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L. K. Rasmussen, E. S. Sorensen, T. E. Petersen, J. Gliemann and P. H. Jensen, “Identification of Glutamine and Lysine Residues in Alzheimer Amyloid Beta A4 Pep- tide Responsible for Transglutaminase-Catalysed Homo- polymerization and Cross-Linking to Alpha 2M Receptor,” FEBS Letters, Vol. 338, No. 2, 1994, pp. 161-166.

has been cited by the following article:

• TITLE: The Functions of the Amyloid Precursor Protein Gene and Its Derivative Peptides: II Experimental Evidence and Clinical Studies

  AUTHORS: Peter K. Panegyres, Emily R. Atkins

  KEYWORDS: Amyloid Precursor Protein Gene

  JOURNAL NAME: Neuroscience and Medicine, Vol.2 No.3, September 28, 2011

  ABSTRACT: In vitro studies suggest Amyloid Precursor Protein Gene (APP) is involved in interaction with the extracellular matrix, neurite growth, adhesion, development, synaptic function, platelet function, and interaction with GTP binding proteins. In vivo experiments show a role in embryonic development, response to cerebral excitotoxicity and gliosis, response to brain injury including ischaemia, hypothalamic function, locomotor function, learning and memory. In vitro observations indicate Aβ has a role in amyloid formation, excitotoxic neuronal injury, tachykinin interaction, endothelial vasoconstrictor response, calcium and oxidative stress, free radical interaction, cell membrane fluidity, apoptosis, astrocyte stimulation, and microglial interaction. Other studies suggest important roles for Aβ oligomers in synaptic function and as an antimicrobial peptide. In vivo investigations show involvement in memory function, the blood brain barrier, and tachykinin response to cerebral injury.