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| Weber, Alexandra At; Hugall, Andrew F; O’hara, Timothy D. |
| The deep ocean is the largest biome on Earth and yet it is among the least studied environments of our planet. Life at great depths requires several specific adaptations; however, their molecular mechanisms remain understudied. We examined patterns of positive selection in 416 genes from four brittle star (Ophiuroidea) families displaying replicated events of deep-sea colonization (288 individuals from 216 species). We found consistent signatures of molecular convergence in functions related to protein biogenesis, including protein folding and translation. Five genes were recurrently positively selected, including chaperonin-containing TCP-1 subunit α (CCTα), which is essential for protein folding. Molecular convergence was detected at the functional and... |
| Tipo: Text |
Palavras-chave: Echinodermata; TC P-1; Protein folding; Positive selection; Protein stability; Pressure adaptation. |
| Ano: 2020 |
URL: https://archimer.ifremer.fr/doc/00659/77136/78452.pdf |
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| Mokry,David Z.; Abrahão,Josielle; Ramos,Carlos H.I.. |
| The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Amyloid; Disaggregase; Shock protein; Molecular chaperones; Prion; Protein folding. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 |
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| Clement,Herlinda; Flores,Vianey; la Rosa,Guillermo De; Zamudio,Fernando; Alagon,Alejandro; Corzo,Gerardo. |
| Abstract Background The cysteine-rich neurotoxins from elapid venoms are primarily responsible for human and animal envenomation; however, their low concentration in the venom may hamper the production of efficient elapid antivenoms. Therefore, the aim of the present study was to produce fully active elapid neurotoxic immunogens for elapid antivenom production. Method Cysteine-rich neurotoxins showed recombinant expression in two strains of E. coli, and were purified using affinity chromatography and reverse-phase HPLC (rpHPLC). Results The cDNA of the four disulfide-bridged peptide neurotoxin Mlat1 was cloned into a modified expression vector, pQE30, which was transfected into two different E. coli strains. The recombinant toxin (HisrMlat1) was... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Micrurus laticorallis; Protein folding; Recombinant; Elapid; Toxin; Protein recognition. |
| Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100318 |
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| Mignaco,J.A.; Lima,L.M.T.R.; Rosenthal,A.; Foguel,D.; Silva,J.L.. |
| The 3rd International Conference on High Pressure Bioscience and Biotechnology was held in the city of Rio de Janeiro from September 27 to September 30, 2004. The meeting, promoted by the International Association of High Pressure Bioscience and Biotechnology (IAHPBB), congregated top scientists and researchers from all over the world. In common, they shared the use of hydrostatic pressure for research, technical development, or industrial applications. The meeting consisted of invited lectures, contributed papers and a well-attended poster session. Very exciting discussions were held inside and outside the sessions, and the goals of discussing state-of-the-art data and establishing working collaborations and co-operations were fully attained. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hydrostatic pressure; Phase diagram; Compressibility; Protein folding; Food technology; Piezotolerance. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800001 |
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| Yon,J.M.. |
| At the present time, protein folding is an extremely active field of research including aspects of biology, chemistry, biochemistry, computer science and physics. The fundamental principles have practical applications in the exploitation of the advances in genome research, in the understanding of different pathologies and in the design of novel proteins with special functions. Although the detailed mechanisms of folding are not completely known, significant advances have been made in the understanding of this complex process through both experimental and theoretical approaches. In this review, the evolution of concepts from Anfinsen's postulate to the "new view" emphasizing the concept of the energy landscape of folding is presented. The main rules of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Protein folding; Energy landscape; Misfolding and disease. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000400001 |
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