The Open Biochemistry Journal最新文献

{"title":"Effects of nerve growth factor and nitric oxide synthase inhibitors on amyloid precursor protein mRNA levels and protein stability.","authors":"Janet C Mackinnon,&nbsp;Patricia Huether,&nbsp;Bettina E Kalisch","doi":"10.2174/1874091X01206010031","DOIUrl":"https://doi.org/10.2174/1874091X01206010031","url":null,"abstract":"<p><p>We determined previously that nitric oxide (NO) modulates the nerve growth factor (NGF)-mediated increases in amyloid precursor protein (APP) levels in PC12 cells. To elucidate potential mechanisms, the effects of NGF and NO synthase (NOS) inhibitors on APP mRNA levels and protein stability were evaluated. Surprisingly, treatment of PC12 cells with NGF resulted in decreased levels of APP695 and APP751/770 mRNA. Therefore, the effect of NGF on APP protein stability was examined using the translation inhibitor, cycloheximide. Under these conditions, NGF did not alter the rate of APP degradation, suggesting that NGF may be enhancing the translation rate of APP. Since NOS inhibitors attenuate the NGF-mediated increase in APP levels, their effect on APP mRNA levels and protein stability was also assessed. S-methylisothiourea (S-MIU), selective for inducible NOS, decreased both APP695 and APP751/770 mRNA levels while the non-selective NOS inhibitor, N(ω)-nitro-L-arginine methylester (L-NAME) had no effect. In both control and NGF-treated PC12 cells, S-MIU increased the half-life of APP, with the greatest effect observed with the APP695 isoform. Based on these data we propose that in PC12 cells, NGF increases APP levels through enhanced translation rate and that NO, which modulates the NGF-induced increase in APP protein, also regulates APP mRNA levels and could play a role in APP processing.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"31-9"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/31/67/TOBIOCJ-6-31.PMC3339428.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30587448","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of α-Particle Radiation on MicroRNA Responses in Human Cell-Lines.","authors":"Vinita Chauhan,&nbsp;Matthew Howland,&nbsp;Ruth Wilkins","doi":"10.2174/1874091X01206010016","DOIUrl":"https://doi.org/10.2174/1874091X01206010016","url":null,"abstract":"<p><p>A variety of alpha (α)-particle emitters are found ubiquitously in the environment, in commercial/therapeutic prod-ucts and are a potential threat in the form of a radiological dispersal device. Our understanding of the biological mechanisms and long-term health effects resulting from α-particle exposure is limited. Exposure to radiation induces modulations of gene networks, possibly through microRNAs (miRNAs), which could be targets for studying biological effects. In this study, changes in miRNA expression patterns after 0.5 Gy, 1.0 Gy and 1.5 Gy of α-particle radiation at a low dose-rate of exposure in three human cell-lines (A549, THP-1 and HFL) were investigated. The screening of 1,145 miRNAs across three human cell-lines resulted in unique, cell-specific responses with no overlap in miRNA expression observed in the three cell-lines. Prediction analysis suggests these α-particle induced miRNA mapped to target genes related to ribosomal assembly, lung carcinoma development, cell communication and keratin sulfate biosynthesis. Taken together, these results suggest that exposure to α-particle radiation results in cell-type specific responses in gene network regulatory processes.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"16-22"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2174/1874091X01206010016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30557036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cardiovascular risk factors in portuguese obese children and adolescents: impact of small reductions in body mass index imposed by lifestyle modifications.","authors":"Henrique Nascimento,&nbsp;Elísio Costa,&nbsp;Petronila Rocha-Pereira,&nbsp;Carla Rego,&nbsp;Helena Ferreira Mansilha,&nbsp;Alexandre Quintanilha,&nbsp;Alice Santos-Silva,&nbsp;Luís Belo","doi":"10.2174/1874091X01206010043","DOIUrl":"https://doi.org/10.2174/1874091X01206010043","url":null,"abstract":"<p><strong>Objectives: </strong>Evaluate cardiovascular risk factors in Portuguese obese children and adolescents and the long-term effects of lifestyle modifications on such risk factors.</p><p><strong>Design: </strong>Transversal cohort study and longitudinal study.</p><p><strong>Setting: </strong>University Hospital S. João and Children's Hospital Maria Pia, Porto.</p><p><strong>Patients/participants: </strong>148 obese children and adolescents [81 females (54.7%); mean age of 11.0 years] and 33 controls (sex and age matched) participated in a cross-sectional study. Sixty obese patients agreed to participate in an one year longitudinal study after medical and nutritionist appointments to improve lifestyle modification; a substantial body mass index (BMI) reduction was defined by a decrease in BMI z-score (BMI z-sc) of 0.3 or more over the studied period.