Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century
RJ Collier - Toxicon, 2001 - Elsevier
Diphtheria toxin is one of the most extensively studied and well understood bacterial toxins.
Ever since its discovery in the late 1800's this toxin has occupied a central focus in the field …
Ever since its discovery in the late 1800's this toxin has occupied a central focus in the field …
Biology and Molecular Epidemiology of Diphtheria Toxin and the tox Gene
RK Holmes - Journal of Infectious Diseases, 2000 - academic.oup.com
Diphtheria toxin (DT) is an extracellular protein of Corynebacterium diphtheriae that inhibits
protein synthesis and kills susceptible cells. The gene that encodes DT (tox) is present in …
protein synthesis and kills susceptible cells. The gene that encodes DT (tox) is present in …
[HTML][HTML] A metalloprotease–disintegrin, MDC9/meltrin‐γ/ADAM9 and PKCδ are involved in TPA‐induced ectodomain shedding of membrane‐anchored heparin …
Y Izumi, M Hirata, H Hasuwa, R Iwamoto… - The EMBO …, 1998 - embopress.org
The ectodomains of many proteins located at the cell surface are shed upon cell stimulation.
One such protein is the heparin‐binding EGF‐like growth factor (HB‐EGF) that exists in a …
One such protein is the heparin‐binding EGF‐like growth factor (HB‐EGF) that exists in a …
Heparin-binding EGF-like growth factor and ErbB signaling is essential for heart function
R Iwamoto, S Yamazaki, M Asakura… - Proceedings of the …, 2003 - National Acad Sciences
The heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) is a member
of the EGF family of growth factors that binds to and activates the EGF receptor (EGFR) and …
of the EGF family of growth factors that binds to and activates the EGF receptor (EGFR) and …
Diphtheria Toxin Binds to the Epidermal Growth Factor (EGF)-like Domain of Human Heparin-binding EGF-like Growth Factor/Diphtheria Toxin Receptor and Inhibits …
T Mitamura, S Higashiyama, N Taniguchi… - Journal of Biological …, 1995 - ASBMB
The membrane anchored form of human heparin-binding epidermal growth factor-like
growth factor (HB-EGF) acts as the diphtheria toxin (DT) receptor. Transfection of human HB …
growth factor (HB-EGF) acts as the diphtheria toxin (DT) receptor. Transfection of human HB …
Mammalian uroplakins. A group of highly conserved urothelial differentiation-related membrane proteins.
The asymmetric unit membrane (AUM) forms the apical plaques of mammalian urothelium
and is believed to play a role in strengthening the urothelial apical surface thus preventing …
and is believed to play a role in strengthening the urothelial apical surface thus preventing …
Heparin‐binding EGF‐like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up‐regulates …
R Iwamoto, S Higashiyama, T Mitamura… - The EMBO …, 1994 - embopress.org
DRAP27, the monkey homolog of human CD9 antigen (DRAP27/CD9) and diphtheria toxin
receptor (DTR) were expressed in mouse L cells. L cells transfected transiently with both …
receptor (DTR) were expressed in mouse L cells. L cells transfected transiently with both …
The membrane protein CD9/DRAP 27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor.
S Higashiyama, R Iwamoto, K Goishi, G Raab… - The Journal of cell …, 1995 - rupress.org
The membrane-anchored heparin-binding EGF-like growth factor precursor (proHB-
EGF)/diphtheria toxin receptor (DTR) belongs to a class of transmembrane growth factors …
EGF)/diphtheria toxin receptor (DTR) belongs to a class of transmembrane growth factors …
Uroplakins Ia and Ib, two major differentiation products of bladder epithelium, belong to a family of four transmembrane domain (4TM) proteins.
The mammalian bladder epithelium elaborates, as a terminal differentiation product, a
specialized plasma membrane called asymmetric unit membrane (AUM) which is believed …
specialized plasma membrane called asymmetric unit membrane (AUM) which is believed …
Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
Q Deng, JT Barbieri - Annu. Rev. Microbiol., 2008 - annualreviews.org
Bacterial pathogens utilize toxins to modify or kill host cells. The bacterial ADP-
ribosyltransferases are a family of protein toxins that covalently transfer the ADP-ribose …
ribosyltransferases are a family of protein toxins that covalently transfer the ADP-ribose …