Search Results - "Gonatas, JO"

Dysregulation of Stathmin, a Microtubule-Destabilizing Protein, and Up-Regulation of Hsp25, Hsp27, and the Antioxidant Peroxiredoxin 6 in a Mouse Model of Familial Amyotrophic Lateral Sclerosis by Strey, Christoph W., Spellman, Daniel, Stieber, Anna, Gonatas, Jacqueline O., Wang, Xiaosong, Lambris, John D., Gonatas, Nicholas K.

“…Gain-of-function mutations of the Cu/Zn superoxide dismutase (SOD1) gene cause dominantly inherited familial amyotrophic lateral sclerosis. The identification…”
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Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1(G93A) mutation of familial amyotrophic lateral sclerosis by Stieber, A, Gonatas, J O, Gonatas, N K

“…Mice expressing the G93A and other mutations of Cu,Zn superoxide dismutase (SOD1(G93A)) are valid models for the familial form of amyotrophic lateral sclerosis…”
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Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progression and fragmentation of the Golgi apparatus by Stieber, Anna, Gonatas, Jacqueline O, Gonatas, Nicholas K

“…Transgenic mice that express the G93A mutation of human Cu,Zn superoxide dismutase (SOD1 G93A), found in familial amyotrophic lateral sclerosis (FALS), showed…”
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Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis by Stieber, Anna, Gonatas, J.O., Moore, J.S., Bantly, Andrew, Yim, H.-S., Yim, M.B., Gonatas, N.K.

“…The Golgi apparatus of motor neurons (GA) is fragmented in sporadic amyotrophic lateral sclerosis (ALS), in familial ALS with SOD1 mutations, and in mice that…”
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The involvement of the Golgi apparatus in the pathogenesis of amyotrophic lateral sclerosis, Alzheimer's disease, and ricin intoxication by Gonatas, N K, Gonatas, J O, Stieber, A

“…Several diseases involving a variety of cells and tissues are associated with defective enzymes of the Golgi apparatus (GA). An intact GA of neurons is crucial…”
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The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene by Stieber, Anna, Gonatas, Jacqueline O, Collard, Jean-Francois, Meier, Jurgen, Julien, Jean-Pierre, Schweitzer, Peter, Gonatas, Nicholas K

“…Fragmentation of the Golgi apparatus (GA) of motor neurons was first described in sporadic amyotrophic lateral sclerosis (ALS) and later confirmed in…”
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Fragmentation of the Golgi apparatus of motor neurons in amyotrophic lateral sclerosis by Gonatas, NK, Stieber, A, Mourelatos, Z, Chen, Y, Gonatas, JO, Appel, SH, Hays, AP, Hickey, WF, Hauw, JJ

“…The Golgi apparatus (complex) is at the center stage of important functions of processing and transport of plasma membrane, lysosomal, and secreted proteins…”
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MG-160. A novel sialoglycoprotein of the medial cisternae of the Golgi apparatus [published eeratum appears in J Biol Chem 1989 Mar 5;264(7):4264] by Gonatas, J O, Mezitis, S G, Stieber, A, Fleischer, B, Gonatas, N K

“…A monoclonal antibody (mAb 10A8), derived from mice immunized with fractions of the Golgi apparatus from rat brain neurons, was exploited to isolate and…”
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MG-160, a membrane sialoglycoprotein of the medial cisternae of the rat Golgi apparatus, binds basic fibroblast growth factor and exhibits a high level of sequence identity to a chicken fibroblast growth factor receptor by Gonatas, J O, Mourelatos, Z, Stieber, A, Lane, W S, Brosius, J, Gonatas, N K

“…We report the primary structure of MG-160, a 160 kDa membrane sialoglycoprotein residing in the medial cisternae of the Golgi apparatus of rat neurons,…”
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Truncations of the C-terminal cytoplasmic domain of MG160, a medial Golgi sialoglycoprotein, result in its partial transport to the plasma membrane and filopodia by Gonatas, J O, Chen, Y J, Stieber, A, Mourelatos, Z, Gonatas, N K

