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Jianchao Zhang, Andrew Kennedy, Daniel Macedo de Melo Jorge, Lijuan Xing, Whitney Reid, Sarah Bui, Joseph Joppich, Molly Rose, Sevval Ercan, Qiyi Tang, David Ginsburg, Andrew W. Tai, Yanzhuang Wang
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Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization
10.1038/s41586-021-03777-9 · 2021
SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
10.1016/j.cell.2020.02.052 · 2020
Cell entry mechanisms of SARS-CoV-2
10.1073/pnas.2003138117 · 2020
Measuring immunity to SARS-CoV-2 infection: comparing assays and animal models
10.1038/s41577-020-00471-1 · 2020
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
10.1038/s41586-020-2286-9 · 2020
N- and O-Glycosylation of the SARS-CoV-2 Spike Protein
10.1021/acs.analchem.0c03173 · 2021
O-glycosylation pattern of the SARS-CoV-2 spike protein reveals an “O-Follow-N” rule
10.1038/s41422-021-00545-2 · 2021
Integrative Imaging Reveals SARS-CoV-2-Induced Reshaping of Subcellular Morphologies
10.1016/j.chom.2020.11.003 · 2020
A Coronavirus E Protein Is Present in Two Distinct Pools with Different Effects on Assembly and the Secretory Pathway
10.1128/jvi.01237-15 · 2015
The Infectious Bronchitis Coronavirus Envelope Protein Alters Golgi pH To Protect the Spike Protein and Promote the Release of Infectious Virus
10.1128/jvi.00015-19 · 2019
The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles
10.1128/jvi.01052-08 · 2008
β-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic Secretory Pathway
10.1016/j.cell.2020.10.039 · 2020
ORF3a of SARS-CoV-2 promotes lysosomal exocytosis-mediated viral egress
10.1016/j.devcel.2021.10.006 · 2021
ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation
10.1016/j.devcel.2020.12.010 · 2021
An Asymptomatic SARS-CoV-2-Infected Infant With Persistent Fecal Viral RNA Shedding in a Family Cluster: A Rare Case Report
10.3389/fmed.2020.562875 · 2020
The D614G mutation redirects SARS-CoV-2 spike to lysosomes and suppresses deleterious traits of the furin cleavage site insertion mutation
2022
SARS-CoV-2 nucleocapsid protein adheres to replication organelles before viral assembly at the Golgi/ERGIC and lysosome-mediated egress
10.1126/sciadv.abl4895 · 2022
SARS-CoV-2 virulence factor ORF3a blocks lysosome function by modulating TBC1D5-dependent Rab7 GTPase cycle
10.1038/s41467-024-46417-2 · 2024
Secretory Vesicles Are the Principal Means of SARS-CoV-2 Egress
10.3390/cells10082047 · 2021
Potential Antiviral Strategy Exploiting Dependence of SARS-CoV-2 Replication on Lysosome-Based Pathway
10.3390/ijms23116188 · 2022
SARS-CoV-2 and the host cell: a tale of interactions
2022
Coronavirus biology and replication: implications for SARS-CoV-2
10.1038/s41579-020-00468-6 · 2021
Membrane remodeling and trafficking piloted by SARS-CoV-2
10.1016/j.tcb.2023.12.006 · 2024
Betacoronavirus Assembly: Clues and Perspectives for Elucidating SARS-CoV-2 Particle Formation and Egress
10.1128/mbio.02371-21 · 2021
The Endolysosomal System: The Acid Test for SARS-CoV-2
10.3390/ijms23094576 · 2022
Friend or Foe? Implication of the autophagy-lysosome pathway in SARS-CoV-2 infection and COVID-19
10.7150/ijbs.72544 · 2022
Bidirectional interplay between SARS-CoV-2 and autophagy
2023
More than one door - Budding of enveloped viruses through cellular membranes
10.1016/j.febslet.2007.03.060 · 2007
Identification of ACE2 modifiers by CRISPR screening
2021
The SARS-CoV-2 Cytopathic Effect Is Blocked by Lysosome Alkalizing Small Molecules
10.1021/acsinfecdis.0c00349 · 2021
Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay
10.1101/cshperspect.a034090 · 2020
Ubiquitination independent of E1 and E2 enzymes by bacterial effectors
10.1038/nature17657 · 2016
Camostat mesylate inhibits SARS-CoV-2 activation by TMPRSS2-related proteases and its metabolite GBPA exerts antiviral activity
10.1016/j.ebiom.2021.103255 · 2021
Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig
10.1038/s41467-020-16048-4 · 2020
Visualization of Early RNA Replication Kinetics of SARS-CoV-2 by Using Single Molecule RNA-FISH Combined with Immunofluorescence
10.3390/v16020262 · 2024
