gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

FIC domain containing

Sponsored links
Top mentioned proteins: ACID, CAN, V1a, STEP, HYPA
Papers on Hype
Global profiling of HYPE mediated AMPylation through a chemical proteomic approach.
Tate et al., London, United Kingdom. In Mol Cell Proteomics, Dec 2015
This post-translational modification also exists in eukaryotes, and AMP transferase activity was recently assigned to HYPE (FICD) protein, which is conserved from C. elegans to humans.
An enzymatic method to estimate the content of L-hydroxyproline.
Watanabe et al., Japan. In J Biotechnol, May 2015
In the present study, we attempted to estimate the content of L-Hyp using coupling systems with metabolic enzymes of the T4LHyp (hydroxyproline 2-epimerase (HypE) and cis-4-hydroxy-D-proline dehydrogenase (HypDH)) and T3LHyp pathways (T3LHyp dehydratase (T3LHypD) and Δ(1)-pyrroline-2-carboxylate reductase (Pyr2CR)) from microorganisms.
HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation.
Ploegh et al., Cambridge, United States. In J Biol Chem, May 2015
Here, we describe the generation, evaluation, and application of four HypE-specific nanobodies: three that inhibit HypE-mediated target AMPylation in vitro and one that acts as an activator.
A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response.
Mattoo et al., Stony Brook, United States. In J Biol Chem, Apr 2015
The human genome encodes a single Fic protein, called HYPE (Huntingtin yeast interacting protein E), with adenylyltransferase activity but unknown physiological target(s).
Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions.
Katan et al., In Structure, 2015
Eukaryotic genomes also encode one FIC-domain protein,HYPE, which has remained poorly characterized.Here we describe the structure of human HYPE, solved by X-ray crystallography, representing the first structure of a eukaryotic FIC-domain protein.
[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.
Stripp et al., Halle, Germany. In Biochem J, 2015
It has been shown that the anaerobically purified HypC-HypD-HypE scaffold complex carries the Fe(CN)2CO moiety of this cofactor.
Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution.
Watanabe et al., Japan. In Plos One, 2014
Hydroxyproline epimerase (HypE), which is in the same protein family as ProR, catalyzes the first step of the trans-4-hydroxy-L-proline metabolism of bacteria.
Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl-Group Channeling during [NiFe]-Hydrogenase Cofactor Generation.
Soboh et al., Berlin, Germany. In Plos One, 2014
HypF catalyzes removal of phosphate and transfers the carbamate group to HypE.
Inhibiting AMPylation: a novel screen to identify the first small molecule inhibitors of protein AMPylation.
Thompson et al., Jupiter, United States. In Acs Chem Biol, 2014
Herein we report the discovery of the first small molecule VopS inhibitors (e.g., calmidazolium, GW7647, and MK886) with Ki's ranging from 6 to 50 μM and upward of 30-fold selectivity versus HYPE, the only known human AMPylator.
Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.
Miki et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, 2014
Hydrogenase pleiotropically acting protein (Hyp)E plays a role in biosynthesis of the cyano groups for the NiFe(CN)2CO center of [NiFe] hydrogenases by catalyzing the ATP-dependent dehydration of the carbamoylated C-terminal cysteine of HypE to thiocyanate.
Hype or hypervirulence: a reflection on problematic C. difficile strains.
Smits, Leiden, Netherlands. In Virulence, 2013
Clostridium difficile infections (CDI) have emerged as a major cause of healthcare associated disease, and recent epidemiological evidence also suggests an important role in community-acquired diarrhea.
Crystal structures of the HypCD complex and the HypCDE ternary complex: transient intermediate complexes during [NiFe] hydrogenase maturation.
Miki et al., Kyoto, Japan. In Structure, 2013
The Fe(CN)(2)CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor).
Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases.
Higuchi et al., Japan. In J Biol Chem, 2012
As a remarkable structural feature of hydrogenase active sites, [NiFe]-hydrogenases harbor one carbonyl and two cyano ligands, where HypE and HypF are involved in the biosynthesis of the nitrile group as a precursor of the cyano groups.
Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.
Dehio et al., Basel, Switzerland. In Nature, 2012
After mutation of the inhibitory motif in various Fic proteins, including the human homologue FICD (also known as HYPE), adenylylation activity is considerably boosted, consistent with the anticipated relief of inhibition.
Predicted roles of the uncharacterized clustered genes in aflatoxin biosynthesis.
Ehrlich, New Orleans, United States. In Toxins (basel), 2009
We suggest that HypC catalyzes the oxidation of norsolorinic acid anthrone; AvfA (AflI), the ring-closure step in formation of hydroxyversicolorone; HypB, the second oxidation step in conversion of O-methylsterigmatocystin to AF; and HypE and NorA (AflE), the final two steps in AFB(1) formation.
share on facebooktweetadd +1mail to friends