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

Tripartite motif containing 54

MURF3, MURF, muscle-specific RING-finger protein
The protein encoded by this gene contains a RING finger motif and is highly similar to the ring finger proteins RNF28/MURF1 and RNF29/MURF2. In vitro studies demonstrated that this protein, RNF28, and RNF29 form heterodimers, which may be important for the regulation of titin kinase and microtubule-dependent signal pathways in striated muscles. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, fibrillin-1, Akt, myostatin, Insulin
Papers using MURF3 antibodies
Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
Gregorio Carol C. et al., In The Journal of Cell Biology, 1999
... For a survey of potential MURF-1 interactions, a full-length MURF-1 cDNA fragment was amplified from human skeletal muscle cDNA by PCR (Saiki et al., 1985) and inserted into pAS2-1 (Matchmaker system II; CLONTECH Laboratories, Inc.) to obtain ...
United Kingdom Co-ordinating Committee in Cancer Research (UKCCR) guidelines for the welfare of animals in experimental neoplasia (second Edition)
Tisdale M J et al., In British Journal of Cancer, 1997
... Goat polyclonal antiserum to MURF3 (E3) and peroxidase-conjugated rabbit polyclonal antisera to goat IgG were purchased from Abcam Ltd (Cambridge, UK) ...
Papers on MURF3
The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass.
Reznick et al., Haifa, Israel. In Free Radic Biol Med, Jan 2016
Since their identification in 2001, the muscle specific E3s, muscle RING finger-1 (MuRF-1) and muscle atrophy F-box (MAFbx), have been shown to be implicated in the regulation of skeletal muscle atrophy in various pathological and physiological conditions.
Time-course changes of catabolic proteins following muscle atrophy induced by dexamethasone.
Amaral et al., São Carlos, Brazil. In Steroids, Jan 2016
Muscle ringer finger1 (MuRF-1), atrogin-1 and myostatin protein levels were analyzed in the tibialis anterior (TA), flexor hallucis longus (FHL) and soleus muscles.
Antioxidant supplementation accelerates cachexia development by promoting tumor growth in C26 tumor-bearing mice.
Rébillard et al., Rennes, France. In Free Radic Biol Med, Jan 2016
Antioxidants supplementation failed to prevent (i) the increase in plasma TNF-α levels and systemic oxidative damage, (ii) skeletal muscle atrophy and (iii) activation of the ubiquitin-proteasome system (MuRF-1, MAFbx and polyubiquitinated proteins).
Activin-βC modulates cachexia by repressing the ubiquitin-proteasome and autophagic degradation pathways.
Gold et al., Dunedin, New Zealand. In J Cachexia Sarcopenia Muscle, Dec 2015
RESULTS: Increased levels of atrogin-1, MuRF-1, Beclin-1, p62, LC3A/B-I, Smad-2 and serum levels of activin-A were noted in the α-KO mice.
Reduced expression of MyHC slow isoform in rat soleus during unloading is accompanied by alterations of endogenous inhibitors of calcineurin/NFAT signaling pathway.
Shenkman et al., Moscow, Russia. In J Muscle Res Cell Motil, Dec 2015
We found that from the 3 day till 14 day of HS the content of MuRF-1 and MuRF-2 in the nuclear fraction fourfold to fivefold increased in HS soleus.
Supplementation of Magnolol Attenuates Skeletal Muscle Atrophy in Bladder Cancer-Bearing Mice Undergoing Chemotherapy via Suppression of FoxO3 Activation and Induction of IGF-1.
Chou et al., Taipei, Taiwan. In Plos One, 2014
The antiatrophic effect of magnolol may be associated with inhibition of myostatin and activin A formation, as well as FoxO3 transcriptional activity resulting from Akt activation, thereby suppressing ubiquitin ligases MuRF-1 and MAFbx/atrogin-1 expression, as well as proteasomal enzyme activity.
The biology of Mur ligases as an antibacterial target.