“…MG160, a type I cysteine-rich membrane sialoglycoprotein residing in the medial cisternae of the rat Golgi apparatus, is highly homologous to CFR, a fibroblast…”
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The Golgi apparatus is present in perisynaptic, subependymal and perivascular processes of astrocytes and in processes of retinal Müller glia by Gonatas, Jacqueline O., Stieber, Anna, Gonatas, Nicholas K., Messing, Albee

“…The Golgi apparatus (GA) of innervated rat and chicken skeletal muscle is present in a typical perinuclear location, and in subsynaptic areas where it…”
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Cloning and sequence analysis of the human MG160, a fibroblast growth factor and E-selectin binding membrane sialoglycoprotein of the Golgi apparatus by Mourelatos, Z, Gonatas, J O, Cinato, E, Gonatas, N K

“…The amino acid sequence of MG160, a membrane sialoglycoprotein of the medial cisternae of the rat Golgi apparatus, is more than 90% identical with CFR, a…”
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Immunocytochemical visualization of the Golgi apparatus in several species, including human, and tissues with an antiserum against MG-160, a sialoglycoprotein of rat Golgi apparatus by Croul, S, Mezitis, SG, Stieber, A, Chen, YJ, Gonatas, JO, Goud, B, Gonatas, NK

“…We used a monoclonal antibody (10A8), derived from mice immunized with fractions enriched in Golgi apparatus of rat brain neurons, to isolate an intrinsic…”
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Fragmentation of the Golgi Apparatus of Motor Neurons in Amyotrophic Lateral Sclerosis Revealed by Organelle-Specific Antibodies by Mourelatos, Z., Adler, H., Hirano, A., Donnenfeld, H., Gonatas, J. O., Gonatas, N. K.

“…Many studies have established the central involvement of the Golgi apparatus in the transport and processing of plasma membrane, lysosomal, and secreted…”
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Assignment of the GLG1 Gene for MG-160, a Fibroblast Growth Factor and E-Selectin Binding Membrane Sialoglycoprotein of the Golgi Apparatus, to Chromosome 16q22-q23 by Fluorescence in Situ Hybridization by Mourelatos, Zissimos, Gonatas, Jacqueline O., Nycum, Lynn M., Gonatas, Nicholas K., Biegel, Jaclyn A.

“…MG-160, originally isolated from rat brain, is a conserved membrane sialoglycoprotein residing in the medial cisternae of the Golgi apparatus of virtually all…”
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Superior sensitivity of conjugates of horseradish peroxidase with wheat germ agglutinin for studies of retrograde axonal transport by Gonatas, NK, Harper, C, Mizutani, T, Gonatas, JO

“…We have compared the retrograde axonal transport of horseradish peroxidase (HRP), to the retrograde transport of HRP conjugated with wheat germ agglutinin…”
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Cholera toxin and wheat germ agglutinin conjugates as neuroanatomical probes: their uptake and clearance, transganglionic and retrograde transport and sensitivity by Wan, X C, Trojanowski, J Q, Gonatas, J O

“…Horseradish peroxidase (HRP) conjugates of 6 different lectins and cholera toxin (CTHRP) were quantitatively compared with respect to: (a) their behavior at…”
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Conjugates of horseradish peroxidase (HRP) with cholera toxin and wheat germ agglutinin are superior to free HRP as orthogradely transported markers by Trojanowski, J Q, Gonatas, J O, Gonatas, N K

“…The relative sensitivity of horseradish peroxidase (HRP) conjugates of cholera toxin (CTHRP) and wheat germ agglutinin (WGHRP) as orthogradely transported…”
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Horseradish peroxidase (HRP) conjugates of cholera toxin and lectins are more sensitive retrogradely transported markers than free HRP by Trojanowski, J Q, Gonatas, J O, Gonatas, N K

“…Horseradish peroxidase (HRP) conjugates of 8 different lectins (wheat germ agglutinin, ricinus communis I and II, peanut agglutinin, lens culinaris, soybean…”
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Cytoarchitecture of the extranuclear and commissural dendrites of hypoglossal nucleus neurons as revealed by conjugates of horseradish peroxidase with cholera toxin by Wan, X S, Trojanowski, J Q, Gonatas, J O, Liu, C N

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