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Insight from early coral-stromatoporoid intergrowth, Late Ordovician of China
Lee, M.,Elias, R.J.,Choh, S.J.,Lee, D.J. Elsevier 2016 Palaeogeography, palaeoclimatology, palaeoecology Vol.463 No.-
One of the earliest endosymbiotic associations with stromatoporoids occurs in the Late Ordovician Xiazhen Formation of southeastern China. Bajgolia, an auloporid tabulate coral characterized by dichotomous branching due to longitudinal fission, is represented by free-living as well as endobiontic forms in various lithofacies representing a wide range of environments. Only two of 11 stromatoporoid genera (Clathrodictyon and Ecclimadictyon) hosted Bajgolia, mainly in reef and related facies. Bajgolia-stromatoporoid associations occur occasionally in the lower part of the formation, but eventually become persistent in the upper part. Such associations were initiated by larval settlement of the coral on the growth surface of the stromatoporoid. Growth of Bajgolia usually kept pace with its host, but the coral's ability to change growth direction and grow faster prevented its envelopment and termination by the stromatoporoid, allowing the establishment and recurrence of an ongoing endosymbiotic relationship between the two organisms. Endobiontic Bajgolia was able to survive with its corallites protruding from the host; in some cases, the growth form of the stromatoporoid changed in response to the coral. The relationships between Bajgolia and stromatoporoids were probably commensal, but there is also evidence for mutualism and/or parasitism. Bajgolia-stromatoporoid associations represent an important stage in the development of complex ecological relationships and community structure, prior to the common and widespread syringoporid (''caunopore tubes'')-stromatoporoid associations in the Siluro-Devonian.
Rahman, F Abdul,Naidu, J,Ngiu, CS,Yaakob, Y,Mohamed, Z,Othman, H,Jarmin, R,Elias, MH,Hamid, N Abdul,Mokhtar, N Mohd,Ali, RA Raja Asian Pacific Journal of Cancer Prevention 2016 Asian Pacific journal of cancer prevention Vol.17 No.8
Background: Hepatocellular carcinoma (HCC) is a common cancer that is frequently diagnosed at an advanced stage. Transarterial chemoembolisation (TACE) is an effective palliative treatment for patients who are not eligible for curative treatment. The two main methods for performing TACE are conventional (c-TACE) or with drug eluting beads (DEB-TACE). We sought to compare survival rates and tumour response between patients undergoing c-TACE and DEB-TACE at our centre. Materials and Methods: A retrospective cohort study of patients undergoing either treatment was carried out from January 2009 to December 2014. Tumour response to the procedures was evaluated according to the modified Response Evaluation Criteria in Solid Tumors (mRECIST). Kaplan-Meier analysis was used to assess and compare the overall survival in the two groups. Results: A total of 79 patients were analysed (34 had c-TACE, 45 had DEB-TACE) with a median follow-up of 11.8 months. A total of 20 patients in the c-TACE group (80%) and 12 patients in the DEB-TACE group (44%) died during the follow up period. The median survival durations in the c-TACE and DEB-TACE groups were $4.9{\pm}3.2$ months and $8.3{\pm}2.0$ months respectively (p=0.008). There was no statistically significant difference noted among the two groups with respect to mRECIST criteria. Conclusions: DEB-TACE demonstrated a significant improvement in overall survival rates for patients with unresectable HCC when compared to c-TACE. It is a safe and promising approach and should potentially be considered as a standard of care in the management of unresectable HCC.
Selenoprotein Gene Nomenclature
Gladyshev, Vadim N.,Arné,r, Elias S.,Berry, Marla J.,Brigelius-Flohé,é,, Regina,Bruford, Elspeth A.,Burk, Raymond F.,Carlson, Bradley A.,Castellano, Sergi,Chavatte, Laurent,Conrad, M American Society for Biochemistry and Molecular Bi 2016 The Journal of biological chemistry Vol.291 No.46
<P>The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4, and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine sulfoxide reductase B1), and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15-kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV), and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing, and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.</P>
Kistler, H. C.,Alabouvette, C.,Baayen, R. P.,Bentley, S.,Brayford, D.,Coddington, A.,Correll, J.,Daboussi, M.-J.,Elias, K.,Fernandez, D.,Gorden, T. R.,Katan, T.,Kim, H. G.,Leslie, J. F.,Martyn, R. D. 충남대학교 생물공학연구소 1999 생물공학연구지 Vol.7 No.-
Fusarium oxysporum Schlechtend.:Fr is a cosmopolitan fungal pathogen (4) responsible for wit and cortical rot diseases of more than 100 economically important plant hosts (3). Genetic diversity within F. oxysporum has been categorized extensively by vegetative compatibility grouping in laboratories around the world. Detailed studies indicate that isolates belonging to the same vegetative compatibility group (VCG) typically possess very similar or identical multilocus haplotypes and belong to the same clonal lineage(19). VCG. therefore, can be good predictors of genetic similarity, clonal lineage. or both. In this communication, we propose a standardization of the system currently used for categorizing genetic diversity within this taxon. Our primary objective is to make the system more understandable and useful by reducing ambiguity and increasing the rigor with which the current system is applied. A secondary goal of this undertaking is to promote international communication and cooperation in this endeavor.
Kim, Han Ie,Saldova, Radka,Park, Jun Hyoung,Lee, Young Hun,Harvey, David J.,Wormald, Mark R.,Wynne, Kieran,Elia, Giuliano,Kim, Hwa-Jung,Rudd, Pauline M.,Lee, Seung-Taek American Chemical Society 2013 JOURNAL OF PROTEOME RESEARCH Vol.12 No.8
<P>Tissue inhibitor of metalloproteinases-1 (TIMP-1) inhibits matrix metalloproteinases (MMPs) by binding at a 1:1 stoichiometry. Here we have shown the involvement of <I>N</I>-glycosylation in the MMP inhibitory ability of TIMP-1. TIMP-1, purified from HEK 293 cells overexpressing TIMP-1 (293 TIMP-1), showed less binding and inhibitory abilities to MMPs than TIMP-1 purified from fibroblasts or SF9 insect cells infected with TIMP-1 baculovirus. Following deglycosylation of TIMP-1, all forms of TIMP-1 showed similar levels of MMP binding and inhibition, suggesting that glycosylation is involved in the regulation of these TIMP-1 activities. Analysis of the <I>N</I>-glycan structures showed that SF9 TIMP-1 has the simplest <I>N</I>-glycan structures, followed by fibroblast TIMP-1 and 293 TIMP-1, in order of increasing complexity in their <I>N</I>-glycan structures. Further analyses showed that cleavage of outer arm fucose residues from the <I>N</I>-glycans of 293 TIMP-1 or knockdown of both FUT4 and FUT7 (which encode for fucosyltransferases that add outer arm fucose residues to <I>N</I>-glycans) enhanced the MMP-binding and catalytic abilities of 293 TIMP-1, bringing them up to the levels of the other TIMP-1. These results demonstrate that the ability of TIMP-1 to inhibit MMPs is at least in part regulated by outer arm fucosylation of its <I>N</I>-glycans.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2013/jprobs.2013.12.issue-8/pr400276r/production/images/medium/pr-2013-00276r_0011.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr400276r'>ACS Electronic Supporting Info</A></P>