Zobrazeno 1 - 10
of 92
pro vyhledávání: '"Frederick Esch"'
Autor:
Frederick Esch, Osvaldo Llanos, Enrique Brandan, Jaime Alvarez, Ricardo D. Moreno, Nibaldo C. Inestrosa, Tim Colby
Publikováno v:
Neuroscience Letters. 144:130-134
Protease inhibition is the mechanism by which some trophic factors promote the extension of neurites. In the rat sciatic nerve, we assessed the ability to induce sprouts of the APP isoform that embodies the Kunitz antiprotease domain and other antipr
Publikováno v:
Peptides. 13:133-139
HP-1 is the most abundant human representative of a recently discovered class of neutrophil cystine- and arginine-rich peptides. These peptides have many potentially regulatory activities expressed at nanomolar concentrations. To establish the levels
Autor:
William G. Conroy, Jon Lindstrom, Ralf Schoepfer, Martin Gore, Frederick Esch, Paul J. Whiting, Kent T. Keyser, Shunichi Shimasaki
Publikováno v:
Molecular Brain Research. 10:61-70
Neuronal nicotinic acetylcholine receptors (AChRs) are composed of two types of subunits: ACh-binding (termed alpha 2, alpha 3, alpha 4 ...) and structural (termed beta 2, beta 3, beta 4 ...). AChR subtypes composed of combinations of subunits of the
Autor:
David C. Turner, Salvatore Carbonetto, Mario Houde, Russell Blacher, Louis F. Reichardt, Nabil J. Tawil, Frederick Esch
Publikováno v:
Biochemistry. 29:6540-6544
A monoclonal antibody (3A3) raised against a rat neural cell line (PC12) was shown previously to bind to the surfaces of these cells, inhibiting substratum adhesion. Immunochemical and other data indicated that the heterodimer recognized by 3A3 was a
Publikováno v:
Neuron. 4:623-631
The validation of NGF as a physiologically important neurotrophic factor has led to intense efforts to identify novel polypeptide growth factors for neurons. We report here the details of a greater than 80,000-fold purification of a neurotrophic mole
Autor:
Justine Whaley, Peter Seubert, Dennis J. Selkoe, Carmen Vigo-Pelfrey, Harry F. Dovey, Robert L. Wolfert, Robert T. McCormack, Sukanto Sinha, Dale Schenk, Cathy Swindlehurst, Frederick Esch, Michael Schiossmacher, Michael K. Lee, Dave Davis, Ivan Lieberburg
Publikováno v:
Nature. 359:325-327
CEREBRAL deposition of the β-amyloid peptide (Aβ) is an invariant feature of Alzheimer's disease. Since the original isola-tion and characterization of αβ (ref. 1) and the subsequent cloning of its precursor protein2–5, no direct evidence for t
Autor:
Frederick Esch, Nikolaos K. Robakis, Kumar Sambamurti, Pamela S. Keim, John P. Anderson, Ivan Lieberburg
Publikováno v:
Neuroscience Letters. 128:126-128
We have identified the secretory cleavage site in the Alzheimer amyloid precursor (APP) in a non-transfected neuronal cell line, using cyanogen bromide digests of APP purified from medium conditioned by PC-12 cells which were differentiated to a neur
Autor:
Frederick Esch, Mark P. Mattson, Alan R. Culwell, Bin Cheng, Russell E. Rydel, Ivan Lieberburg
Publikováno v:
Neuron. 10(2)
The β-amyloid precursor protein (βAPP) is a membrane-spanning glycoprotein that is the source of the β-amyloid peptide (βAP) which accumulates as senile plaques in the brains of patients with Alzheimer's disease. βAPP is normally processed such
Autor:
David W. Leung, Annette S. Parent, Felix P. Eckenstein, Karoly Nikolics, George Cachianes, Rae Nishi, James N. Coulombe, Frederick Esch
Publikováno v:
Neuron. 8(6)
Ciliary ganglion (CG) neurons undergo a period of cell death during development that may be regulated by the limited availability of trophic factor produced by their target tissues. We have previously reported the purification of a ciliary neurotroph
Publikováno v:
The Journal of biological chemistry. 266(31)
Site-specific mutagenesis techniques have been used to construct active site variants of the Kunitz-type protease inhibitor domain present in the Alzheimer's beta-amyloid precursor protein (APP-KD). Striking alteration of its protease inhibitory prop