Results 21 to 30 of about 1,934 (175)

Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2

open access: yesToxins, 2016
Ricin is a type 2 ribosome-inactivating protein (RIP), containing a catalytic A chain and a lectin-like B chain. It inhibits protein synthesis by depurinating the N-glycosidic bond at α-sarcin/ricin loop (SRL) of the 28S rRNA, which thereby prevents the ...
Wei-Wei Shi   +5 more
doaj   +1 more source

Computational analysis of fusion protein of anti-HER2 scFv and alpha luffin: A new immunotoxin protein for HER2 positive cancers

open access: yesBrazilian Journal of Pharmaceutical Sciences, 2022
The present study deals with the computational design and analysis of a novel fusion protein based on a single chain variable fragment that binds to the extracellular domain of human epidermal growth factor receptor 2 (HER2) in breast cancer cells. Alpha
Farzaneh Barkhordari   +5 more
doaj   +1 more source

Enhancing the efficacy of cytotoxic agents for cancer therapy using photochemical internalisation. [PDF]

open access: yes, 2015
Photochemical internalisation (PCI) is a technique for improving cellular delivery of certain bioactive agents which are prone to sequestration within endolysosomes.
Adigbli   +69 more
core   +1 more source

Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation

open access: yesToxins, 2016
To improve the pharmacological properties of maize ribosome-inactivating protein (maize RIP) for targeting HIV-infected cells, the previously engineered TAT-fused active form of maize RIP (MOD) was further engineered for cysteine-directed PEGylation.
Ka-Yee Au   +4 more
doaj   +1 more source

Small-molecule inhibitor leads of ribosome-inactivating proteins developed using the doorstop approach. [PDF]

open access: yesPLoS ONE, 2011
Ribosome-inactivating proteins (RIPs) are toxic because they bind to 28S rRNA and depurinate a specific adenine residue from the α-sarcin/ricin loop (SRL), thereby inhibiting protein synthesis.
Yuan-Ping Pang   +11 more
doaj   +1 more source

Pokeweed Antiviral Protein, a Ribosome Inactivating Protein: Activity, Inhibition and Prospects

open access: yesToxins, 2015
Viruses employ an array of elaborate strategies to overcome plant defense mechanisms and must adapt to the requirements of the host translational systems. Pokeweed antiviral protein (PAP) from Phytolacca americana is a ribosome inactivating protein (RIP)
Artem V. Domashevskiy, Dixie J. Goss
doaj   +1 more source

Ribosome-inactivating proteins (RIPs) and their important health promoting property

open access: yesRSC Advances, 2016
Ribosome-inactivating proteins (RIPs), widely present in plants, certain fungi and bacteria, can inhibit protein synthesis by removing one or more specific adenine residues from the large subunit of ribosomal RNAs (rRNAs).
Shuzhen Wang   +5 more
openaire   +1 more source

A double safety lock tumor-specific device for suicide gene therapy in breast cancer [PDF]

open access: yes, 2020
Producción CientíficaThe complexity and continuous evolution of cancer make the design of novel strategies of treatment a constant challenge in biomedicine.
Arias Vallejo, Francisco Javier   +5 more
core   +2 more sources

Preparation of an antitumor and antivirus agent: chemical modification of α-MMC and MAP30 from Momordica Charantia L. with covalent conjugation of polyethyelene glycol [PDF]

open access: yes, 2012
Background: Alpha-momorcharin (α-MMC) and momordica anti-HIV protein (MAP30) derived from Momordica charantia L. have been confirmed to possess antitumor and antivirus activities due to their RNA-N-glycosidase activity. However, strong immunogenicity and
Li, Juan   +4 more
core   +1 more source

Dianthin and Its Potential in Targeted Tumor Therapies [PDF]

open access: yes, 2019
Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety.
Fuchs, Hendrik
core   +1 more source

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