Results 31 to 40 of about 24,109 (233)

Ribosome inactivating proteins and apoptosis

FEBS Letters, 2005
Ribosome inactivating proteins (RIPs) are protein toxins that are of plant or microbial origin that inhibit protein synthesis by inactivating ribosomes. Recent studies suggest that RIPs are also capable of inducing cell death by apoptosis. Though many reports are available on cell death induced by RIPs, the mechanism involved is not well studied ...
Narayanan, Sriram, Surendranath, Kalpana, Bora, Namrata, Surolia, Avadhesha, Karande, Anjali A   +4 more
openaire   +2 more sources

Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities. [PDF]

PLoS ONE, 2012
Ribosome-inactivating proteins (RIPs) inactivate prokaryotic or eukaryotic ribosomes by removing a single adenine in the large ribosomal RNA. Here we show maize RIP (MOD), an atypical RIP with an internal inactivation loop, interacts with the ribosomal ...
Yuen-Ting Wong, Yiu-Ming Ng, Amanda Nga-Sze Mak, Kong-Hung Sze, Kam-Bo Wong, Pang-Chui Shaw   +5 more
doaj   +1 more source

Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3 [PDF]

, 2004
Colicin E3 is a cytotoxic ribonuclease that specifically cleaves 16S rRNA at the ribosomal A-site to abolish protein synthesis in sensitive Escherichia coli cells.
Bohm, Boon, Bowman, Carr, Cuchillo, Garinot-Schneider, Irie, Kerr, Kleanthous, Kleanthous, Makarov, Mosbahi, Ogawa, Ohno, Ohno, Ohno-Iwashita, Parret, Pommer, Rojas, Scholz, Schultz, Sidikaro, Smarda, Soelaiman, Steege, Tomita, Walker, Walker, Walker, Walker, Wallis   +30 more
core   +2 more sources

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

, 2015
Photochemical internalisation (PCI) is a technique for improving cellular delivery of certain bioactive agents which are prone to sequestration within endolysosomes.
Adigbli, Adigbli, Arentsen, Baglo, Berg, Berg, Berg, Berg, Berstad, Bodles-Brakhop, Bostad, Bostad, Bull-Hansen, Castano, Castano, Chong, Dietze, Dietze, Elisabeth Olsen, Fretz, Gaware, Gooding, Gottesman, Hirschberg, Høgset, Jørgensen, Kunz, Lai, Lai, Lakshmanan, Lou, Lu, Lund, Mathews, Mroz, Mroz, Norum, Norum, Norum, Norum, Pasparakis, Peng, Peng, Prasmickaite, Reginato, Rosenblum, Selbo, Selbo, Selbo, Selbo, Selbo, Selbo, Selbo, Selbo, Selbo, St Denis, Stratford, Todorova, Vikdal, Wang, Wang, Wang, Weyergang, Weyergang, Woodhams, Xu, Yaghini, Yao, Yip, Zahreddine   +69 more
core   +1 more source

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]

, 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, Liu, Shuangfeng, Meng, Yanfa, Meng, Yao, Zhao, Xiaojun   +4 more
core   +1 more source

Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens [PDF]

, 2011
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A Babino, AA Jeyaprakash, AM Wu, AM Wu, AM Wu, AM Wu, AM Wu, AM Wu, AM Wu, AM Wu, E Zenteno, EJM Damme Van, GF Springer, GF Springer, GF Springer, GWG Bird, K Puri, KA Kulkarni, KA Kulkarni, M Duk, M Duk, M Sarkar, N Taniguchi, N Vega, R Lotan, R Ravishankar, R Sankaranarayanan, R Zenteno, S Hirohashi, S Tollefsen, SH Itzkowitz, SI Hakomori, SI Hakomori, SI Hakomori, SJ Rinderle, T Singh, T Singh, T Singh, TR Transue, V Piller, W Wang, X Lee, Y Yoda   +42 more
core   +3 more sources

Transcriptional profiling of colicin-induced cell death of Escherichia coli MG1655 identifies potential mechanisms by which bacteriocins promote bacterial diversity [PDF]

, 2004
We report the transcriptional response of Escherichia coli MG1655 to damage induced by colicins E3 and E9, bacteriocins that kill cells through inactivation of the ribosome and degradation of chromosomal DNA, respectively. Colicin E9 strongly induced the
Hinton, Jay C. D., James, Richard, Kleanthous, Colin, Moore, Geoffrey R., Rolfe, Matthew, Thompson, Arthur, WALKER, DANIEL   +6 more
core   +2 more sources

RIPpore: A Novel Host-Derived Method for the Identification of Ricin Intoxication through Oxford Nanopore Direct RNA Sequencing

Toxins, 2022
Ricin is a toxin which enters cells and depurinates an adenine base in the sarcin-ricin loop in the large ribosomal subunit, leading to the inhibition of protein translation and cell death.
Yan Ryan, Abbie Harrison, Hannah Trivett, Catherine Hartley, Jonathan David, Graeme C. Clark, Julian A. Hiscox   +6 more
doaj   +1 more source

Inhibition of HIV-1 replication by balsamin, a ribosome inactivating protein of Momordica balsamina [PDF]

, 2013
Ribosome-inactivating proteins (RIPs) are endowed with several medicinal properties, including antiviral activity. We demonstrate here that the recently identified type I RIP from Momordica balsamina also possesses antiviral activity, as determined by ...
Ahmed, Zahra, Blanchet, Fabien P., Kaur, Inderdeep, Mangeat, Bastien, Piguet, Vincent, Puri, Munish   +5 more
core   +4 more sources

Membrane fusion mediated by ricin and viscumin [PDF]

, 1998
The ribosome inactivating plant proteins (RIPs) ricin and viscumin but not Ricinus communis agglutinin are able induce vesicle–vesicle fusion. A model is suggested in which the toxicity of the RIPs is partially determined by their fusogenicity.
Peter Pohl, Yura N Antonenko, Veronika Y Evtodienko, Elena E Pohl, Sapar M Saparov, Igor I Agapov, Alexander G Tonevitsky, Lord, Brinkmann, Sandvig, Beaumelle, Bilge, Sandvig, O'Hare, Citores, Saltvedt, Barbieri, Bendas, Köhler, Tonevitsky, Woodbury, Mueller, MacDonald, Utsumi, Chernomordik, Simon, Hoekstra, Yoshida, Yoshida, Simpson, Rapak, Bau, Okimoto, Hudson, Siegel, Tonevitsky, Agapov, Goldmacher, Gottstein, Raso   +39 more
core   +1 more source