Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite surface protein 1 expressed in mammalian cells-Reference-Cited by-同舟云学术

Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite surface protein 1 expressed in mammalian cells

Published:1999-12-01 Issue:12 Volume:9 Page:1347-1356
ISSN:0959-6658
Container-title:Glycobiology
language:en
Short-container-title:Glycobiology

Author:

Yang S.,Nikodem D.,Davidson E. A.,Gowda D. C.

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

Link

http://academic.oup.com/glycob/article-pdf/9/12/1347/1687716/9-12-1347.pdf

Reference34 articles.

1. Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1

2. A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies.

3. A recombinant baculovirus 42-kilodalton C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 protects Aotus monkeys against malaria

4. A soluble receptor for interleukin Iβ encoded by Vaccinia Virus: A novel mechanism of virus modulation of the host response to infection

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1. Overlooked post-translational modifications of proteins in Plasmodium falciparum: N- and O-glycosylation - A Review;Memórias do Instituto Oswaldo Cruz;2010-12

2. Proteomic Profiling ofPlasmodium falciparumthrough Improved, Semiquantitative Two-Dimensional Gel Electrophoresis;Journal of Proteome Research;2010-05-07

3. Malaria;Handbook of Glycomics;2010

4. Effect of GPI anchor moiety on the immunogenicity of DNA plasmids encoding the 19-kDa C-terminal portion of Plasmodium falciparum MSP-1;Parasite Immunology;2008-06

5. Viral vectors for malaria vaccine development;Vaccine;2007-03