M
Mario J. Borgnia
Researcher at National Institutes of Health
Publications - 113
Citations - 9140
Mario J. Borgnia is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Biology & Medicine. The author has an hindex of 34, co-authored 91 publications receiving 7977 citations. Previous affiliations of Mario J. Borgnia include Research Triangle Park & Durham University.
Papers
More filters
Journal ArticleDOI
A collaborative framework for 3D alignment and classification of heterogeneous subvolumes in cryo-electron tomography
Oleg Kuybeda,Gabriel A. Frank,Alberto Bartesaghi,Mario J. Borgnia,Sriram Subramaniam,Guillermo Sapiro +5 more
TL;DR: The genetic identity of each virus particle present in the mixture can be assigned based solely on the structural information derived from single envelope glycoproteins displayed on the virus surface by the nuclear norm-based, collaborative alignment method presented here.
Journal ArticleDOI
Cellular and molecular biology of the aquaporin water channels.
TL;DR: The high water permeability characteristic of mammalian red cell membranes is now known to be caused by the protein AQP1, a tetramer with each subunit containing an aqueous pore likened to an hourglass formed by obversely arranged tandem repeats.
Journal ArticleDOI
Molecular architecture of native HIV-1 gp120 trimers.
TL;DR: In this article, the structure and conformational changes of trimeric HIV-1 gp120 have been investigated in unliganded and CD4-bound states, and it was shown that CD4 binding results in a major reorganization of the Env trimer, causing an outward rotation and displacement of each gp120 monomer.
Journal ArticleDOI
The Aquaporins, Blueprints for Cellular Plumbing Systems
TL;DR: The abundance of the protein in rat renal proximal tubules and descending thin limbs sparked the idea that the 28-kDa polypeptide may be the long sought water channel, and its unique N-terminal amino acid sequence permitted cloning from an erythroid cDNA library.
Journal ArticleDOI
Controlling the SARS-CoV-2 spike glycoprotein conformation.
Rory Henderson,Rory Henderson,Robert J. Edwards,Robert J. Edwards,Katayoun Mansouri,Katarzyna Janowska,Victoria Stalls,Sophie M. C. Gobeil,Megan Kopp,Dapeng Li,Rob Parks,Allen L. Hsu,Mario J. Borgnia,Barton F. Haynes,Barton F. Haynes,Priyamvada Acharya,Priyamvada Acharya +16 more
TL;DR: Two soluble ectodomain constructs are developed for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs ‘down’ position or adopts ‘up’ state conformations more readily than the wild-type S- protein.