Paradis-Bleau et al., Montréal, Canada. In Mol Microbiol, 2014
The amide ligases MurC, MurD, MurE and MurF function with the same catalytic mechanism and share conserved amino acid regions and structural features that can conceivably be exploited for the design of inhibitors that simultaneously target more than one enzyme.
Glucocorticoid-induced skeletal muscle atrophy.
Thissen et al., Brussels, Belgium. In Int J Biochem Cell Biol, 2013
The stimulation by GC of these two proteolytic systems is mediated through the increased expression of several Atrogenes ("genes involved in atrophy"), such as FOXO, Atrogin-1, and MuRF-1.
Mechanisms stimulating muscle wasting in chronic kidney disease: the roles of the ubiquitin-proteasome system and myostatin.
Mitch et al., Houston, United States. In Clin Exp Nephrol, 2013
In muscle, the specific ligases are Atrogin-1 and MuRF-1, and their expression has characteristics of a biomarker of accelerated muscle proteolysis.
Atrogin-1, MuRF-1, and sarcopenia.
Mendias et al., Ann Arbor, United States. In Endocrine, 2013
Atrogin-1 and MuRF-1 are two E3 ubiquitin ligases that are important regulators of ubiquitin-mediated protein degradation in skeletal muscle.
MuRFs: specialized members of the TRIM/RBCC family with roles in the regulation of the trophic state of muscle and its metabolism.
Labeit et al., Liverpool, United Kingdom. In Adv Exp Med Biol, 2011
Here, we review recent progress on the structural biology of MuRF1, the MuRF family member being most clearly associated with muscle diseases.
Developmental regulation of MURF ubiquitin ligases and autophagy proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly and turnover.
Gautel et al., London, United Kingdom. In Dev Biol, 2011
Knockdown of both MURF2 and MURF3 severely disrupts the formation of ordered Z- and M-bands, likely by perturbed tubulin dynamics
Rapid disuse atrophy of diaphragm fibers in mechanically ventilated humans.
Shrager et al., United States. In N Engl J Med, 2008
increased active caspase-3 expression of 100% (P=0.05), a 200% higher ratio of atrogin-1 messenger RNA (mRNA) transcripts to MBD4 (a housekeeping gene) (P=0.002), and a 590% higher ratio of MuRF-1 mRNA transcripts to MBD4 (P=0.001).
Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3.
Olson et al., Dallas, United States. In J Clin Invest, 2007
muscle RING finger 1 and muscle RING finger 3 as key E3 ubiquitin ligases for the ubiquitin proteasome system-dependent turnover of sarcomeric proteins and reveal a potential basis for myosin storage myopathies
Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction.
Olson et al., Dallas, United States. In Proc Natl Acad Sci U S A, 2007
MuRF3 has an essential role in maintaining cardiac integrity and function after acute myocardial infarction and turnover of FHL2 and gamma-filamin contributes to this cardioprotective function of MuRF3
Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein.
Olson et al., Dallas, United States. In J Cell Biol, 2000
Functional analysis of the mouse counterpart.
The MURF3 gene of T. brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase.
Stuart et al., Seattle, United States. In Cell, 1990
Mitochondrial MURF3 transcripts of T. brucei are extensively edited by the addition and deletion of uridines.
Guide RNAs in kinetoplastid mitochondria have a nonencoded 3' oligo(U) tail involved in recognition of the preedited region.
Simpson et al., Los Angeles, United States. In Cell, 1990
Maxicircle-encoded guide RNAs (gRNAs) for cytochrome b and maxicircle unidentified reading frames 2 and 3 (MURF2 and MURF3) were isolated by hybrid selection and sequenced.
Editing of kinetoplastid mitochondrial mRNAs by uridine addition and deletion generates conserved amino acid sequences and AUG initiation codons.
Simpson et al., Los Angeles, United States. In Cell, 1988
Uridine additions and deletions in the 5' ends of the COIII, MURF2, and MURF3 transcripts create new N-terminal amino acid sequences that are conserved between species, and new AUG initiation codons in several cases.
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