Glycobiology of Plasmodium falciparum

E. A. Davidson; D. C. Gowda

doi:10.1016/S0300-9084(01)01316-5

Glycobiology of Plasmodium falciparum

E. A. Davidson, D. C. Gowda

Research output: Contribution to journal › Review article › peer-review

33 Scopus citations

Abstract

The human malaria parasite, Plasmodium falciparum, has as its only glycoconjugate GPI anchors. These structures, present in essentially all parasite surface proteins, are associated with disease pathology. In contrast, the parasite depends for essential recognition events on saccharides associated with host cell glycoproteins and proteoglycans.

Original language	English (US)
Pages (from-to)	601-604
Number of pages	4
Journal	Biochimie
Volume	83
Issue number	7
DOIs	https://doi.org/10.1016/S0300-9084(01)01316-5
State	Published - 2001

All Science Journal Classification (ASJC) codes

Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/S0300-9084(01)01316-5

Cite this

@article{8c8ab90a44c04e37afb52fb7b9891b44,

title = "Glycobiology of Plasmodium falciparum",

abstract = "The human malaria parasite, Plasmodium falciparum, has as its only glycoconjugate GPI anchors. These structures, present in essentially all parasite surface proteins, are associated with disease pathology. In contrast, the parasite depends for essential recognition events on saccharides associated with host cell glycoproteins and proteoglycans.",

author = "Davidson, \{E. A.\} and Gowda, \{D. C.\}",

note = "Funding Information: Work reported from our laboratories was supported by grants from the National Institute of Allergy and Infectious Diseases, NIH (AI45086, AI-41139) and a grant from the Burroughs Wellcome Fund for New Initiatives in malaria Research.",

year = "2001",

doi = "10.1016/S0300-9084(01)01316-5",

language = "English (US)",

volume = "83",

pages = "601--604",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier B.V.",

number = "7",

}

TY - JOUR

T1 - Glycobiology of Plasmodium falciparum

AU - Davidson, E. A.

AU - Gowda, D. C.

N1 - Funding Information: Work reported from our laboratories was supported by grants from the National Institute of Allergy and Infectious Diseases, NIH (AI45086, AI-41139) and a grant from the Burroughs Wellcome Fund for New Initiatives in malaria Research.

PY - 2001

Y1 - 2001

N2 - The human malaria parasite, Plasmodium falciparum, has as its only glycoconjugate GPI anchors. These structures, present in essentially all parasite surface proteins, are associated with disease pathology. In contrast, the parasite depends for essential recognition events on saccharides associated with host cell glycoproteins and proteoglycans.

AB - The human malaria parasite, Plasmodium falciparum, has as its only glycoconjugate GPI anchors. These structures, present in essentially all parasite surface proteins, are associated with disease pathology. In contrast, the parasite depends for essential recognition events on saccharides associated with host cell glycoproteins and proteoglycans.

UR - https://www.scopus.com/pages/publications/0034845272

UR - https://www.scopus.com/inward/citedby.url?scp=0034845272&partnerID=8YFLogxK

U2 - 10.1016/S0300-9084(01)01316-5

DO - 10.1016/S0300-9084(01)01316-5

M3 - Review article

C2 - 11522388

AN - SCOPUS:0034845272

SN - 0300-9084

VL - 83

SP - 601

EP - 604

JO - Biochimie

JF - Biochimie

IS - 7

ER -

Glycobiology of Plasmodium falciparum

Abstract

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this