Relevant bibliographies by topics / Myosin 1g

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'Myosin 1g'

Author: Grafiati
Published: 6 July 2024
Last updated: 31 July 2025

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Journal articles on the topic "Myosin 1g"

1

Estrada-Abreo, Laura A., Leonor Rodríguez-Cruz, Yanelly Garfias-Gómez, et al. "High expression of Myosin 1g in pediatric acute lymphoblastic leukemia." Oncotarget 12, no. 19 (2021): 1937–45. http://dx.doi.org/10.18632/oncotarget.28055.

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2

Dart, A. E., S. Tollis, M. D. Bright, G. Frankel, and R. G. Endres. "The motor protein myosin 1G functions in Fc R-mediated phagocytosis." Journal of Cell Science 125, no. 24 (2012): 6020–29. http://dx.doi.org/10.1242/jcs.109561.

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3

Konno, Tetsuo, Masami Shimizu, Hidekazu Ino, et al. "A novel mutation in the cardiac myosin-binding protein C gene is responsible for hypertrophic cardiomyopathy with severe ventricular hypertrophy and sudden death." Clinical Science 110, no. 1 (2005): 125–31. http://dx.doi.org/10.1042/cs20050189.

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It has been demonstrated previously that clinical phenotypes of HCM (hypertrophic cardiomyopathy) caused by mutations in the cardiac MyBP-C (myosin-binding protein C) gene show late onset, low penetrance and favourable clinical course. However, we have encountered severe phenotypes in several carriers of the MyBP-C gene mutations. The aim of the present study was to screen novel MyBP-C gene mutations in patients with HCM and to investigate the genetic differences in affected subjects with severe phenotypes. The MyBP-C gene was screened in 292 Japanese probands with HCM, and a novel c.2067+1G→A
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4

Méndez, Irene, Ana Isabel Fernández, Maria Ángeles Espinosa, et al. "Founder mutation in myosin-binding protein C with an early onset and a high penetrance in males." Open Heart 8, no. 2 (2021): e001789. http://dx.doi.org/10.1136/openhrt-2021-001789.

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ObjectiveOne of the challenges in hypertrophic cardiomyopathy (HCM) is to determine the pathogenicity of genetic variants and to establish genotype/phenotype correlations. This study aimed to: (1) demonstrate that MYBPC3 c.2149–1G>A is a founder pathogenic variant, (2) describe the phenotype and clinical characteristics of mutation carriers and (3) compare these patients with those with the most frequent pathogenic HCM variants: MYBPC3 p.Arg502Trp/Gln.MethodsWe reviewed genetic tests performed in HCM probands at our institution. We carried out transcript analyses to demonstrate the splicing
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5

Rodríguez-Téllez, Rosa Isela, Rosa María Ribas-Aparicio, and Genaro Patiño-López. "Detection of Myosin 1g Overexpression in Pediatric Leukemia by Novel Monoclonal Antibodies." International Journal of Molecular Sciences 23, no. 7 (2022): 3912. http://dx.doi.org/10.3390/ijms23073912.

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Myosin 1g (Myo1g) is a mechanoenzyme associated with actin filaments, expressed exclusively in hematopoietic cells, and involved in various cellular functions, including cell migration, adhesion, and membrane trafficking. Despite the importance of Myo1g in distinct functions, there is currently no monoclonal antibody (mAb) against Myo1g. mAbs are helpful tools for the detection of specific antigens in tumor cells and other tissues. The development of mAbs against targeted dysregulated molecules in cancer cells remains a crucial tool for aiding in the diagnosis and the treatment of patients. Us
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6

Olety, Balaji, Mike Wälte, Ulrike Honnert, Hermann Schillers, and Martin Bähler. "Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity." FEBS Letters 584, no. 3 (2009): 493–99. http://dx.doi.org/10.1016/j.febslet.2009.11.096.