</p><p><strong>Main outcome measures: </strong>Lipid profile (triglycerides, cholesterol, HDLc, LDLc, lipoprotein (a), apolipoproteins A and B) and circulating levels of C-reactive protein (CRP), adiponectin, glucose, and insulin.</p><p><strong>Results: </strong>Compared with the lean children, obese patients demonstrated statistically significantly higher insulin resistance index [Homeostasis model assessment (HOMA)], and triglycerides, LDLc, apolipoprotein (apo) B, insulin and CRP concentrations, whereas their HDLc and apo A levels were significantly lower (cross-sectional study). In the longitudinal study (n=60), a substantial BMI reduction occurred in 17 (28.3%) obese patients which led to a significant reduction in triglycerides, cholesterol, LDLc, apo B, glucose and insulin levels and in HOMA. The ΔBMI values over the studied period correlated inversely and significantly with BMI (P<0.001) and HOMA (P=0.026) values observed at baseline. In multiple linear regression analysis, BMI at baseline remained associated to changes in BMI over the studied period (standardised Beta: -0.271, P=0.05).</p><p><strong>Conclusion: </strong>Our data demonstrates that small reductions in BMI-zc, imposed by lifestyle modifications in obese children and adolescents, improve the cardiovascular risk profile of such patients. Furthermore, patients with higher BMI and/or insulin resistance seem to experience a greater relative reduction in their BMI after lifestyle improvements.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"43-50"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5e/40/TOBIOCJ-6-43.PMC3358715.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30645250","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity.","authors":"Casey Zelus,&nbsp;Ayano Fox,&nbsp;Anastasia Calciano,&nbsp;Bianca S Faridian,&nbsp;Luiza A Nogaj,&nbsp;David A Moffet","doi":"10.2174/1874091X01206010066","DOIUrl":"https://doi.org/10.2174/1874091X01206010066","url":null,"abstract":"<p><p>The aggregation of the amyloidogenic polypeptide IAPP (Islet Amyloid Polypeptide, amylin) is believed to play a direct role in the death of pancreatic β-islet cells in type II diabetes. Preventing the initial aggregation event of IAPP is one strategy for slowing, and possibly preventing, the progression of this disease. Here, we investigate myricetin's potential as an inhibitor of IAPP aggregation. We show that myricetin prevented thioflavin T binding in a concentration dependent manner. Atomic force microscopy revealed that myricetin prevented fiber formation under rigorous conditions conducive to forming IAPP aggregates. Using an IAPP-EGFP (Enhanced Green Fluorescent Protein) protein construct, we find that high concentrations of myricetin slowed the in vivo aggregation of IAPP-EGFP. Myricetin was also found to rescue living mammalian cells from the toxic effects of IAPP. These results indicate that myricetin is a strong inhibitor of IAPP amyloid aggregation and a potential lead molecule for the development of an amyloid inhibiting therapeutic.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"66-70"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1e/18/TOBIOCJ-6-66.PMC3394101.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30759471","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Endoplasmic Reticulum (ER) Stress Enhances Tip60 (A Histone Acetyltransferase) Binding to the Concanavalin A.","authors":"Eun Jeoung Lee,&nbsp;Sung Hwa Shin,&nbsp;Sunghee Hyun,&nbsp;Jaesun Chun,&nbsp;Sang Sun Kang","doi":"10.2174/1874091X01206010001","DOIUrl":"https://doi.org/10.2174/1874091X01206010001","url":null,"abstract":"<p><p>Herein, we report that the concanavalin A binding of Tip60 (a target of the human immunodeficiency virus type 1-encoded transactivator Tat interacting protein 60 KD; a histone acetyltransferase; HAT) is enhanced as the result of endoplasmic reticulum (ER) stress. The cell expression of Tip60 combined with site-directed mutagenesis analysis was used to identify the glutamine 324 residue as the lecithin binding (Concanavalin A; Con A) site. The Tip60 N324A mutant strain, which seems to be the Con A binding-deficient, was attenuated the protein-protein interactions with FE65 and its protein stability, but its ability of G0-G1 cell cycle arrest was not interrupted. Interestingly, both HAT activity and the nuclear localization of Tip60 N324A mutant were enhanced than those of Tip60 WT. Thus, our results indicate that the Con A binding deficient of Tip60 seems to be one of the most pivotal posttranslational modifications (such as N-glycosylation) for its functional regulation signal, which is generated in response to ER stress.