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Two highly conserved cysteine residues in HPV16 L2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes
Samuel K. Campos
, Michelle A. Ozbun
Immunobiology
BIO5, Institute of
Cancer Biology - GIDP
Molecular and Cellular Biology
Research output
:
Contribution to journal
›
Article
›
peer-review
53
Scopus citations
Overview
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Dive into the research topics of 'Two highly conserved cysteine residues in HPV16 L2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes'. Together they form a unique fingerprint.
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Immunology and Microbiology
Virion
100%
Disulfide Bond
100%
Keratinocyte
100%
Human Papillomavirus Type 16
100%
Epitope
50%
Wild Type
33%
B Cell
16%
Lysosome
16%
Amino Terminal Sequence
16%
Endocytosis
16%
Capsid
16%
Wart Virus
16%
Tandem Mass Spectrometry
16%
Pharmacology, Toxicology and Pharmaceutical Science
Infection
100%
Cysteine
100%
Disulfide Bond
100%
Human Papillomavirus Type 16
100%
Epitope
42%
Disulfide
28%
Thiol
14%
Receptor
14%
Capsid Protein
14%
Papillomavirus Infection
14%
Furin
14%
Keyphrases
Thiol Labeling
16%
L2 Protein
16%
HPV16 Infection
16%