Brefeldin A inhibits degradation as well as production and secretion of collagen in human lung fibroblasts
10.1016/s0021-9258(18)53746-7 · 1993
Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65
10.1038/ncomms2669 · 2013
Ultrastructural modifications induced by SARS-CoV-2 in Vero cells: a kinetic analysis of viral factory formation, viral particle morphogenesis and virion release
10.1007/s00018-020-03745-y · 2021
GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
10.1083/jcb.200907132 · 2010
Cell cycle regulation of Golgi membrane dynamics
10.1016/j.tcb.2013.01.008 · 2013
Reconstitution of the cell cycle-regulated Golgi disassembly and reassembly in a cell-free system
10.1038/nprot.2010.38 · doi-reference
The small chemical vacuolin-1 alters the morphology of lysosomes without inhibiting Ca2+-regulated exocytosis
10.1038/sj.embor.7400495 · doi-reference
Drug repurposing screens reveal cell-type-specific entry pathways and FDA-approved drugs active against SARS-Cov-2
10.1016/j.celrep.2021.108959 · doi-reference
Chloroquine does not inhibit infection of human lung cells with SARS-CoV-2
10.1038/s41586-020-2575-3 · doi-reference
Comparative Transcriptome Analysis Reveals the Intensive Early Stage Responses of Host Cells to SARS-CoV-2 Infection
10.3389/fmicb.2020.593857 · doi-reference
Proteomics of SARS-CoV-2-infected host cells reveals therapy targets
10.1038/s41586-020-2332-7 · doi-reference
Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19
10.1016/j.cell.2020.04.026 · doi-reference
10.1101/2022.04.20.488883
10.1101/2022.04.20.488883 · doi-reference
The luminal domain of TGN38 interacts with integrin beta 1 and is involved in its trafficking
10.1034/j.1600-0854.2000.010904.x · doi-reference
TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN
10.1091/mbc.4.1.93 · doi-reference
The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
10.1083/jcb.125.2.253 · doi-reference
In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
10.1126/science.abd5223 · doi-reference
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
10.1038/s41586-020-2665-2 · doi-reference
Virus entry: molecular mechanisms and biomedical applications
10.1038/nrmicro817 · doi-reference
Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
10.1083/jcb.200110007 · doi-reference
ERK regulates Golgi and centrosome orientation towards the leading edge through GRASP65
10.1083/jcb.200805045 · doi-reference
GRASP depletion-mediated Golgi destruction decreases cell adhesion and migration via the reduction of α5β1 integrin
10.1091/mbc.e18-07-0462 · doi-reference
Nonredundant Roles of GRASP55 and GRASP65 in the Golgi Apparatus and Beyond
10.1016/j.tibs.2020.08.001 · doi-reference
Cytosolic Ca2+ Modulates Golgi Structure Through PKCα-Mediated GRASP55 Phosphorylation
10.1016/j.isci.2020.100952 · doi-reference
The Golgi stacking protein GORASP2/GRASP55 serves as an energy sensor to promote autophagosome maturation under glucose starvation
10.1080/15548627.2018.1491214 · doi-reference
An mTORC1-GRASP55 signaling axis controls unconventional secretion to reshape the extracellular proteome upon stress
10.1016/j.molcel.2021.06.017 · doi-reference
Golgi structure formation, function, and post-translational modifications in mammalian cells
10.12688/f1000research.11900.1 · doi-reference
Glycosylation Quality Control by the Golgi Structure
10.1016/j.jmb.2016.02.030 · doi-reference
GRASPs in Golgi Structure and Function
10.3389/fcell.2015.00084 · doi-reference
GRASP55 regulates the unconventional secretion and aggregation of mutant huntingtin
10.1016/j.jbc.2022.102219 · doi-reference
Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function
10.1091/mbc.e17-02-0112 · doi-reference
Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport
10.1371/journal.pone.0001647 · doi-reference
A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
10.1093/emboj/cdg317 · doi-reference
Mapping the functional domains of the Golgi stacking factor GRASP65
10.1074/jbc.m412407200 · doi-reference
Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly
10.1242/bio.20122659 · doi-reference
The role of GRASP65 in Golgi cisternal stacking and cell cycle progression
10.1111/j.1600-0854.2010.01055.x · doi-reference