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Search results 301 to 337 out of 337 for Dmpk

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Type

Details

Score

Publication

26082468 | J:225427

First Author:	Bisset DR
Year:	2015
Journal:	Hum Mol Genet
Title:	Therapeutic impact of systemic AAV-mediated RNA interference in a mouse model of myotonic dystrophy.
Volume:	24
Issue:	17
Pages:	4971-83

•

Publication

25403273 | J:230299

First Author:	Ohsawa N
Year:	2015
Journal:	Genes Cells
Title:	ABLIM1 splicing is abnormal in skeletal muscle of patients with DM1 and regulated by MBNL, CELF and PTBP1.
Volume:	20
Issue:	2
Pages:	121-34

•

Publication

28369518 | J:242840

First Author:	Ravel-Chapuis A
Year:	2017
Journal:	Hum Mol Genet
Title:	Misregulation of calcium-handling proteins promotes hyperactivation of calcineurin-NFAT signaling in skeletal muscle of DM1 mice.
Volume:	26
Issue:	12
Pages:	2192-2206

•

Publication

15972723 | J:100392

First Author:	Kimura T
Year:	2005
Journal:	Hum Mol Genet
Title:	Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2+-ATPase in myotonic dystrophy type 1.
Volume:	14
Issue:	15
Pages:	2189-200

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Publication

17702765 | J:172184

First Author:	Yuan Y
Year:	2007
Journal:	Nucleic Acids Res
Title:	Muscleblind-like 1 interacts with RNA hairpins in splicing target and pathogenic RNAs.
Volume:	35
Issue:	16
Pages:	5474-86

•

Publication

24659496 | J:211196

First Author:	Ferreboeuf M
Year:	2014
Journal:	Hum Mol Genet
Title:	Nuclear protein spreading: implication for pathophysiology of neuromuscular diseases.
Volume:	23
Issue:	15
Pages:	4125-33

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Publication

25887157 | J:230537

First Author:	Peng X
Year:	2015
Journal:	Biochim Biophys Acta
Title:	Celf1 regulates cell cycle and is partially responsible for defective myoblast differentiation in myotonic dystrophy RNA toxicity.
Volume:	1852
Issue:	7
Pages:	1490-7

•

Publication

30997488 | J:277136

First Author:	Yadava RS
Year:	2019
Journal:	Hum Mol Genet
Title:	MBNL1 overexpression is not sufficient to rescue the phenotypes in a mouse model of RNA toxicity.
Volume:	28
Issue:	14
Pages:	2330-2338

•

Publication

37390204 | J:342764

First Author:	Da Silva A
Year:	2023
Journal:	Sci Adv
Title:	N-acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function.
Volume:	9
Issue:	26
Pages:	eade6308

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Publication

9887331 | J:52367

First Author:	Lu X
Year:	1999
Journal:	Hum Mol Genet
Title:	Cardiac elav-type RNA-binding protein (ETR-3) binds to RNA CUG repeats expanded in myotonic dystrophy.
Volume:	8
Issue:	1
Pages:	53-60

•

Publication

10802668 | J:61881

First Author:	Sarkar PS
Year:	2000
Journal:	Nat Genet
Title:	Heterozygous loss of Six5 in mice is sufficient to cause ocular cataracts.
Volume:	25
Issue:	1
Pages:	110-4

•

Publication

16601207 | -

First Author:	Moraes KC
Year:	2006
Journal:	RNA
Title:	CUG-BP binds to RNA substrates and recruits PARN deadenylase.
Volume:	12
Issue:	6
Pages:	1084-91

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Publication

8948631 | -

First Author:	Timchenko LT
Year:	1996
Journal:	Nucleic Acids Res
Title:	Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy.
Volume:	24
Issue:	22
Pages:	4407-14

•

Publication

16862542 | -

First Author:	Leroy O
Year:	2006
Journal:	J Neurosci Res
Title:	ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally enhanced in myotonic dystrophy type I.
Volume:	84
Issue:	4
Pages:	852-9

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Publication

11124939 | -

First Author:	Timchenko NA
Year:	2001
Journal:	J Biol Chem
Title:	RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of CUGBP1.
Volume:	276
Issue:	11
Pages:	7820-6

