by SRrp86 and its interacting proteins.
Authors: Li, Jun, et.al. .
Journal: Molecular and cellular biology (Mol Cell Biol), Vol. 23 (21): 7437-47, 2003 .
Snippet: We show that SRrp86 interacts with all of the core SR proteins, as well as a subset of other splicing regulatory proteins, including SAF-B, hnRNP G, YB-1, and p72.
Affiliation: Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235, USA. .
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4: Title: A unique glutamic acid-lysine (EK) domain acts as a splicing inhibitor.
Authors: Li, Jun, et.al. .
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 277 (42): 39485-92, 2002 .
Snippet: To further investigate the function and domains of SRrp86, we generated a series of chimeric proteins by swapping the RNA recognition motif and RS domains between SRrp86 and two canonical members of the SR superfamily, ASF/SF2 and SRp75.
Affiliation: Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235, USA. .
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5: Title: [Molecular cloning, characterization, chromosomal assignment, genomic organization and verification of SFRS12(SRrp508), a novel member of human SR protein superfamily and a human homolog of rat SRrp86].
Authors: Zhang, De-Li, et.al. .
Journal: Yi chuan xue bao = Acta genetica Sinica (Yi Chuan Xue Bao), Vol. 29 (5): 377-83, 2002 .
Snippet: Furthermore, we have experimentally cloned and sequenced a cDNA fragment of 1680 bp containing the full-length ORF of 1527 bp in this novel human gene by RT-PCR from the single-stranded human pancreas cDNA library (Clontech), which is fully identical with that of the in silico cloning determined by the nucleotide sequencing.
Affiliation: Peking University Center for Human Disease Genomics, China National Center for Human Genome Research, Beijing 100083, China. delizhang@bjmu.edu .
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6: Title: Regulation of alternative splicing by SRrp86 through coactivation and repression of specific SR proteins.
Authors: Barnard, Daron C, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 8 (4): 526-33, 2002 .
Snippet: Regulation of SR protein activity, coupled with regulated protein expression, suggest that SRrp86 may play a crucial role in determining tissue specific patterns of alternative splicing.
Affiliation: Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, USA. .
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7: Title: Identification and characterization of a novel serine-arginine-rich splicing regulatory protein.
Authors: Barnard, D C, et.al. .
Journal: Molecular and cellular biology (Mol Cell Biol), Vol. 20 (9): 3049-57, 2000 .
Snippet: Full-length p86, but not a mutant lacking the RS-EK-RS domains, was found to preferentially interact with itself, SRp20, ASF/SF2, SRp55, and, to a slightly lesser extent, SC35.
Affiliation: Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, USA. .
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