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2174/1874091X01206010001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30527607","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tianma modulates blood vessel tonicity.","authors":"Lin Feng,&nbsp;Arulmani Manavalan,&nbsp;Manisha Mishra,&nbsp;Siu Kwan Sze,&nbsp;Jiang-Miao Hu,&nbsp;Klaus Heese","doi":"10.2174/1874091X01206010056","DOIUrl":"https://doi.org/10.2174/1874091X01206010056","url":null,"abstract":"<p><p>Tianma is a traditional Chinese medicine (TCM) often used for the treatment of hypertension and heart diseases. To elucidate the function of tianma at the molecular level, we investigated the effect of tianma on vascular functions and aortic protein metabolism. We found that long-term treatment with tianma (~2.5g/kg/day for three months) in one-year-old rats could enhance acetylcholine (ACh)-induced vasorelaxation in endothelium-intact thoracic aortic rings against both KCl (80 mM)- and phenylephrine (PE)-induced contraction. By using the iTRAQ (isobaric tag for relative and absolute quantification) technique, we confirmed from the functional data at the proteome level that tianma treatment down-regulated the expressions of contractile proteins (e.g. Acta2) and other related structural proteins (e.g. desmin), and up-regulated the expressions of extracellular matrix (ECM) glycoproteins (e.g. Fbln5) and anti-thrombotic proteins (e.g. Anxa2) in aortic tissue. By inductive reasoning, tianma could perform its vasodilatory effect not only by inhibiting vascular smooth muscle contraction, but also by enhancing blood vessel elasticity and stabilizing the arterial structure. Thus, tianma might become a novel therapeutic herbal medicine for cardiovascular diseases by regulating the aortic proteome metabolism.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"6 ","pages":"56-65"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2174/1874091X01206010056","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30755931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In the Huh7 Hepatoma Cells Diclofenac and Indomethacin Activate Differently the Unfolded Protein Response and Induce ER Stress Apoptosis.","authors":"Silvia Franceschelli,&nbsp;Ornella Moltedo,&nbsp;Giuseppina Amodio,&nbsp;Gianfranco Tajana,&nbsp;Paolo Remondelli","doi":"10.2174/1874091X01105010045","DOIUrl":"https://doi.org/10.2174/1874091X01105010045","url":null,"abstract":"<p><p>Non-steroidal anti-inflammatory drugs (NSAIDs) are cyclooxygenases (COXs) inhibitors frequently used in the treatment of acute and chronic inflammation. Side effects of NSAIDs are often due to their ability to induce apoptosis. Located at the Endoplasmic Reticulum membranes a tripartite signalling pathway, collectively known as the Unfolded Protein Response (UPR), decides survival or death of cells exposed to cytotoxic agents. To shed light on the molecular events responsible for the cytotoxicity of NSAIDs, we analysed the ability of diclofenac and indomethacin to activate the UPR in the human hepatoma cell line Huh7. We report that both NSAIDs can induce differently the single arms of the UPR. We show that indomethacin turns on the PERK and, only in part, the ATF6 and IRE1 pathways. Instead, diclofenac reduces the expression of ATF6 and does not stimulate the IRE1 endonuclease, which drives the expression of the prosurvival factor XBP1. Diclofenac, as well as indomethacin, is able to activate efficiently only the PERK pathway of the UPR, which induces the expression of the proapoptotic GADD153/CHOP protein. Our results highlight the importance of the UPR in evaluating the potential of drugs to induce apoptosis.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"5 ","pages":"45-51"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b4/ac/TOBIOCJ-5-45.PMC3182409.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30038089","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Oxidative State of LDL is the Major Determinant of Anti/Prooxidant Effect of Coffee on Cu Catalysed Peroxidation.","authors":"Ciriaco Carru,&nbsp;Valeria Pasciu,&nbsp;Salvatore Sotgia,&nbsp;Angelo Zinellu,&nbsp;Maria Cristina Nicoli,&nbsp;Luca Deiana,&nbsp;Bruna Tadolini,&nbsp;Bastiano Sanna,&nbsp;Bruno Masala,&nbsp;Gianfranco Pintus","doi":"10.2174/1874091X01105010001","DOIUrl":"https://doi.org/10.2174/1874091X01105010001","url":null,"abstract":"<p><p>Antioxidants exert contrasting effect on low density lipoprotein (LDL) oxidation catalysed by metals, acting as pro-oxidants under select in vitro conditions. Through our study on the effect of coffee on LDL oxidation, we identified the parameters governing this phenomenon, contributing to the comprehension of its mechanism and discovering significant implications for correct alimentary recommendations. By measuring conjugated diene formation, we have analysed the quantitative and qualitative effects exerted by an extract of roasted coffee on LDL oxidation triggered by copper sulphate. When the relative effects of different coffee concentrations were plotted against the lag time (LT) of control LDL (C-LDL), the apparently random experimental data arranged in sensible patterns: by increasing the LT the