Localisation of islet amyloid polypeptide (IAPP) in pancreatic islets of transgenic mice expressing the human or rat IAPP gene. 1993

E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
Dept. of Human Anatomy, University of Oxford, UK.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D007515 Islets of Langerhans Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN. Islands of Langerhans,Islet Cells,Nesidioblasts,Pancreas, Endocrine,Pancreatic Islets,Cell, Islet,Cells, Islet,Endocrine Pancreas,Islet Cell,Islet, Pancreatic,Islets, Pancreatic,Langerhans Islands,Langerhans Islets,Nesidioblast,Pancreatic Islet
D008297 Male Males
D008822 Mice, Transgenic Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN. Transgenic Mice,Founder Mice, Transgenic,Mouse, Founder, Transgenic,Mouse, Transgenic,Mice, Transgenic Founder,Transgenic Founder Mice,Transgenic Mouse
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013045 Species Specificity The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species. Species Specificities,Specificities, Species,Specificity, Species

Related Publications

E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
October 1994, Nihon rinsho. Japanese journal of clinical medicine,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
December 2006, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
April 1999, Metabolism: clinical and experimental,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
January 1997, Regulatory peptides,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
September 1989, Diabetes research and clinical practice,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
December 2000, Molecular medicine (Cambridge, Mass.),
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
May 1996, Regulatory peptides,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
March 2013, Transplantation proceedings,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
July 1996, Proceedings of the National Academy of Sciences of the United States of America,
E J De Koning, and J W Höppener, and C Oosterwijk, and S J Verbeek, and H J Visser, and H S Jansz, and C J Lips, and J F Morris, and A Clark
June 2006, Diabetologia,
Copied contents to your clipboard!