A family of gram-negative, facultatively anaerobic, rod-shaped bacteria that do not form endospores. Its organisms are distributed worldwide with some being saprophytes and others being plant and animal parasites. Many species are of considerable economic importance due to their pathogenic effects on agriculture and livestock
Leclercq, Jean, 1911-1993. : Theologizing friendship : how amicitia in the thought of Aelred and Aquinas inscribes the scholastic turn / Nathan Lefler ; with a foreword by Austin G. Murphy, OSB
Lecomte, Alain, 1947- : Logic and grammar : essays dedicated to Alain Lecomte on the occasion of his 60th birthday / Sylvain Pogodalla, Myriam Quatrini, Christian Retoré (eds.)
LeConte, Mount (Tenn.) -- History : Smoky Jack : the adventures of a dog and his master on Mount Le Conte / by Paul J. Adams ; Anne Bridges and Ken Wise, editors
Lecoq, Jacques -- Interviews. : Commedia Oz : playing commedia in contemporary Australia / Steven Gration and Nicky Peelgrane
2008
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Pfahlbau -- Architektur -- LeCorbusier. : Le Corbusier, the noble savage : toward an archaeology of modernism / Adolf Max Vogt ; translated by Radka Donnell
1998
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Lecouturier, Henri -- Trials, litigation, etc : On appeal from His Majesty's Court of Appeal (England) between Henri Lecouturier, George Idle Chapman & Company, Limited, W. H. Garrett and La Compagnie Fermiere de la Grande Chartreuse, Appellants and Albert Rey and Augustin Marie Herbault (on behalf of themselves and all other members of The Carthusian Order and La Union Agricola), respondents
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins
A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins
A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition
A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms
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Lectins -- Therapeutic use : Galectins and disease implications for targeted therapeutics / Anatole A. Klyosov, Peter G. Traber, editors
