Biochimica et biophysica acta最新文献_第2页

Retraction notice to "Immunosuppressive networks in the tumour environment and their effect in dendritic cells".[Biochim. Biophys. Acta (1795) (2009) 16-24]. “肿瘤环境中的免疫抑制网络及其在树突状细胞中的作用”的撤回通知[生物化学]。Biophys。学报(1795)(2009)16-24]。

Biochimica et biophysica acta Pub Date : 2013-04-01

引用次数: 0

Chromatin-mediated Candida albicans virulence. 染色质介导的白色念珠菌毒力。

Biochimica et biophysica acta Pub Date : 2013-03-01

Jessica Lopes da Rosa, Paul D Kaufman

引用次数: 0

Centromeric chromatin and the pathway that drives its propagation. 着丝粒染色质和驱动其繁殖的途径。

Biochimica et biophysica acta Pub Date : 2013-03-01

Samantha J Falk, Ben E Black

引用次数: 0

Lessons from senescence: chromatin maintenance in non-proliferating cells. 衰老的教训:非增殖细胞的染色质维持。

Biochimica et biophysica acta Pub Date : 2013-03-01

Taranjit Singh Rai, Peter D Adams

引用次数: 0

Transport of inorganic phosphate in Leishmania infantum and compensatory regulation at low inorganic phosphate concentration. 幼利什曼原虫体内无机磷酸盐的转运及低无机磷酸盐浓度下的代偿调节。

Biochimica et biophysica acta Pub Date : 2013-03-01

T Russo-Abrahão, M Alves-Bezerra, D Majerowicz, A L Freitas-Mesquita, C F Dick, K C Gondim, J R Meyer-Fernandes

{"title":"Transport of inorganic phosphate in Leishmania infantum and compensatory regulation at low inorganic phosphate concentration.","authors":"T Russo-Abrahão, M Alves-Bezerra, D Majerowicz, A L Freitas-Mesquita, C F Dick, K C Gondim, J R Meyer-Fernandes","doi":"","DOIUrl":"","url":null,"abstract":"Background: Proliferation of Leishmania infantum depends on exogenous inorganic phosphate (P(i)) but little is known about energy metabolism and transport of P(i) across the plasma membrane in Leishmania sp.Methods: We investigated the kinetics of 32P(i) transport, the influence of H+ and K+ ionophores and inhibitors, and expression of the genes for the Na+:P(i) and H+:P(i) cotransporters.Results: The proton ionophore FCCP, bafilomycin A1 (vacuolar ATPase inhibitor), nigericin (K+ ionophore) and SCH28080 (an inhibitor of H+, K(+)-ATPase) all inhibited the transport of P(i). This transport showed Michaelis-Menten kinetics with K0.5 and V(max) values of 0.016 +/- 0.002 mM and 564.9 +/- 18.06 pmol x h(-1) x 10(-7) cells, respectively. These values classify the P(i) transporter of L. infantum among the high-affinity transporters, a group that includes Pho84 of Saccharomyces cerevisiae. Two sequences were identified in the L. infantum genome that code for phosphate transporters. However, transcription of the PHO84 transporter was 10-fold higher than the PHO89 transporter in this parasite. Accordingly, P(i) transport and LiPho84 gene expression were modulated by environmental P(i) variations.Conclusions: These findings confirm the presence of a P(i) transporter in L. infantum, similar to PHO84 in S. cerevisiae, that contributes to the acquisition of inorganic phosphate and could be involved in growth and survival of the promastigote forms of L. infantum.General significance: This work provides the first description of a PHO84-like P(i) transporter in a Trypanosomatide parasite of the genus Leishmania, responsible for many infections worldwide.","PeriodicalId":8811,"journal":{"name":"Biochimica et biophysica acta","volume":"1830 3","pages":"2683-9"},"PeriodicalIF":0.0,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31428075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The role of FACT in making and breaking nucleosomes. FACT在制造和破坏核小体中的作用。

