Results 221 to 230 of about 25,229 (271)

Unveiling key genetic loci and candidate genes for brown spot disease resistance in rice based on QTL analysis. [PDF]

Sci Rep
Zhao DD, Chung H, Farooq M, Kim NG, Choi SY, Kim S, Kim SM, Lee JH, Du XX, Kim KM.   +9 more
europepmc   +1 more source

Structure of Ribosome-Inactivating Protein from <i>Mirabilis jalapa</i> and Its L12-Stalk-Dependent Inhibition of <i>Escherichia coli</i> Ribosome. [PDF]

Toxins (Basel)
Nishida N, Ninomiya Y, Yoshida T, Tanzawa T, Maki Y, Yoshida H, Tsuge H, Habuka N.   +7 more
europepmc   +1 more source

Biological activity of ribosome-inactivating proteins from rice and their involvement in stress responses

, 2020
Jeroen De Zaeytijd
openalex   +1 more source

Recombinant tritin protein exhibits antiviral activity against zucchini yellow mosaic virus. [PDF]

BMC Plant Biol
Demi̇rel S, Usta M, Korkmaz G, Kurt Z.
europepmc   +1 more source

Ricin and Abrin in Biosecurity: Detection Technologies and Strategic Responses. [PDF]

Toxins (Basel)
Zajaczkowski W, Bojarska E, Furtak E, Bijak M, Szelenberger R, Niemcewicz M, Podogrocki M, Stela M, Cichon N.   +8 more
europepmc   +1 more source

An improved lentivirus vector for safer transgene integration and protein transduction [PDF]

Schenkwein, Diana
core  

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Ribosome-inactivating proteins from plants

BBA - Biomembranes, 1993
Maria Giulia Battelli
exaly   +3 more sources

The Structure of Ribosome Inactivating Proteins

Mini-Reviews in Medicinal Chemistry, 2004
Ribosome Inactivating Proteins, RIPs, depurinate an invariant adenine from the 28S rRNA of eukaryotic ribosomes; they have evolved to near enzymatic perfection for this task. The N-glycosidase fold is conserved in plant and bacterial enzymes. RIPs can form complexes with cell surface recognition proteins that dramatically increase the cytotoxicity of ...
Jon D, Robertus, Arthur F, Monzingo
openaire   +2 more sources

Ribosome-inactivating proteins up to date

FEBS Letters, 1986
Ribosome‐inactivating proteins (RIPs) from plants inactivate eukaryotic ribosomes, as far as studied by rendering their 60 S subunit unable to bind elongation factor 2. These proteins seem widely distributed and possibly ubiquitous in plants. They are either type 1, those consisting of a single polypeptide chain, or type 2 (ricin and related toxins ...
Stirpe, Fiorenzo, Barbieri, Luigi
exaly   +3 more sources