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

PRP40 pre-mRNA processing factor 40 homolog A

Top mentioned proteins: ACID, CAN, Urease, MBL, HAD
Papers on HYPA
On-line coupling of continuous-flow gel electrophoresis with inductively coupled plasma-mass spectrometry to quantitatively evaluate intracellular metal binding properties of metallochaperones HpHypA and HpHspA in E. coli cells.
Sun et al., Hong Kong, Hong Kong. In Metallomics, Oct 2015
Herein, we examine the feasibility of the GE-ICP-MS system in the quantitative analysis of intracellular metal binding properties using two Helicobacter pylori metallochaperones HypA and HspA overexpressed in E. coli cells as showcases.
Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.
Miki et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, Jul 2015
The Ni atom at the catalytic center of [NiFe] hydrogenases is incorporated by a Ni-metallochaperone, HypA, and a GTPase/ATPase, HypB.
Specificity of the Zn(2+), Cd(2+) and Ni(2+) ion binding sites in the loop domain of the HypA protein.
Kozlowski et al., Wrocław, Poland. In Dalton Trans, Jul 2015
The zinc binding loop domain of the HypA protein of Helicobacter pylori consists of two CXXC motifs with flanking His residues.
UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.
Sun et al., Hong Kong, Hong Kong. In J Biol Chem, Jun 2015
Importantly, we demonstrate for the first time that UreE serves as a bridge to grasp Ni(2+) from HypA, subsequently donating it to UreG.
TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabERAB11.
Peñalva et al., London, United Kingdom. In Proc Natl Acad Sci U S A, May 2015
In Aspergillus nidulans, RabO(RAB1) resides in the Golgi, RabE(RAB11) localizes to exocytic post-Golgi carriers undergoing transport to the apex, and hypA encodes Trs120.
Dynamic HypA zinc site is essential for acid viability and proper urease maturation in Helicobacter pylori.
Maroney et al., Bethesda, United States. In Metallomics, Apr 2015
Urease is regulated in part by nickelation, a process that requires the HypA protein, which is a putative nickel metallochaperone that is generally associated with hydrogenase maturation.
[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
Minimally six accessory proteins (HypA-HypF) are necessary for NiFe(CN)2CO cofactor biosynthesis in Escherichia coli.
Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori.
Sun et al., Hong Kong, Hong Kong. In Metallomics, 2014
In this work, we characterized the molecular details of the interaction of metallochaperones UreE and HypA in Helicobacter pylori.
Mannose-binding lectin exon 1 and promoter polymorphisms in tuberculosis disease in a Mediterranean area.
Payeras-Cifré et al., Palma, Spain. In Int J Immunogenet, 2014
The diplotype LYQA/HYPA was present in 12 out of 57 of the pulmonary TB cases but in none of the extrapulmonary TB patients.
Effect of Chelate Type and Radioisotope on the Imaging Efficacy of 4 Fibrin-Specific PET Probes.
Caravan et al., United States. In J Nucl Med, 2014
METHODS: Probes were synthesized using a known fibrin-specific peptide conjugated to either NODAGA (FBP8, FBP10) or NOTA-monoamide (FBP9, FBP11) as chelators, followed by labeling with (64)Cu (FBP8 and FBP9) or Al(18)F (FBP10 and FBP11).
Mannose-binding lectin genetic analysis: possible protective role of the HYPA haplotype in the development of recurrent urinary tract infections in men.
Castaldo et al., Napoli, Italy. In Int J Infect Dis, 2014
The frequencies of the L allele (-550) and the HYPA haplotype were higher in controls than in patients stratified according to sex (p < 0.05).
Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.
Zamble et al., Toronto, Canada. In Biochemistry, 2013
The two accessory proteins HypA and HypB interact with each other and are thought to cooperate to insert nickel into the active site of the hydrogenase-3 precursor protein.
Identification and structure of a novel archaeal HypB for [NiFe] hydrogenase maturation.
Miki et al., Kyoto, Japan. In J Mol Biol, 2013
HypB (metal-binding GTPase) and HypA (nickel metallochaperone) are required for nickel insertion into [NiFe] hydrogenase.
Specific metal recognition in nickel trafficking.
Maroney et al., Amherst Center, United States. In Biochemistry, 2012
We also illustrate a variety of mechanisms, including molecular recognition in the case of NikA protein and examples of allosteric regulation for HypA, NikR, and RcnR, employed to generate specific biological responses to nickel ions.
Structural basis of [NiFe] hydrogenase maturation by Hyp proteins.
Miki et al., Kyoto, Japan. In Biol Chem, 2012
HypA and HypB are involved in the Ni insertion, whereas the other four Hyp proteins (HypCDEF) are required for the biosynthesis, assembly and insertion of the Fe(CN)2CO group.
Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA.
Sun et al., Hong Kong, Hong Kong. In J Biol Chem, 2012
The unique N terminus of H. pylori HypB was identified to participate in the interaction with H. pylori HypA.
Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA).
Hu et al., Shanghai, China. In J Biol Chem, 2011
Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA).
A transient and low-populated protein-folding intermediate at atomic resolution.
Kay et al., Toronto, Canada. In Science, 2010
an atomic-resolution structure of an "invisible" folding intermediate of a small protein module: the FF domain; structure reveals non-native elements preventing formation of native conformation in the carboxyl-terminal part of the protein
Structure of FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group II/III WW domains.
Tanokura et al., Tokyo, Japan. In J Biol Chem, 2007
FBP11 binding mechanism underlies the molecular pathology of severe neurological disorders, e.g., Rett syndrome and Huntington disease.
Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis.
Coghlan et al., Beaverton, United States. In Neuromolecular Med, 2004
NAKAP-HypA scaffold is a potential nuclear docking site for huntingtin protein and may contribute to the nuclear accumulation of huntingtin observed in HD.
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