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008 150903s2010 gw | o |||| 0|eng d
020 _a9783642121760
_99783642121760
024 7 _a10.1007/9783642121760
_2doi
035 _avtls000354833
039 9 _a201509030536
_bVLOAD
_c201405060341
_dVLOAD
_y201402191028
_zstaff
040 _aMX-SnUAN
_bspa
_cMX-SnUAN
_erda
050 4 _aQK861-899
100 1 _aLord, J. Michael.
_eeditor.
_9339432
245 1 0 _aToxic Plant Proteins /
_cedited by J. Michael Lord, Martin R. Hartley.
264 1 _aBerlin, Heidelberg :
_bSpringer Berlin Heidelberg :
_bImprint: Springer,
_c2010.
300 _ax, 270 páginas 41 ilustraciones, 12 ilustraciones en color.
_brecurso en línea.
336 _atexto
_btxt
_2rdacontent
337 _acomputadora
_bc
_2rdamedia
338 _arecurso en línea
_bcr
_2rdacarrier
347 _aarchivo de texto
_bPDF
_2rda
490 0 _aPlant Cell Monographs,
_x1861-1370 ;
_v18
500 _aSpringer eBooks
505 0 _aEvolution of Plant Ribosome-Inactivating Proteins -- RNA N-Glycosidase Activity of Ribosome-Inactivating Proteins -- Enzymatic Activities of Ribosome-Inactivating Proteins -- Type I Ribosome-Inactivating Proteins from Saponaria officinalis -- Type 1 Ribosome-Inactivating Proteins from the Ombú Tree (Phytolacca dioica L.) -- Sambucus Ribosome-Inactivating Proteins and Lectins -- Ribosome-Inactivating Proteins from Abrus pulchellus -- Ribosome-Inactivating Proteins in Cereals -- Ribosome Inactivating Proteins and Apoptosis -- The Synthesis of Ricinus communis Lectins -- How Ricin Reaches its Target in the Cytosol of Mammalian Cells -- Ribosome-Inactivating Protein-Containing Conjugates for Therapeutic Use.
520 _aMany plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.
590 _aPara consulta fuera de la UANL se requiere clave de acceso remoto.
700 1 _aHartley, Martin R.
_eeditor.
_9339433
710 2 _aSpringerLink (Servicio en línea)
_9299170
776 0 8 _iEdición impresa:
_z9783642121753
856 4 0 _uhttp://remoto.dgb.uanl.mx/login?url=http://dx.doi.org/10.1007/978-3-642-12176-0
_zConectar a Springer E-Books (Para consulta externa se requiere previa autentificación en Biblioteca Digital UANL)
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