antioxidant activity of coffee decreased progressively to become prooxidant. The critical LT, at which coffee switches from antioxidant to prooxidant, increased by increasing coffee concentration. Also the contrasting results obtained following a delayed addition of coffee to the assay, arranged in a simple pattern when referred to the LT of C-LDL: the prooxidant effect decreased to become antioxidant as the LT of C-LDL increased. The dependence of coffee effect on the LT of C-LDL was influenced by LDL but not by metal catalyst concentration. These novel findings point to the oxidative state of LDL as a major parameter controlling the anti/prooxidant effect of coffee and suggest the LT of C-LDL as a potent analytical tool to express experimental data when studying the action exerted by a compound on LDL oxidation.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"5 ","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/d1/34/TOBIOCJ-5-1.PMC3104561.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29907698","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Parkin, A Top Level Manager in the Cell's Sanitation Department.","authors":"Carolyn A Rankin,&nbsp;Ambrish Roy,&nbsp;Yang Zhang,&nbsp;Mark Richter","doi":"10.2174/1874091X01105010009","DOIUrl":"https://doi.org/10.2174/1874091X01105010009","url":null,"abstract":"<p><p>Parkin belongs to a class of multiple RING domain proteins designated as RBR (RING, in between RING, RING) proteins. In this review we examine what is known regarding the structure/function relationship of the Parkin protein. Parkin contains three RING domains plus a ubiquitin-like domain and an in-between-RING (IBR) domain. RING domains are rich in cysteine amino acids that act as ligands to bind zinc ions. RING domains may interact with DNA or with other proteins and perform a wide range of functions. Some function as E3 ubiquitin ligases, participating in attachment of ubiquitin chains to signal proteasome degradation; however, ubiquitin may be attached for purposes other than proteasome degradation. It was determined that the C-terminal most RING, RING2, is essential for Parkin to function as an E3 ubiquitin ligase and a number of substrates have been identified. However, Parkin also participates in a number of other fiunctions, such as DNA repair, microtubule stabilization, and formation of aggresomes. Some functions, such as participation in a multi-protein complex implicated in NMDA activity at the post synaptic density, do not require ubiquitination of substrate molecules. Recent observations of RING proteins suggest their function may be regulated by zinc ion binding. We have modeled the three RING domains of Parkin and have identified a new set of RING2 ligands. This set allows for binding of two rather than just one zinc ion, opening the possibility that the number of zinc ions bound acts as a molecular switch to modulate Parkin function.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"5 ","pages":"9-26"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/d2/89/TOBIOCJ-5-9.PMC3104551.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29907700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production of free radicals and oxygen consumption by primary equine endothelial cells during anoxia-reoxygenation.","authors":"Geoffroy de Rebière de Pouyade,&nbsp;Alexandra Salciccia,&nbsp;Justine Ceusters,&nbsp;Ginette Deby-Dupont,&nbsp;Didier Serteyn,&nbsp;Ange Mouithys-Mickalad","doi":"10.2174/1874091X01105010052","DOIUrl":"https://doi.org/10.2174/1874091X01105010052","url":null,"abstract":"<p><p>The endothelium plays an active role in ischemia/reperfusion injuries. Herein, we report the effect of a single or successive cycles of anoxia/reoxygenation (A/R) on the mitochondrial respiratory function of equine endothelial cells (cultured from carotids) monitored by high resolution oxymetry, and on their production of reactive oxygen species (ROS). ROS were measured by electron paramagnetic resonance (ESR) using POBN and DMPO spin traps, and by gas chromatography (GC) of ethylene released by ROS-induced α-keto-γ-(methylthio)butyric acid (KMB) oxidation. The oxygen consumption significantly decreased with the number of A/R cycles, and POBN-ESR spectra were specific of adducts formed in the cells from superoxide anion. After a one-hour A/R cycle, high intensity DMPO-ESR spectra were observed and assigned to superoxide anion trapping; the GC results confirmed an important production of ROS compared to normoxic cells. These results show that A/R induces mitochondrial alterations in endothelial cells, and strongly stimulates their oxidative activity as demonstrated by ESR and GC methods.</p>","PeriodicalId":515405,"journal":{"name":"The Open Biochemistry Journal","volume":"5 ","pages":"52-9"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1e/de/TOBIOCJ-5-52.PMC3242399.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30355621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}