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Publication

18267972 | -

First Author:	Graindorge A
Year:	2008
Journal:	Nucleic Acids Res
Title:	Identification of CUG-BP1/EDEN-BP target mRNAs in Xenopus tropicalis.
Volume:	36
Issue:	6
Pages:	1861-70

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Publication

16836486 | -

First Author:	Cosson B
Year:	2006
Journal:	Biol Cell
Title:	Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding.
Volume:	98
Issue:	11
Pages:	653-65

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Publication

11577082 | -

First Author:	Anant S
Year:	2001
Journal:	J Biol Chem
Title:	Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor.
Volume:	276
Issue:	50
Pages:	47338-51

•

Publication

15226369 | -

First Author:	Ladd AN
Year:	2004
Journal:	J Cell Sci
Title:	Multiple domains control the subcellular localization and activity of ETR-3, a regulator of nuclear and cytoplasmic RNA processing events.
Volume:	117
Issue:	Pt 16
Pages:	3519-29

•

Protein Domain

IPR034198 | CELF1/2_RRM2

Type:

Domain

Description:

The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 2 (RRM2) of CELF-1 and CELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].

•

Protein Domain

IPR034199 | CELF1/2_RRM3

Type:

Domain

Description:

The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 3 (RRM3) of CELF-1 andCELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequenceidentity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].

•

Publication

33503262 | J:303720

First Author:	Tanner MK
Year:	2021
Journal:	Nucleic Acids Res
Title:	Targeted splice sequencing reveals RNA toxicity and therapeutic response in myotonic dystrophy.
Volume:	49
Issue:	4
Pages:	2240-2254

•

Publication

10893231 | J:74955

First Author:	Good PJ
Year:	2000
Journal:	J Biol Chem
Title:	A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator.
Volume:	275
Issue:	37
Pages:	28583-92

•

Protein

P28659

Organism:	Mus musculus/domesticus
Length:	486
Fragment?:	false

•

Protein

A0A0R4J0T5

Organism:	Mus musculus/domesticus
Length:	487
Fragment?:	false

•

Publication

25723530 | -

First Author:	Kim G
Year:	2015
Journal:	PLoS Genet
Title:	Region-specific activation of oskar mRNA translation by inhibition of Bruno-mediated repression.
Volume:	11
Issue:	2
Pages:	e1004992

•

Protein Domain

IPR034196 | CELF1/2_RRM1

Type:

Domain

Description:

The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 1 (RRM1) of CELF-1 and CELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].Proteins containing this motif also include Drosophila melanogaster Bruno protein, which plays a central role in regulation ofOskar (Osk) expression in flies. It mediates repression by binding to regulatory Bruno response elements (BREs) in the Osk mRNA 3' UTR []. The full-length Bruno protein contains three RRMs, two located in the N-terminal half of the protein and the third near the C terminus, separated by a linker region.

•

Protein

Q9Z0H4

Organism:	Mus musculus/domesticus
Length:	508
Fragment?:	false

•

Protein

S4R2U7

Organism:	Mus musculus/domesticus
Length:	460
Fragment?:	false

•

Protein

A0A0R4J2B0

Organism:	Mus musculus/domesticus
Length:	440
Fragment?:	false

•

Protein

E9QA47

Organism:	Mus musculus/domesticus
Length:	478
Fragment?:	false

•

Protein

V9GX43

Organism:	Mus musculus/domesticus
Length:	443
Fragment?:	true

•

Protein

S4R1S7

Organism:	Mus musculus/domesticus
Length:	472
Fragment?:	false

•

Protein

S4R2S7

Organism:	Mus musculus/domesticus
Length:	276
Fragment?:	true

•

Protein

S4R2J2

Organism:	Mus musculus/domesticus
Length:	92
Fragment?:	true

•

Protein

S4R2L5

Organism:	Mus musculus/domesticus
Length:	134
Fragment?:	true

•

Publication

- | J:101977

First Author:	The Jackson Laboratory
Year:	2005
Journal:	Unpublished
Title:	Information obtained from The Jackson Laboratory, Bar Harbor, ME

•

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