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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 01 Sep 2015.

SMT3 Smt3p

Smt3, SUMO, Smt3p, Pmt3
Top mentioned proteins: Ubiquitin, CAN, DAPI, SUMO-2, Ubc9
Papers using Smt3 antibodies
Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity.
Supplier
Cobine Paul, In PLoS ONE, 1997
... Aos1/ Uba2, Ubc9, SUMO-1 and SUMO-1 rabbit monoclonal antibody were purchased with the SUMOlink kit from Active Motif, Carlsbad, CA ...
Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation
Supplier
Malumbres Marcos et al., In Frontiers in Oncology, 1997
... SUMOylation of recombinant Aurora-A protein was tested using Active Motif SUMO link (Active Motif, #40120) and following manufacturer’s ...
SUMO-2/3 regulates topoisomerase II in mitosis
Supplier
Dasso Mary et al., In The Journal of Cell Biology, 1986
... The processed and full-length forms of SUMO-2 and -3 were cloned into pGEX4T-1, fused at their NH2 termini to an EGFP fragment that was excised from a pEGFP C-1 plasmid (CLONTECH Laboratories, Inc.) ...
Papers on Smt3
Sumoylation of Sir2 differentially regulates transcriptional silencing in yeast.
New
Mishra et al., Hyderābād, India. In Nucleic Acids Res, 28 Sep 2015
We identify Siz2 as the key SUMO ligase and show that multiple lysines in Sir2 are subject to this sumoylation activity.
The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells.
New
Rudd et al., Cambridge, United Kingdom. In Mol Cell, 26 Sep 2015
Here, we show that the immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the NPC, and that this interaction is needed for optimal NFATc1 and NF-κB p65 nuclear entry in T cells.
DeSUMOylation: An Important Therapeutic Target and Protein Regulatory Event.
New
Huo et al., Wuhan, China. In Dna Cell Biol, 26 Sep 2015
UNASSIGNED: The discovery of the process of small ubiquitin-like modifier (SUMO)-mediated post-translational modification of targets (SUMOylation) in early 1990s proved to be a significant step ahead in understanding mechanistic regulation of proteins and their functions in diverse life processes at the cellular level.
Expression of plectasin in Bacillus subtilis using SUMO technology by a maltose-inducible vector.
New
Li et al., Harbin, China. In J Ind Microbiol Biotechnol, 25 Sep 2015
To explore an effective approach for expressing plectasin in Bacillus subtilis, the sequence encoding plectasin fused with the small ubiquitin-like modifier (SUMO) gene, the 6 × His gene and the signal peptide of SacB were cloned into an E. coli-B.
Ubiquitylation, neddylation and the DNA damage response.
Review
New
Jackson et al., Cambridge, United Kingdom. In Open Biol, Apr 2015
Ubiquitin and the ubiquitin-like protein (UBL) SUMO have established roles in regulating the cellular response to DNA double-strand breaks (DSBs).
Sumo and the cellular stress response.
Review
New
Enserink, Oslo, Norway. In Cell Div, Dec 2014
The ubiquitin family member Sumo has important functions in many cellular processes including DNA repair, transcription and cell division.
Advances in the development of SUMO specific protease (SENP) inhibitors.
Review
New
Zhang et al., Yokohama, Japan. In Comput Struct Biotechnol J, Dec 2014
Sumoylation is a reversible post-translational modification that involves the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to their substrate proteins.
Interconnection between flowering time control and activation of systemic acquired resistance.
Review
New
Nandi et al., New Delhi, India. In Front Plant Sci, Dec 2014
SUMO conjugation and deconjugation mechanisms also similarly affect SAR and flowering in an SA-dependent manner.
Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity.
Review
New
Pountney et al., Gold Coast, Australia. In Biomolecules, Dec 2014
α-Synuclein inclusion bodies are a pathological hallmark of several neurodegenerative diseases, including Parkinson's disease, and contain aggregated α-synuclein and a variety of recruited factors, including protein chaperones, proteasome components, ubiquitin and the small ubiquitin-like modifier, SUMO-1.
Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.
Review
New
Impact
Wilkinson et al., Bristol, United Kingdom. In Physiol Rev, Oct 2014
Hundreds of different proteins are SUMO substrates, and dysfunction of protein SUMOylation is implicated in a many different diseases.
Sumoylation pathway is required to maintain the basal breast cancer subtype.
New
Impact
Weigel et al., Iowa City, United States. In Cancer Cell, Jul 2014
Disruption of the sumoylation pathway by knockdown of sumoylation enzymes, mutation of the SUMO-target lysine of TFAP2A, or treatment with sumoylation inhibitors induced a basal-to-luminal transition, which was dependent on TFAP2A.
Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212 regulate meiotic recombination.
New
Impact
Hunter et al., Davis, United States. In Nat Genet, Feb 2014
Designation of crossovers involves selective localization of the SUMO ligase RNF212 to a minority of recombination sites, where it stabilizes pertinent factors such as MutSγ (ref.
Cbx4 governs HIF-1α to potentiate angiogenesis of hepatocellular carcinoma by its SUMO E3 ligase activity.
New
Impact
Chen et al., Shanghai, China. In Cancer Cell, Feb 2014
Cbx4 is a polycomb group protein that is also a SUMO E3 ligase, but its potential roles in tumorigenesis remain to be explored.
Control of nuclear activities by substrate-selective and protein-group SUMOylation.
Review
Impact
Psakhye et al., Martinsried, Germany. In Annu Rev Genet, 2012
Reversible modification of proteins by SUMO (small ubiquitin-like modifier) affects a large number of cellular processes.
Using dot blot with immunochemical detection to evaluate global changes in SUMO-2/3 conjugation.
Knejzlík et al., Praha, Czech Republic. In Biotechniques, 2012
Small ubiquitin-related modifier-2/3 (SUMO-2/3) is a member of the ubiquitin-like (Ubl) protein family.
Drosophila Smt3 negatively regulates JNK signaling through sequestering Hipk in the nucleus.
GeneRIF
Jiao et al., Beijing, China. In Development, 2011
although knockdown of the homeodomain-interacting protein kinase (Hipk) suppresses Smt3 depletion-induced activation of JNK, Hipk overexpression synergistically enhances this type of JNK activation
Ubiquitin-proteasome genes as targets for modulation of cisplatin sensitivity in fission yeast.
GeneRIF
Perego et al., Milano, Italy. In Bmc Genomics, 2010
Data show that pmt3 mutants exhibiting hypersensitivity to cisplatin.
Role of the Zn(2+) motif of E1 in SUMO adenylation.
GeneRIF
Chen et al., Duarte, United States. In J Biol Chem, 2010
the Zn(2+) motif of E1 has a role in SUMO adenylation
Cdk1 and SUMO regulate Swe1 stability.
GeneRIF
Brandeis et al., Jerusalem, Israel. In Plos One, 2009
Cdk1 and SUMO (Smt3) regulate Swe1 stability
Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation.
GeneRIF
Courey et al., Los Angeles, United States. In Plos One, 2008
SUMO coordinates multiple regulatory processes during oogenesis and early embryogenesis
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