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Published by Springer
ISBN 10: 1555212417ISBN 13: 9781555212414
Seller: ThriftBooks-Dallas, Dallas, TX, U.S.A.
Book
Hardcover. Condition: Good. No Jacket. Pages can have notes/highlighting. Spine may show signs of wear. ~ ThriftBooks: Read More, Spend Less 3.1.
Published by Springer
ISBN 10: 1555212417ISBN 13: 9781555212414
Seller: ThriftBooks-Atlanta, AUSTELL, GA, U.S.A.
Book
Hardcover. Condition: Good. No Jacket. Missing dust jacket; Pages can have notes/highlighting. Spine may show signs of wear. ~ ThriftBooks: Read More, Spend Less 3.1.
Published by Springer
ISBN 10: 1555212417ISBN 13: 9781555212414
Seller: ThriftBooks-Dallas, Dallas, TX, U.S.A.
Book
Hardcover. Condition: Good. No Jacket. Missing dust jacket; Pages can have notes/highlighting. Spine may show signs of wear. ~ ThriftBooks: Read More, Spend Less 3.1.
Published by Springer, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: booksXpress, Bayonne, NJ, U.S.A.
Book
Soft Cover. Condition: new.
Published by Springer, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: booksXpress, Bayonne, NJ, U.S.A.
Book
Hardcover. Condition: new.
Published by Springer, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: Ria Christie Collections, Uxbridge, United Kingdom
Book Print on Demand
Condition: New. PRINT ON DEMAND Book; New; Fast Shipping from the UK. No. book.
Published by Springer, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: Ria Christie Collections, Uxbridge, United Kingdom
Book Print on Demand
Condition: New. PRINT ON DEMAND Book; New; Fast Shipping from the UK. No. book.
Published by Springer, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: Lucky's Textbooks, Dallas, TX, U.S.A.
Book
Condition: New.
Published by Springer, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: Lucky's Textbooks, Dallas, TX, U.S.A.
Book
Condition: New.
Published by Springer Berlin Heidelberg Sep 2012, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germany
Book Print on Demand
Taschenbuch. Condition: 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.
Published by Springer Berlin Heidelberg Jun 2010, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germany
Book Print on Demand
Buch. Condition: 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.
Published by Springer Berlin Heidelberg, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: moluna, Greven, Germany
Book Print on Demand
Gebunden. Condition: 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.
Published by Springer Berlin Heidelberg, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: moluna, Greven, Germany
Book Print on Demand
Condition: 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.
Published by Springer Berlin Heidelberg, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: AHA-BUCH GmbH, Einbeck, Germany
Book
Taschenbuch. Condition: 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.
Published by Springer Berlin Heidelberg, 2010
ISBN 10: 3642121756ISBN 13: 9783642121753
Seller: AHA-BUCH GmbH, Einbeck, Germany
Book
Buch. Condition: 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.
Published by Springer Verlag, 2013
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: Revaluation Books, Exeter, United Kingdom
Book
Paperback. Condition: Brand New. 2010 edition. 290 pages. 9.25x6.10x0.66 inches. In Stock.
Published by Springer, 2012
ISBN 10: 3642263771ISBN 13: 9783642263774
Seller: dsmbooks, Liverpool, United Kingdom
Book
Paperback. Condition: Like New. Like New. book.