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

Enolase-phosphatase 1

E1 enzyme, E-I enzyme
Top mentioned proteins: Ubiquitin, V1a, CAN, Smt3, STEP
Papers on E1 enzyme
Facile synthesis of covalent probes to capture enzymatic intermediates during E1 enzyme catalysis.
Statsyuk et al., Evanston, United States. In Chem Commun (camb), Dec 2015
UNASSIGNED: We report a facile synthetic strategy to prepare UBL-AMP electrophilic probes that form a covalent bond with the catalytic cysteine of cognate E1s, mimicking the tetrahedral intermediate of the E1-UBL-AMP complex.
UFBP1, a Key Component of the Ufm1 Conjugation System, Is Essential for Ufmylation-Mediated Regulation of Erythroid Development.
Li et al., Wuhu, China. In Plos Genet, Nov 2015
Interestingly, depletion of Uba5, a Ufm1 E1 enzyme, also caused elevation of ER stress and under-expression of erythroid transcription factors in erythroleukemia K562 cells.
Ubiquitin related modifier-1 (LdUrm1): an early endosome associated ubiquitin like conjugation in Leishmania donovani.
Salotra et al., New Delhi, India. In Mol Microbiol, Nov 2015
We identified LdUba4 as the E1 enzyme for LdUrm1 and demonstrated its energy dependent enzymatic activity.
A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation.
Zhou et al., San Diego, United States. In Plos One, 2014
We applied this method to analyze the auto-sumoylation of the E1 enzyme in vitro and compared it to the GG-remnant method using Smt3-I96R as a substrate.
Archaeal Inorganic Pyrophosphatase Displays Robust Activity under High-Salt Conditions and in Organic Solvents.
Maupin-Furlow et al., Gainesville, United States. In Appl Environ Microbiol, 2014
To demonstrate that HvPPA could drive thermodynamically unfavorable reactions to completion under conditions of reduced water activity, a novel coupled assay was developed; HvPPA hydrolyzed the PPi by-product generated in 2 M NaCl by UbaA (a "salt-loving" noncanonical E1 enzyme that adenylates ubiquitin-like proteins in the presence of ATP).
Ubiquitin-conjugating enzyme E2C: a potential cancer biomarker.
Dong et al., Sydney, Australia. In Int J Biochem Cell Biol, 2014
The core domain is required for ubiquitin adduct formation by interacting with the ubiquitin-fold domain in the E1 enzyme, and contributes to the E3 enzyme binding.
Uba1 functions in Atg7- and Atg3-independent autophagy.
Baehrecke et al., Worcester, United States. In Nat Cell Biol, 2013
Rather, Uba1, the E1 enzyme used in ubiquitylation, is required for autophagy and reduction of cell size.
Two ubiquitin-like conjugation systems that mediate membrane formation during autophagy.
Nakatogawa, Yokohama, Japan. In Essays Biochem, 2012
Sequential reactions by the E1 enzyme Atg7 and the E2 enzyme Atg10 conjugate Atg12 to the lysine residue in Atg5, and the resulting Atg12-Atg5 conjugate forms a complex with Atg16.
Archaeal proteasomes and sampylation.
Maupin-Furlow, Gainesville, United States. In Subcell Biochem, 2012
Unlike eukaryotes, sampylation only requires an E1 enzyme homolog of the E1-E2-E3 ubiquitylation cascade to mediate protein conjugation.
E3 ubiquitin ligase-mediated regulation of bone formation and tumorigenesis.
Marie et al., Paris, France. In Cell Death Dis, 2012
The ubiquitination of proteins occurs through a three-step process involving ubiquitin activation by the E1 enzyme, allowing for the transfer to a ubiquitin-conjugated enzyme E2 and to the targeted protein via ubiquitin-protein ligases (E3), the most abundant group of enzymes involved in ubiquitination.
[Study on natural products for drug development].
Tsukamoto, Kumamoto, Japan. In Yakugaku Zasshi, 2010
We succeeded in isolating various compounds with three distinct inhibitory activities against an E1 enzyme reaction, Ubc13 (E2)-Uev1A interaction, and p53-HDM2 (E3) interaction as well as the proteasome inhibitors.
ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death.
Debnath et al., San Francisco, United States. In Cell, 2010
ATG12-ATG3 complex formation requires ATG7 as the E1 enzyme and ATG3 autocatalytic activity as the E2, resulting in the covalent linkage of ATG12 onto a single lysine on ATG3.
Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8.
Schulman et al., Memphis, United States. In Nature, 2003
We report here the structure and mutational analysis of human APPBP1-UBA3, the heterodimeric E1 enzyme for NEDD8 (ref.
The nucleoporin RanBP2 has SUMO1 E3 ligase activity.
Melchior et al., Martinsried, Germany. In Cell, 2002
SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9.
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Schindelin et al., Stony Brook, United States. In Nature, 2001
The activation of ubiquitin and related protein modifiers is catalysed by members of the E1 enzyme family that use ATP for the covalent self-attachment of the modifiers to a conserved cysteine.
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