Skip to main navigation
Skip to search
Skip to main content
UTMB Health Research Expert Profiles Home
Help & FAQ
Home
Experts
Departments
Equipment
Projects/Grants
Publications
Activities
Press/Media
Honors
Impacts
Search by expertise, name or affiliation
Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
Thomas J. Smith
, Norman H. Olson
, R. Holland Cheng
, Elaine S. Chase
, Timothy S. Baker
Research output
:
Contribution to journal
›
Article
›
peer-review
118
Scopus citations
Overview
Fingerprint
Fingerprint
Dive into the research topics of 'Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility'. Together they form a unique fingerprint.
Sort by
Weight
Alphabetically
Keyphrases
Virus-neutralizing Antibody
100%
Conformational Change
100%
Capsid
100%
Antigen-antibody Complex
100%
Human Rhinovirus
100%
Virus Neutralization
100%
Antibody Flexibility
100%
Virus
50%
Immunoglobulin
50%
Monoclonal Antibody
50%
Electron Density
50%
Cryogenic Electron Microscopy
50%
Human Rhinovirus 14
50%
Fc Fragment
50%
Hinge Region
50%
Icosahedral
50%
Elbow
50%
Image Reconstruction
50%
Fab Fragment
50%
IgG Structure
50%
Degree of Mobility
50%
Constant Domain
50%
Immunology and Microbiology
Capsid
100%
Neutralization
100%
Human Rhinovirus
100%
Monoclonal Antibody
50%
Cryo-Electron Microscopy
50%
Human Rhinovirus B14
50%
Hinge Region
50%
Immunoglobulin F(ab) Fragment
50%
Myeloma Protein
50%
Immunoglobulin Fc Fragment
50%
Elbow
50%
Virus
50%