Journal article

Antibodies expose multiple weaknesses in the glycan shield of HIV.

Abstract:: A shield of glycans coat the viral envelope proteins of the human immunodeficiency virus (HIV). Broadly neutralising antibodies can recognise this shield despite structural variation in these ‘self’ carbohydrate structures.

Publication status:: Published

Peer review status:: Peer reviewed

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APA Style

Crispin, M., & Bowden, T. (2013). Antibodies expose multiple weaknesses in the glycan shield of HIV. Nature Structural and Molecular Biology, 20(7), 771–772.

MLA Style

Crispin, M., and T. Bowden. “Antibodies Expose Multiple Weaknesses in the Glycan Shield of HIV.” Nature Structural and Molecular Biology, vol. 20, no. 7, Nature Publishing Group, 2013, pp. 771–72.

Chicago Style

Crispin, M, and T Bowden. 2013. “Antibodies Expose Multiple Weaknesses in the Glycan Shield of HIV.” Nature Structural and Molecular Biology 20 (7): 771–72.
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Publisher copy:: 10.1038/nsmb.2627

Authors

+ Crispin, M More by this author

Institution:: University of Oxford
Division:: MSD
Department:: Biochemistry
Role:: Author

+ Bowden, T More by this author

Institution:: University of Oxford
Division:: MSD
Department:: NDM
Sub department:: Structural Biology
Role:: Author

+ Wellcome Trust More from this funder

+ International AIDS Vaccine Initiative Neutralizing Antibody Center More from this funder

+ Center for HIV/AIDS Vaccine Immunology and Immunogen Design. More from this funder

Publisher:: Nature Publishing Group
Journal:: Nature Structural and Molecular Biology More from this journal
Volume:: 20
Issue:: 7
Pages:: 771-772
Publication date:: 2013-07-01
DOI:: 10.1038/nsmb.2627
EISSN:: 1545-9985
ISSN:: 1545-9993

Language:: English
Pubs id:: pubs:410971
UUID:: uuid:ae108b51-defd-4bc6-b641-ce13eb9fd974
Local pid:: pubs:410971
Source identifiers:: 410971
Deposit date:: 2013-11-17

Terms of use

Copyright holder:: Crispin and Bowden
Copyright date:: 2013
Notes:: Copyright © 2013 Crispin and Bowden

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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