BMC Biochemistry

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Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-Like kinase Mst3
BMC Biochemistry - - 2011
Johnthan Gordon, Juyeon Hwang, Karma J Carrier, Candace A Jones, Quiana L Kern, Carlos S Moreno, Richard H Karas, David C Pallas
Striatin, a putative protein phosphatase 2A (PP2A) B-type regulatory subunit, is a multi-domain scaffolding protein that has recently been linked to several diseases including cerebral cavernous malformation (CCM), which causes symptoms ranging from headaches to stroke. Striatin association with the PP2A A/C (structural subunit/catalytic subunit) heterodimer alters PP2A substrate specificity, but ...... hiện toàn bộ
Low-magnesium, trans-cleavage activity by type III, tertiary stabilized hammerhead ribozymes with stem 1 discontinuities
BMC Biochemistry - Tập 6 - Trang 1-9 - 2005
Donald H Burke, S Travis Greathouse
Low concentrations of free magnesium in the intracellular environment can present critical limitations for hammerhead ribozymes, especially for those that are designed for intermolecular (trans) cleavage of a host or pathogen RNA. Tertiary stabilizing motifs (TSM's) from natural and artificial ribozymes with a "type I" topology have been exploited to stabilize trans-cleaving hammerheads. Ribozymes...... hiện toàn bộ
Preferential inhibition of xanthine oxidase by 2-amino-6-hydroxy-8-mercaptopurine and 2-amino-6-purine thiol
BMC Biochemistry - Tập 8 - Trang 1-11 - 2007
Sukirti Kalra, Gopabandhu Jena, Kulbhushan Tikoo, Anup Kumar Mukhopadhyay
The anticancer drug, 6-mercaptopurine (6MP) is subjected to metabolic clearance through xanthine oxidase (XOD) mediated hydroxylation, producing 6-thiouric acid (6TUA), which is excreted in urine. This reduces the effective amount of drug available for therapeutic efficacy. Co-administration of allopurinol, a suicide inhibitor of XOD, which blocks the hydroxylation of 6MP inadvertently enhances th...... hiện toàn bộ
A study on the two binding sites of hexokinase on brain mitochondria
BMC Biochemistry - Tập 8 - Trang 1-6 - 2007
Abolfazl Golestani, Hassan Ramshini, Mohsen Nemat-Gorgani
Type I hexokinase (HK-I) constitutes the predominant form of the enzyme in the brain, a major portion of which is associated with the outer mitochondrial membrane involving two sets of binding sites. In addition to the glucose-6-phosphate (G6P)-sensitive site (Type A), the enzyme is bound on a second set of sites (Type B) which are, while insensitive to G6P, totally releasable by use of high conce...... hiện toàn bộ
Analysis of Escherichia coli nicotinate mononucleotide adenylyltransferase mutants in vivo and in vitro
BMC Biochemistry - Tập 6 - Trang 1-9 - 2005
Martin Stancek, Robert Schnell, Monica Rydén-Aulin
Adenylation of nicotinate mononucleotide to nicotinate adenine dinucleotide is the penultimate step in NAD+ synthesis. In Escherichia coli, the enzyme nicotinate mononucleotide adenylyltransferase is encoded by the nadD gene. We have earlier made an initial characterization in vivo of two mutant enzymes, NadD72 and NadD74. Strains with either mutation have decreased intracellular levels of NAD+, e...... hiện toàn bộ
Similarity of molecular phenotype between known epilepsy gene LGI1 and disease candidate gene LGI2
BMC Biochemistry - Tập 11 - Trang 1-13 - 2010
Vachiranee Limviphuvadh, Ling Ling Chua, Rabi 'Atul' Adawiyah Bte Rahim, Frank Eisenhaber, Sebastian Maurer-Stroh, Sharmila Adhikari
The LGI2 (leucine-rich, glioma inactivated 2) gene, a prime candidate for partial epilepsy with pericentral spikes, belongs to a family encoding secreted, beta-propeller domain proteins with EPTP/EAR epilepsy-associated repeats. In another family member, LGI1 (leucine-rich, glioma inactivated 1) mutations are responsible for autosomal dominant lateral temporal epilepsy (ADLTE). Because a few LGI1 ...... hiện toàn bộ
Characterization of association of human mitochondrial lysyl-tRNA synthetase with HIV-1 Pol and tRNA3Lys
BMC Biochemistry - Tập 19 - Trang 1-10 - 2018
Fawzi Khoder-Agha, José M. Dias, Martine Comisso, Marc Mirande
An important step in human immunodeficiency virus type 1 (HIV-1) replication is the packaging of tRNA3Lys from the host cell, which plays the role of primer RNA in the process of initiation of reverse transcription. The viral GagPol polyprotein precursor, and the human mitochondrial lysyl-tRNA synthetase (mLysRS) from the host cell, have been proposed to be involved in the packaging process. More ...... hiện toàn bộ
Biosynthesis of the proteasome inhibitor syringolin A: the ureido group joining two amino acids originates from bicarbonate
BMC Biochemistry - Tập 10 - Trang 1-9 - 2009
Christina Ramel, Micha Tobler, Martin Meyer, Laurent Bigler, Marc-Olivier Ebert, Barbara Schellenberg, Robert Dudler
Syringolin A, an important virulence factor in the interaction of the phytopathogenic bacterium Pseudomonas syringae pv. syringae B728a with its host plant Phaseolus vulgaris (bean), was recently shown to irreversibly inhibit eukaryotic proteasomes by a novel mechanism. Syringolin A is synthesized by a mixed non-ribosomal peptide synthetase/polyketide synthetase and consists of a tripeptide part i...... hiện toàn bộ
Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
BMC Biochemistry - - 2005
Toumy Guettouche, Frank Boellmann, William S Lane, Richard Voellmy
Heat shock factor (HSF/HSF1) not only is the transcription factor primarily responsible for the transcriptional response of cells to physical and chemical stress but also coregulates other important signaling pathways. The factor mediates the stress-induced expression of heat shock or stress proteins (HSPs). HSF/HSF1 is inactive in unstressed cells and is activated during stress. Activation is acc...... hiện toàn bộ
Probing the stability of the “naked” mucin-like domain of human α-dystroglycan
BMC Biochemistry - Tập 14 - Trang 1-7 - 2013
Manuela Bozzi, Enrico Di Stasio, Giovanni Luca Scaglione, Claudia Desiderio, Claudia Martelli, Bruno Giardina, Francesca Sciandra, Andrea Brancaccio
α-Dystroglycan (α-DG) is heavily glycosylated within its central mucin-like domain. The glycosylation shell of α-dystroglycan is known to largely influence its functional properties toward extracellular ligands. The structural features of this α-dystroglycan domain have been poorly studied so far. For the first time, we have attempted a recombinant expression approach in E. coli cells, in order to...... hiện toàn bộ
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