نتایج جستجو برای: syt

تعداد نتایج: 361  

Journal: :The Journal of Cell Biology 2003
Ward C. Tucker J. Michael Edwardson Jihong Bai Hyun-Jung Kim Thomas F.J. Martin Edwin R. Chapman

The synaptotagmins (syts) are a family of membrane proteins proposed to regulate membrane traffic in neuronal and nonneuronal cells. In neurons, the Ca2+-sensing ability of syt I is critical for fusion of docked synaptic vesicles with the plasma membrane in response to stimulation. Several putative Ca2+-syt effectors have been identified, but in most cases the functional significance of these i...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Rodolfo R Llinás Mutsuyuki Sugimori Kimberly A Moran Jorge E Moreira Mitsunori Fukuda

Synaptotagmin (Syt) I, a ubiquitous synaptic vesicle protein, comprises a transmembrane region and two C2 domains. The C2 domains, which have been shown to be essential for both synaptic vesicle exocytosis and endocytosis, are also seen as the Ca(2+) sensors in synaptic vesicular release. In a previous study, we reported that a polyclonal antibody raised against the squid (Loligo pealei) Syt I ...

Journal: :Journal of immunology 2004
Kazunori Ida Satoshi Kawaguchi Yuriko Sato Tomohide Tsukahara Yuki Nabeta Hiroeki Sahara Hideyuki Ikeda Toshihiko Torigoe Shingo Ichimiya Kenjiro Kamiguchi Takuro Wada Satoshi Nagoya Hiroaki Hiraga Akira Kawai Takeshi Ishii Nobuhito Araki Akira Myoui Seiichi Matsumoto Toshifumi Ozaki Hideki Yoshikawa Toshihiko Yamashita Noriyuki Sato

To investigate the effects of anchor substitutions in SYT-SSX junction peptide, an HLA-A24 anchor residue (position 9) of the SYT-SSX B peptide (GYDQIMPKK) was substituted to more favorable residues according to the HLA-A24-binding motif. Among four substitutes constructed, a substitute with isoleucine (termed K9I peptide) most apparently enhanced the affinity for HLA-A24 molecule. Subsequent i...

2017
Farhad Shahi Razieh Alishahi Hossein Pashaiefar Isa Jahanzad Naser Kamalian Ardeshir Ghavamzadeh Marjan Yaghmaie

Background & Objective Soft tissue sarcomas (STS) constitute an uncommon and heterogeneous group of tumors of mesenchymal origin and various cytogenetic abnormalities ranging from distinct genomic rearrangements, such as chromosomal translocations and amplifications, to more intricate rearrangements involving multiple chromosomes. Fluorescence in situ hybridization (FISH) can be used to identif...

Journal: :The Biochemical journal 2013
Stefan Mahrhold Jasmin Strotmeier Consuelo Garcia-Rodriguez Jianlong Lou James D Marks Andreas Rummel Thomas Binz

The highly specific binding and uptake of BoNTs (botulinum neurotoxins; A-G) into peripheral cholinergic motoneurons turns them into the most poisonous substances known. Interaction with gangliosides accumulates the neurotoxins on the plasma membrane and binding to a synaptic vesicle membrane protein leads to neurotoxin endocytosis. SV2 (synaptic vesicle glycoprotein 2) mediates the uptake of B...

Journal: :The Journal of Cell Biology 2007
Min Dong William H. Tepp Huisheng Liu Eric A. Johnson Edwin R. Chapman

Botulinum neurotoxins (BoNTs) target presynaptic nerve terminals by recognizing specific neuronal surface receptors. Two homologous synaptic vesicle membrane proteins, synaptotagmins (Syts) I and II, bind toxins BoNT/B and G. However, a direct demonstration that Syts I/II mediate toxin binding and entry into neurons is lacking. We report that BoNT/B and G fail to bind and enter hippocampal neur...

Journal: :The Journal of Cell Biology 2003
Min Dong David A. Richards Michael C. Goodnough William H. Tepp Eric A. Johnson Edwin R. Chapman

Botulinum neurotoxins (BoNTs) cause botulism by entering neurons and cleaving proteins that mediate neurotransmitter release; disruption of exocytosis results in paralysis and death. The receptors for BoNTs are thought to be composed of both proteins and gangliosides; however, protein components that mediate toxin entry have not been identified. Using gain-of-function and loss-of-function appro...

Journal: :Neuron 2016
Olexiy Kochubey Norbert Babai Ralf Schneggenburger

Various Synaptotagmin (Syt) isoform genes are found in mammals, but it is unknown whether Syts can function redundantly in a given nerve terminal, or whether isoforms can be switched during the development of a nerve terminal. Here, we investigated the possibility of a developmental Syt isoform switch using the calyx of Held as a model synapse. At mature calyx synapses, fast Ca(2+)-driven trans...

Journal: :Anticancer research 2014
Hiroaki Kimura Norio Yamamoto Hideji Nishida Katsuhiro Hayashi Akihiko Takeuchi Takayuki Nojima Hiroko Ikeda Seiko Sawada-Kitamura Hiroyuki Tsuchiya

A 10-year-old boy underwent arthroscopic curettage for an intra-articular mass in knee joint. The tumor was diagnosed as low-grade fibrous sarcoma. Five years later, the patient presented with a recurrent tumor. The patient underwent a marginal excision with knee joint preservation and without adjuvant therapy. Two years after the last surgery, the patient is thriving with no evidence of recurr...

2018
Shinpei Ogino Hirotaka Konishi Daisuke Ichikawa Junichi Hamada Katsutoshi Shoda Tomohiro Arita Shuhei Komatsu Atsushi Shiozaki Kazuma Okamoto Sanae Yamazaki Satoru Yasukawa Eiichi Konishi Eigo Otsuji

Synovial sarcoma (SS) is genetically characterized by chromosomal translocation, which generates SYT-SSX fusion transcripts. Although SS can occur in any body part, primary gastric SS is substantially rare. Here we describe a detection of the fusion gene sequence of gastric SS in plasma cell-free DNA (cfDNA). A gastric submucosal tumor was detected in the stomach of a 27-year-old woman and diag...

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