Articoli correlati a Toxic Plant Proteins: 18
Many 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.
Le informazioni nella sezione "Riassunto" possono far riferimento a edizioni diverse di questo titolo.
Contenuti:
Evolution 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.
Product Description:
Book by None
Le informazioni nella sezione "Su questo libro" possono far riferimento a edizioni diverse di questo titolo.
- EditoreSpringer Verlag
- Data di pubblicazione2010
- ISBN 10 3642121756
- ISBN 13 9783642121753
- RilegaturaCopertina rigida
- Numero di pagine270
- RedattoreLord J. Michael, Hartley Martin R.
Compra nuovo
Scopri di più su questo articolo
EUR 160,83
Spese di spedizione:
GRATIS
In U.S.A.
I migliori risultati di ricerca su AbeBooks
Immagini fornite dal venditore
Toxic Plant Proteins (Plant Cell Monographs) [Hardcover ]
Da:
Valutazione libreria
Descrizione libro Hardcover. Condizione: new. Codice articolo 9783642121753
Compra nuovo
EUR 160,83
Convertire valuta
Foto dell'editore
Toxic Plant Proteins (Plant Cell Monographs, 18)
Da:
Valutazione libreria
Descrizione libro Condizione: New. Codice articolo ABLIING23Mar3113020218858
Compra nuovo
EUR 171,48
Convertire valuta
Foto dell'editore
Toxic Plant Proteins
Print on Demand
Da:
Valutazione libreria
Descrizione libro Condizione: New. PRINT ON DEMAND Book; New; Fast Shipping from the UK. No. book. Codice articolo ria9783642121753_lsuk
Compra nuovo
EUR 165,16
Convertire valuta
Immagini fornite dal venditore
Toxic Plant Proteins
Editore:
Springer Berlin Heidelberg Jun 2010
(2010)
ISBN 10: 3642121756
ISBN 13: 9783642121753
Nuovo
Rilegato
Quantità: 2
Da:
Valutazione libreria
Descrizione libro Buch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Many 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. 280 pp. Englisch. Codice articolo 9783642121753
Compra nuovo
EUR 160,49
Convertire valuta
Immagini fornite dal venditore
Toxic Plant Proteins
Editore:
Springer Berlin Heidelberg
(2010)
ISBN 10: 3642121756
ISBN 13: 9783642121753
Nuovo
Rilegato
Quantità: > 20
Da:
Valutazione libreria
Descrizione libro Gebunden. Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Written by acknowledged experts in the field the book focuses on the structure, function and some potential applications of toxic plant proteinsMany plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the re. Codice articolo 5049782
Compra nuovo
EUR 136,16
Convertire valuta
Immagini fornite dal venditore
Toxic Plant Proteins
Editore:
Springer Berlin Heidelberg
(2010)
ISBN 10: 3642121756
ISBN 13: 9783642121753
Nuovo
Rilegato
Quantità: 1
Da:
Valutazione libreria
Descrizione libro Buch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - Many 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. Codice articolo 9783642121753
Compra nuovo
EUR 164,03
Convertire valuta