Your browser doesn't support javascript.
loading
The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori.
Pang, Siew Siew; Nguyen, Stanley Thai Son; Perry, Andrew J; Day, Christopher J; Panjikar, Santosh; Tiralongo, Joe; Whisstock, James C; Kwok, Terry.
Afiliação
  • Pang SS; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia.
  • Nguyen STS; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia; Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia.
  • Perry AJ; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia.
  • Day CJ; Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
  • Panjikar S; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia; Australian Synchrotron, 800 Blackburn Road, Clayton, Melbourne, Victoria 3168, Australia.
  • Tiralongo J; Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
  • Whisstock JC; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia; Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia. Electronic
  • Kwok T; Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia; Department of Microbiology, Monash University, Clayton Campus, Melbourne, Victoria 3800 Australia. Electronic address: terry.kwok@monash.edu.
J Biol Chem ; 289(10): 6332-6340, 2014 Mar 07.
Article em En | MEDLINE | ID: mdl-24375407
Assuntos
Palavras-chave
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Antígenos CD15 / Helicobacter pylori / Adesinas Bacterianas / Ácido N-Acetilneuramínico Idioma: En Ano de publicação: 2014 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Antígenos CD15 / Helicobacter pylori / Adesinas Bacterianas / Ácido N-Acetilneuramínico Idioma: En Ano de publicação: 2014 Tipo de documento: Article