Relevant bibliographies by topics / ICA512/IA-2

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'ICA512/IA-2'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "ICA512/IA-2"

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Torkko, Juha M., M. Evangelina Primo, Ronald Dirkx та ін. "Stability of proICA512/IA-2 and Its Targeting to Insulin Secretory Granules Require β4-Sheet-Mediated Dimerization of Its Ectodomain in the Endoplasmic Reticulum". Molecular and Cellular Biology 35, № 6 (2015): 914–27. http://dx.doi.org/10.1128/mcb.00994-14.

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The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown. Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro . Here we show that ME ICA512 prompts proICA512 dimerization in the endoplasmic reticulum. Perturbation of ME ICA512 β2-strand N-glycosylation upon S508A replacement allows for proICA512 dimerization, O -
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2

Trajkovski, Mirko, Hassan Mziaut, Anke Altkrüger та ін. "Nuclear translocation of an ICA512 cytosolic fragment couples granule exocytosis and insulin expression in β-cells". Journal of Cell Biology 167, № 6 (2004): 1063–74. http://dx.doi.org/10.1083/jcb.200408172.

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Islet cell autoantigen 512 (ICA512)/IA-2 is a receptor tyrosine phosphatase-like protein associated with the insulin secretory granules (SGs) of pancreatic β-cells. Here, we show that exocytosis of SGs and insertion of ICA512 in the plasma membrane promotes the Ca2+-dependent cleavage of ICA512 cytoplasmic domain by μ-calpain. This cleavage occurs at the plasma membrane and generates an ICA512 cytosolic fragment that is targeted to the nucleus, where it binds the E3-SUMO ligase protein inhibitor of activated signal transducer and activator of transcription-y (PIASy) and up-regulates insulin ex
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3

Myers, M. A., M. R. Laks, S. J. Feeney, et al. "Antibodies to ICA512/IA-2 in Rodent Models of IDDM." Journal of Autoimmunity 11, no. 3 (1998): 265–72. http://dx.doi.org/10.1006/jaut.1998.0192.

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4

Kawasaki, Eiji, Liping Yu, Roberto Gianani, et al. "Evaluation of Islet Cell Antigen (ICA) 512/IA-2 Autoantibody Radioassays Using Overlapping ICA512/IA-2 Constructs1." Journal of Clinical Endocrinology & Metabolism 82, no. 2 (1997): 375–80. http://dx.doi.org/10.1210/jcem.82.2.3723.

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5

Kawasaki, E. "Evaluation of Islet Cell Antigen (ICA) 512/IA-2 Autoantibody Radioassays Using Overlapping ICA512/IA-2 Constructs." Journal of Clinical Endocrinology & Metabolism 82, no. 2 (1997): 375–80. http://dx.doi.org/10.1210/jc.82.2.375.

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6

Sosa, Laura, Juha M. Torkko, María E. Primo, et al. "Biochemical, biophysical, and functional properties of ICA512/IA-2 RESP18 homology domain." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1864, no. 5 (2016): 511–22. http://dx.doi.org/10.1016/j.bbapap.2016.01.013.

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7

Miao, Dongmei, Liping Yu, Claudio Tiberti, et al. "ICA512(IA-2) Epitope Specific Assays Distinguish Transient from Diabetes Associated Autoantibodies." Journal of Autoimmunity 18, no. 2 (2002): 191–96. http://dx.doi.org/10.1006/jaut.2001.0577.

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8

Eisenbarth, George S., and Joy Jeffrey. "The natural history of type 1A diabetes." Arquivos Brasileiros de Endocrinologia & Metabologia 52, no. 2 (2008): 146–55. http://dx.doi.org/10.1590/s0004-27302008000200002.

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We can now predict the development of Type 1A (Immune Mediated) diabetes primarily through the determination of four biochemically characterized islet autoantibodies [insulin, GAD65, IA-2 (ICA512) and (Znt8)]. Prediction is possible because beta-cell destruction is chronically progressive and very slow in most, but not all individuals. We can also prevent type 1A diabetes in animal models and a major goal is the prevention of type 1A diabetes in man with multiple clinical trials underway.
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9

Cunningham, JL, ET Janson, B. Eriksson, K. Oberg, and AE Gobl. "Transmembrane protein tyrosine phosphatase IA-2 (ICA512) is expressed in human midgut carcinoids but is not detectable in normal enterochromaffin cells." Journal of Endocrinology 164, no. 3 (2000): 315–22. http://dx.doi.org/10.1677/joe.0.1640315.

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A potential upregulation of receptor type protein tyrosine phosphatase IA-2 (ICA512) expression was detected by differential display and investigated in midgut carcinoid tumours. Normal intestine tissue and tumour tissue from 13 midgut carcinoid patients were studied by in situ hybridisation using an IA-2 ribonucleotide probe and confocal microscopy using specific IA-2 antibodies. Previously, it had been shown that IA-2 is located in the secretory granules of virtually all neuroendocrine cells. However, we found that IA-2 was not detectable in resting normal enterochromaffin (EC) cells of the
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10

Yokota, I., J. Matsuda, E. Naito, M. Ito, K. Shima, and Y. Kuroda. "Comparison of GAD and ICA512/IA-2 Antibodies at and After the Onset of IDDM." Diabetes Care 21, no. 1 (1998): 49–52. http://dx.doi.org/10.2337/diacare.21.1.49.

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Dissertations / Theses on the topic "ICA512/IA-2"

1

Schubert, Sandra. "The Role of [beta]2-Syntrophin Phosphorylation in Secretory Granule Exocytosis." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2006. http://nbn-resolving.de/urn:nbn:de:swb:14-1146851994562-42414.

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The trafficking of insulin secretory granules(SGs) of pancreatic b-cells is a tightly controlled complex network. Increasing evidence indicates that the cortical actin cytoskeleton modulates the mobility and exocytosis of SGs,yet the mechanisms anchoring SGs to the cytoskeleton is not completely understood.It has been shown by Ort et al.(2000,2001) that the cytoplasmic tail of an intrinsic membrane protein of the SGs named ICA512/IA-2 binds the PDZ domain of b2-syntrophin,which in turn binds to the F-actin-binding protein utrophin. These data also indicate that stimulation of SG exocytosis aff
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2

Schubert, Sandra. "The Role of [beta]2-Syntrophin Phosphorylation in Secretory Granule Exocytosis." Doctoral thesis, Technische Universität Dresden, 2005. https://tud.qucosa.de/id/qucosa%3A23710.

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Abstract:
The trafficking of insulin secretory granules(SGs) of pancreatic b-cells is a tightly controlled complex network. Increasing evidence indicates that the cortical actin cytoskeleton modulates the mobility and exocytosis of SGs,yet the mechanisms anchoring SGs to the cytoskeleton is not completely understood.It has been shown by Ort et al.(2000,2001) that the cytoplasmic tail of an intrinsic membrane protein of the SGs named ICA512/IA-2 binds the PDZ domain of b2-syntrophin,which in turn binds to the F-actin-binding protein utrophin. These data also indicate that stimulation of SG exocytosis aff
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