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7

Maravillas-Montero, José L., Orestes López-Ortega, Genaro Patiño-López, and Leopoldo Santos-Argumedo. "Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes." European Journal of Immunology 44, no. 3 (2014): 877–86. http://dx.doi.org/10.1002/eji.201343873.

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8

Patino Lopez, Genaro, E. Michael Ostap, and Stephen Shaw. "Myosin 1G is a hematopoietic-restricted protein highly enriched in lymphocyte plasma membrane/microvilli whose deficiency impairs lymphocyte activation (35.40)." Journal of Immunology 182, no. 1_Supplement (2009): 35.40. http://dx.doi.org/10.4049/jimmunol.182.supp.35.40.

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Abstract Class I myosins regulate diverse aspects of locomotion, vesicular traffic, and peripheral process architecture in amoeba and in mammalian cells. Mass spectrometric analysis of lymphocyte fractions enriched for plasma membrane/microvilli identified myosin 1G (Myo1G) as abundant and enriched from human peripheral blood T-cells and Myo1G plus Myo1C as abundant and enriched from a mouse pre-B-cell line. To understand its structure and function, we have investigated Myo1G by immunofluorescence, by immunoblot, by transfection of wt and mutant constructs and by creation of a knockout mouse.
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9

Picquet, F., V. Bouet, L. Cochon, M. Lacour, and M. Falempin. "Changes in rat soleus muscle phenotype consecutive to a growth in hypergravity followed by normogravity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 289, no. 1 (2005): R217—R224. http://dx.doi.org/10.1152/ajpregu.00596.2004.

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It has been demonstrated that a long-term stay in hypergravity (HG: 2G) modified the phenotype and the contractile properties of rat soleus muscle. The ability of this muscle to contract was drastically reduced, which is a sign of anticipated aging. Consequently, our aim was to determine whether rats conceived, born, and reared in hypergravity showed adaptative capacities in normogravity (NG: 1G). This study was performed on rats divided into two series: the first was reared in HG until 100 days and was submitted to normogravity until 115 to 220 postnatal days (HG-NG rats); the second was made
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10

Patino-Lopez, Genaro, L. Aravind, Xiaoyun Dong, Michael J. Kruhlak, E. Michael Ostap, and Stephen Shaw. "Myosin 1G Is an Abundant Class I Myosin in Lymphocytes Whose Localization at the Plasma Membrane Depends on Its Ancient Divergent Pleckstrin Homology (PH) Domain (Myo1PH)." Journal of Biological Chemistry 285, no. 12 (2010): 8675–86. http://dx.doi.org/10.1074/jbc.m109.086959.

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Dissertations / Theses on the topic "Myosin 1g"

1

Janardhana, Kurup Akshai. "Étude de la myosine nonconventionelle myosine1g dans l'asymétrie droite-gauche du poisson zèbre." Electronic Thesis or Diss., Université Côte d'Azur, 2022. http://www.theses.fr/2022COAZ6028.

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L'asymétrie Droite-Gauche (DG) fait référence au placement asymétrique des organes par rapport à la ligne médiane du corps. Des dérèglements de l'établissement de l'asymétrie DG au cours du développement peuvent conduire à des organes mal placés - une situation qui peut être mortelle.J'utilise le poisson zèbre pour étudier les mécanismes qui établissent l'asymétrie DG. Chez le poisson, un organe cilié - la vésicule de Kupffer (KV) agit comme Organisateur central de l'asymétrie DG (ODG). Le ligand nodal Southpaw (Spaw) et son antagoniste Dand5 sont initialement exprimés de manière symétrique au
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Conference papers on the topic "Myosin 1g"

1

Souza, Taís Aparecida Matozo de, Letícia Kogachi, Maria Clara Martins Ferreira, Tania Carolina Reis, and Bruna Alencar. "Myosin 1g involvement in HIV-1 entry and infection in Jurkat cells." In Anais do XXXII Congresso Brasileiro de Virologia: Virologia em Casa. Even3, 2021. http://dx.doi.org/10.29327/146355.32-11.

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Journal articles
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