Results 21 to 30 of about 1,930 (169)
Natural Products with Inhibitory Activity against Human Immunodeficiency Virus Type 1
Infections caused by human immunodeficiency virus (HIV) are considered one of the main public health problems worldwide. Antiretroviral therapy (ART) is the current modality of treatment for HIV‐1 infection. It comprises the combined use of several drugs and can decrease the viral load and increase the CD4+ T cell count in patients with HIV‐1 infection,
Maria S. Serna-Arbeláez +6 more
wiley +1 more source
This review provides an updated and comprehensive overview on the ethnomedicinal use, phytochemistry, pharmacology, and toxicology of M. loriformis. Phytochemical analysis of M. loriformis revealed that it is composed of phenolics, flavonoids, condensed tannins, chlorophylls, alkaloids, and steroids.
Intan Soraya Che Sulaiman +3 more
wiley +1 more source
Impaired antibody-mediated protection and defective IgA B cell memory in experimental infection of adults with respiratory syncytial virus [PDF]
Rationale: Despite relative antigenic stability, respiratory syncytial virus (RSV) re-infects throughout life. After >40 years of research, no effective human vaccine exists and correlates of protection remain poorly defined.
Chiu, C +10 more
core +6 more sources
Depurination of plant ribosomes by pokeweed antiviral protein [PDF]
Mammalian ribosomes have been shown to be enzymatically modified by ribosomal inactivating protein (RIPs) via specific depurination of rRNA. Here we report that ribosomes isolated from wheat germ contain intact and undepurinated rRNA and are depurinated by pokeweed antiviral protein (PAP).
Taylor, Blair E., Irvin, James D.
openaire +2 more sources
Pokeweed Antiviral Protein Accesses Ribosomes by Binding to L3 [PDF]
Pokeweed antiviral protein (PAP), a 29-kDa ribosome-inactivating protein, catalytically removes an adenine residue from the conserved alpha-sarcin loop of the large rRNA, thereby preventing the binding of eEF-2.GTP complex during protein elongation. Because the alpha-sarcin loop has been placed near the peptidyltransferase center in Escherichia coli ...
K A, Hudak, J D, Dinman, N E, Tumer
openaire +2 more sources
Actions of Pokeweed Antiviral Protein on Virus-infected Protoplasts [PDF]
Pokeweed antiviral protein (PAP) belongs to a group of ribosome-inactivating proteins (RIPs) that inactivate ribosomes by depurinating rRNA at a specific site. To study the mechanism for the antiviral activity of PAP, the actions of PAP on TMV-infected and uninfected tobacco protoplasts were investigated.
K, Watanabe +3 more
openaire +2 more sources
Background Ricin A chain (RTA) and Pokeweed antiviral proteins (PAPs) are plant-derived N-glycosidase ribosomal-inactivating proteins (RIPs) isolated from Ricinus communis and Phytolacca Americana respectively. This study was to investigate the potential
Yasser Hassan, Sherry Ogg, Hui Ge
doaj +1 more source
Viruses and the cellular RNA decay machinery. [PDF]
The ability to control cellular and viral gene expression, either globally or selectively, is central to a successful viral infection, and it is also crucial for the host to respond and eradicate pathogens.
Gaglia, Marta, Glaunsinger, Britt
core +1 more source
Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]
Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core +2 more sources
Application or overexpression of α‐MMC in Nicotiana benthamiana increased resistance to TMV infection by means of modulating ROS homeostasis through controlling the expression of antioxidant enzyme‐encoding genes. Abstract Alpha‐momorcharin (α‐MMC), a member of the plant ribosomal inactivating proteins (RIPs) family, has been proven to exhibit ...
Feng Zhu +5 more
wiley +1 more source

