The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection

A functional interaction between GRP78 and Zika virus E protein

(2021) Sarawut Khongwichit et al.   Scientific Reports

COVID-19 spike-host cell receptor GRP78 binding site prediction

(2020) Ibrahim M. Ibrahim et al.   JOURNAL OF INFECTION

Gene expression and in situ protein profiling of candidate SARS-CoV-2 receptors in human airway epithelial cells and lung tissue

(2020) Jennifer A. Aguiar et al.   EUROPEAN RESPIRATORY JOURNAL

The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection

(2020) Dat P. Ha et al.   JOURNAL OF INFECTION

Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity

(2020) Ludovico Cantuti-Castelvetri et al.   SCIENCE

AR12 (OSU-03012) suppresses GRP78 expression and inhibits SARS-CoV-2 replication

(2020) Jonathan O. Rayner et al.   BIOCHEMICAL PHARMACOLOGY

High GRP78 levels in Covid-19 infection: A case-control study

(2020) Ramazan Sabirli et al.   LIFE SCIENCES

Cell surface expression of 78 kDa glucose regulated protein (GRP78) mediates diabetic nephropathy

(2019) Richard Van Krieken et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells

(2018) Hin Chu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Endoplasmic reticulum stress activates SRC, relocating chaperones to the cell surface where GRP78/CD109 blocks TGF-β signaling

(2018) Yuan-Li Tsai et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends

(2018) Kristine Faye R. Pobre et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

GRP78 Is an Important Host Factor for Japanese Encephalitis Virus Entry and Replication in Mammalian Cells

(2017) Minu Nain et al.   JOURNAL OF VIROLOGY

Characterization and Mechanism of Stress-induced Translocation of 78-Kilodalton Glucose-regulated Protein (GRP78) to the Cell Surface

(2015) Yuan-Li Tsai et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

GRP78/Dna K Is a Target for Nexavar/Stivarga/Votrient in the Treatment of Human Malignancies, Viral Infections and Bacterial Diseases

(2015) Jane L. Roberts et al.   JOURNAL OF CELLULAR PHYSIOLOGY

HSPA5 is an essential host factor for Ebola virus infection

(2014) St. Patrick Reid et al.   ANTIVIRAL RESEARCH

Monoclonal Antibody against Cell Surface GRP78 as a Novel Agent in Suppressing PI3K/AKT Signaling, Tumor Growth, and Metastasis

(2013) R. Liu et al.   CLINICAL CANCER RESEARCH

The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies

(2012) B Luo et al.   ONCOGENE

Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting

(2011) Min Ni et al.   BIOCHEMICAL JOURNAL

GRP78: A Multifunctional Receptor on the Cell Surface

(2009) Mario Gonzalez–Gronow et al.   ANTIOXIDANTS & REDOX SIGNALING

Therapeutic angiogenesis of mouse hind limb ischemia by novel peptide activating GRP78 receptor on endothelial cells

(2007) Britta Hardy et al.   BIOCHEMICAL PHARMACOLOGY