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	Provedor de dados BJMBR (1) Genet. Mol. Biol. (1) Autor Brennan,P.J. (1) Li,Hongyan (1) Liu,Zhenhui (1) Ma,Lifang (1) Mahapatra,S. (1) Marques,M.A.M. (1) Pessolani,M.C.V. (1) Santos,S. (1) Sarno,E.N. (1) Spencer,J.S. (1) Xia,Jianjun (1) Zhang,Shicui (1) Mais... Palavra-chave Ribosomal protein (2) Adhesion (1) Amphioxus (1) Branchiostoma (1) Copy number (1) Histone (1) Laminin (1) Mycobacterium leprae (1) S27 (1) Schwann cell (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2005 (1) 2001 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Characterization and copy number of the S27 ribosomal protein gene from amphioxus Branchiostoma belcheri tsingtauense Genet. Mol. Biol. Ma,Lifang; Zhang,Shicui; Liu,Zhenhui; Li,Hongyan; Xia,Jianjun. A cDNA clone encoding ribosomal protein S27 (AmphiS27) was identified in the gut cDNA library of amphioxus Branchiostoma belcheri tsingtauense. This cDNA consists of 607 bp and contains a 255 bp open reading frame (ORF) corresponding to a deduced protein of 84 amino acids with a calculated molecular mass of 9,488 Da and an isoelectric point (pI) of 9.500. Alignment of the deduced AmphiS27 amino acid sequence with 12 known S27 protein sequences indicates that AmphiS27 shares 94-99% homology with its vertebrate homologue, 84-94% with invertebrate homologues and 69-72% with homologues from other eukaryotes, suggesting that AmphiS27 is more closely related to the vertebrate S27 protein than to its invertebrate counterpart. Southern blot analysis showed a... Tipo: Info:eu-repo/semantics/article Palavras-chave: Amphioxus; Branchiostoma; Ribosomal protein; S27; Copy number. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572005000500029 Further biochemical characterization of Mycobacterium leprae laminin-binding proteins BJMBR Marques,M.A.M.; Mahapatra,S.; Sarno,E.N.; Santos,S.; Spencer,J.S.; Brennan,P.J.; Pessolani,M.C.V.. It has been demonstrated that the alpha2 chain of laminin-2 present on the surface of Schwann cells is involved in the process of attachment of Mycobacterium leprae to these cells. Searching for M. leprae laminin-binding molecules, in a previous study we isolated and characterized the cationic proteins histone-like protein (Hlp) and ribosomal proteins S4 and S5 as potential adhesins involved in M. leprae-Schwann cell interaction. Hlp was shown to bind alpha2-laminins and to greatly enhance the attachment of mycobacteria to ST88-14 Schwann cells. In the present study, we investigated the laminin-binding capacity of the ribosomal proteins S4 and S5. The genes coding for these proteins were PCR amplified and their recombinant products were shown to bind... Tipo: Info:eu-repo/semantics/article Palavras-chave: Mycobacterium leprae; Laminin; Adhesion; Schwann cell; Ribosomal protein; Histone. Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000400004 Registros recuperados: 2 Primeira ... 1 ... Última

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