Literature DB >> 7981969

Microbial sialidases: does bigger always mean better?

E R Vimr1.   

Abstract

Sialidases are a superfamily of N-acylneuraminate-releasing (sialic-acid-releasing) exoglycosidases found mainly in higher eukaryotes and in some, mostly pathogenic, viruses, bacteria and protozoans. The functions of sialidases are poorly understood and, until recently, their biochemical and evolutionary relationships were unclear. A comparative approach has demonstrated the remarkable similarities and differences between nonviral sialidases, and is providing clues about their functions.

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Year:  1994        PMID: 7981969     DOI: 10.1016/0966-842x(94)90003-5

Source DB:  PubMed          Journal:  Trends Microbiol        ISSN: 0966-842X            Impact factor:   17.079


  20 in total

Review 1.  Mucinases and sialidases: their role in the pathogenesis of sexually transmitted infections in the female genital tract.

Authors:  R Wiggins; S J Hicks; P W Soothill; M R Millar; A P Corfield
Journal:  Sex Transm Infect       Date:  2001-12       Impact factor: 3.519

2.  Cloning and characterization of sialidases with 2-6' and 2-3' sialyl lactose specificity from Pasteurella multocida.

Authors:  S Mizan; A Henk; A Stallings; M Maier; M D Lee
Journal:  J Bacteriol       Date:  2000-12       Impact factor: 3.490

3.  A surface-exposed neuraminidase affects complement resistance and virulence of the oral spirochaete Treponema denticola.

Authors:  Kurni Kurniyati; Weiyan Zhang; Kai Zhang; Chunhao Li
Journal:  Mol Microbiol       Date:  2013-08-01       Impact factor: 3.501

Review 4.  Sialoside-based pattern recognitions discriminating infections from tissue injuries.

Authors:  Yang Liu; Guo-Yun Chen; Pan Zheng
Journal:  Curr Opin Immunol       Date:  2011-01-03       Impact factor: 7.486

5.  High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries.

Authors:  Harshal A Chokhawala; Hai Yu; Xi Chen
Journal:  Chembiochem       Date:  2007-01-22       Impact factor: 3.164

6.  Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface.

Authors:  H Hu; T Shioda; C Moriya; X Xin; M K Hasan; K Miyake; T Shimada; Y Nagai
Journal:  J Virol       Date:  1996-11       Impact factor: 5.103

7.  Sialidase and sialoglycoproteases can modulate virulence in Porphyromonas gingivalis.

Authors:  Wilson Aruni; Elaine Vanterpool; Devon Osbourne; Francis Roy; Arun Muthiah; Yuetan Dou; Hansel M Fletcher
Journal:  Infect Immun       Date:  2011-04-18       Impact factor: 3.441

8.  Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain.

Authors:  J Martinez; S Steenbergen; E Vimr
Journal:  J Bacteriol       Date:  1995-10       Impact factor: 3.490

Review 9.  Diversity of microbial sialic acid metabolism.

Authors:  Eric R Vimr; Kathryn A Kalivoda; Eric L Deszo; Susan M Steenbergen
Journal:  Microbiol Mol Biol Rev       Date:  2004-03       Impact factor: 11.056

Review 10.  Biosynthesis of the polysialic acid capsule in Escherichia coli K1.

Authors:  E Vimr; S Steenbergen; M Cieslewicz
Journal:  J Ind Microbiol       Date:  1995-10
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