Biochimica et biophysica acta Pub Date : 2013-03-01

Tim Formosa

{"title":"The role of FACT in making and breaking nucleosomes.","authors":"Tim Formosa","doi":"","DOIUrl":"","url":null,"abstract":"FACT is a roughly 180 kDa heterodimeric protein complex important for managing the properties of chromatin in eukaryotic cells. Chromatin is a repressive barrier that plays an important role in protecting genomic DNA and regulating access to it. This barrier must be temporarily removed during transcription, replication, and repair, but it also must be rapidly restored to the original state afterwards. Further, the properties of chromatin are dynamic and must be adjusted as conditions dictate. FACT was identified as a factor that destabilizes nucleosomes in vitro, but it has now also been implicated as a central factor in the deposition of histones to form nucleosomes, as an exchange factor that swaps the histones within existing nucleosomes for variant forms, and as a tether that prevents histones from being displaced by the passage of RNA polymerases during transcription. FACT therefore plays central roles in building, maintaining, adjusting. and overcoming the chromatin barrier. This review summarizes recent results that have begun to reveal how FACT can promote what appear to be contradictory goals, using a simple set of binding activities to both enhance and diminish the stability of nucleosomes. This article is part of a Special Issue entitled: Histone chaperones and Chromatin assembly.","PeriodicalId":8811,"journal":{"name":"Biochimica et biophysica acta","volume":"1819 3-4","pages":"247-55"},"PeriodicalIF":0.0,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32058971","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Green tea catechins can bind and modify ERp57/PDIA3 activity. 绿茶儿茶素可以结合和修饰ERp57/PDIA3的活性。

Biochimica et biophysica acta Pub Date : 2013-03-01

Lucie Trnková, Daniela Ricci, Caterina Grillo, Gianni Colotti, Fabio Altieri

{"title":"Green tea catechins can bind and modify ERp57/PDIA3 activity.","authors":"Lucie Trnková, Daniela Ricci, Caterina Grillo, Gianni Colotti, Fabio Altieri","doi":"","DOIUrl":"","url":null,"abstract":"Background: Green tea is a rich source of polyphenols, mainly catechins (flavanols), which significantly contribute to the beneficial health effects of green tea in the prevention and treatment of various diseases. In this study the effects of four green tea catechins on protein ERp57, also known as protein disulfide isomerase isoform A3 (PDIA3), have been investigated in an in vitro model.Methods: The interaction of catechins with ERp57 was explored by fluorescence quenching and surface plasmon resonance techniques and their effect on ERp57 activities was investigated.Results: A higher affinity was observed for galloylated cathechins, which bind close to the thioredoxin-like redox-sensitive active sites of the protein, with a preference for the oxidized form. The effects of these catechins on ERp57 properties were also investigated and a moderate inhibition of the reductase activity of ERp57 was observed as well as a strong inhibition of ERp57 DNA binding activity.Conclusions: Considering the high affinity of galloylated catechins for ERp57 and their capability to inhibit ERp57 binding to other macromolecular ligands, some effects of catechins interaction with this protein on eukaryotic cells may be expected.General significance: This study provides information to better understand the molecular mechanisms underlying the biological activities of catechins and to design new polyphenol-based ERp57-specific inhibitors.","PeriodicalId":8811,"journal":{"name":"Biochimica et biophysica acta","volume":"1830 3","pages":"2671-82"},"PeriodicalIF":0.0,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31428074","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

All roads lead to chromatin: multiple pathways for histone deposition. 所有途径都通向染色质:组蛋白沉积的多种途径。

Biochimica et biophysica acta Pub Date : 2013-03-01

Qing Li, Rebecca Burgess, Zhiguo Zhang

引用次数: 0

Histone chaperones and chromatin assembly. 组蛋白伴侣和染色质组装。

Biochimica et biophysica acta Pub Date : 2013-03-01

Paul Kaufman

引用次数: 0

Histone chaperones link histone nuclear import and chromatin assembly. 组蛋白伴侣连接组蛋白核输入和染色质组装。

Biochimica et biophysica acta Pub Date : 2013-03-01

Kristin M Keck, Lucy F Pemberton

{"title":"Histone chaperones link histone nuclear import and chromatin assembly.","authors":"Kristin M Keck, Lucy F Pemberton","doi":"","DOIUrl":"","url":null,"abstract":"Histone chaperones are proteins that shield histones from nonspecific interactions until they are assembled into chromatin. After their synthesis in the cytoplasm, histones are bound by different histone chaperones, subjected to a series of posttranslational modifications and imported into the nucleus. These evolutionarily conserved modifications, including acetylation and methylation, can occur in the cytoplasm, but their role in regulating import is not well understood. As part of histone import complexes, histone chaperones may serve to protect the histones during transport, or they may be using histones to promote their own nuclear localization. In addition, there is evidence that histone chaperones can play an active role in the import of histones. Histone chaperones have also been shown to regulate the localization of important chromatin modifying enzymes. This review is focused on the role histone chaperones play in the early biogenesis of histones, the distinct cytoplasmic subcomplexes in which histone chaperones have been found in both yeast and mammalian cells and the importins/karyopherins and nuclear localization signals that mediate the nuclear import of histones. We also address the role that histone chaperone localization plays in human disease. This article is part of a Special Issue entitled: Histone chaperones and chromatin assembly.","PeriodicalId":8811,"journal":{"name":"Biochimica et biophysica acta","volume":"1819 3-4","pages":"277-89"},"PeriodicalIF":0.0,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32058970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0