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Relevant bibliographies by topics / Huntingtin-interacting protein 7

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Journal articles

Academic literature on the topic 'Huntingtin-interacting protein 7'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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Journal articles on the topic "Huntingtin-interacting protein 7"

1

Rao, Dinesh S., Sarah V. Bradley, Priti D. Kumar, et al. "Altered receptor trafficking in Huntingtin Interacting Protein 1-transformed cells." Cancer Cell 3, no. 5 (2003): 471–82. http://dx.doi.org/10.1016/s1535-6108(03)00107-7.

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2

Tanno, Yoshihiro, Tetsuji Mori, Sachihiko Yokoya, et al. "Localization of huntingtin-interacting protein-2 (Hip-2) mRNA in the developing mouse brain." Journal of Chemical Neuroanatomy 17, no. 2 (1999): 99–107. http://dx.doi.org/10.1016/s0891-0618(99)00030-7.

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3

Mandela, Prashant, and Xin-Ming Ma. "Kalirin, a Key Player in Synapse Formation, Is Implicated in Human Diseases." Neural Plasticity 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/728161.

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Synapse formation is considered to be crucial for learning and memory. Understanding the underlying molecular mechanisms of synapse formation is a key to understanding learning and memory. Kalirin-7, a major isoform of Kalirin in adult rodent brain, is an essential component of mature excitatory synapses. Kalirin-7 interacts with multiple PDZ-domain-containing proteins including PSD95, spinophilin, and GluR1 through its PDZ-binding motif. In cultured hippocampal/cortical neurons, overexpression of Kalirin-7 increases spine density and spine size whereas reduction of endogenous Kalirin-7 expres

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4

Engel, Bastian, Jana Diestelhorst, Maciej K. Janik, et al. "THU-003-European multicenter validation of autoantibodies against huntingtin-interacting protein 1-related protein for the diagnosis of autoimmune hepatitis in adults." Journal of Hepatology 70, no. 1 (2019): e162. http://dx.doi.org/10.1016/s0618-8278(19)30287-7.

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5

Xiang, Jianxing, Su Yang, Ning Xin, et al. "DYRK1A regulates Hap1–Dcaf7/WDR68 binding with implication for delayed growth in Down syndrome." Proceedings of the National Academy of Sciences 114, no. 7 (2017): E1224—E1233. http://dx.doi.org/10.1073/pnas.1614893114.

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Huntingtin-associated protein 1 (Hap1) is known to be critical for postnatal hypothalamic function and growth. Hap1 forms stigmoid bodies (SBs), unique neuronal cytoplasmic inclusions of unknown function that are enriched in hypothalamic neurons. Here we developed a simple strategy to isolate the SB-enriched fraction from mouse brain. By analyzing Hap1 immunoprecipitants from this fraction, we identified a Hap1-interacting SB component, DDB1 and CUL4 associated factor 7 (Dcaf7)/WD40 repeat 68 (WDR68), whose protein level and nuclear translocation are regulated by Hap1. Moreover, we found that

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6

Schäffers, Olivier J. M., Joost G. J. Hoenderop, René J. M. Bindels, and Jeroen H. F. de Baaij. "The rise and fall of novel renal magnesium transporters." American Journal of Physiology-Renal Physiology 314, no. 6 (2018): F1027—F1033. http://dx.doi.org/10.1152/ajprenal.00634.2017.

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Body Mg2+ balance is finely regulated in the distal convoluted tubule (DCT), where a tight interplay among transcellular reabsorption, mitochondrial exchange, and basolateral extrusion takes place. In the last decades, several research groups have aimed to identify the molecular players in these processes. A multitude of proteins have been proposed to function as Mg2+ transporter in eukaryotes based on phylogenetic analysis, differential gene expression, and overexpression studies. However, functional evidence for many of these proteins is lacking. The aim of this review is, therefore, to crit

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7

Alshafie, Walaa, Maryam Fotouhi, Irina Shlaifer, Thomas M. Durcan, Peter S. McPherson, and Carl Laflamme. "Antibody Characterization Report for Optineurin." April 30, 2021. https://doi.org/10.5281/zenodo.4730992.

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Head to head comparison of available commercial antibodies against Optineurin by immunoblot (Western blot), immunoprecipitation and immunofluorescence. The following study was funded in part by Genome Québec's Genomics Integration Program, awarded to the laboratory of Peter S. McPherson. This work is part of the ALS-Reproducible Antibody Platform (ALS-RAP), established as a public-private partnership by three prominent ALS charities - the ALS Association (USA), the Motor Neurone Disease Association (UK), and the ALS Society of Canada.

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8

Yue, Hong-Wei, Jun-Ye Hong, Shu-Xian Zhang, Lei-Lei Jiang, and Hong-Yu Hu. "PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates." Scientific Reports 11, no. 1 (2021). http://dx.doi.org/10.1038/s41598-021-87382-w.

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AbstractPolyglutamine (polyQ) expansion of proteins can trigger protein misfolding and amyloid-like aggregation, which thus lead to severe cytotoxicities and even the respective neurodegenerative diseases. However, why polyQ aggregation is toxic to cells is not fully elucidated. Here, we took the fragments of polyQ-expanded (PQE) ataxin-7 (Atx7) and huntingtin (Htt) as models to investigate the effect of polyQ aggregates on the cellular proteostasis of endogenous ataxin-3 (Atx3), a protein that frequently appears in diverse inclusion bodies. We found that PQE Atx7 and Htt impair the cellular p

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9

Ruíz, Moleón Vera, Maryam Fotouhi, Charles Alende, et al. "Antibody Characterization Report for Optineurin (2023)." November 9, 2023. https://doi.org/10.5281/zenodo.10091740.

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This report presents a guide to selecting high-quality commercial antibodies against Optineurin by immunoblot (Western blot), immunoprecipitation and immunofluorescence, using a knockout based validation approach. The research displayed in this study can be considered a subsequent study following the initial Optineurin report published to the YCharOS community in 2021 (DOI:10.5281/zenodo.4730992). Antibodies ab213556**, 60293-1-Ig*, 702766** and 711879**, previously characterized in the initial report, were retested in all three applications, employing our revised standardized protocols.

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10

Kachemov, Marketta, Vineet Vaibhav, Charlene Smith, et al. "Dysregulation of protein SUMOylation networks in Huntington’s disease R6/2 mouse striatum." Brain, October 11, 2024. http://dx.doi.org/10.1093/brain/awae319.

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Abstract Huntington’s disease (HD) is a neurodegenerative disorder caused by an expanded CAG repeat mutation in the Huntingtin (HTT) gene. The mutation impacts neuronal protein homeostasis and cortical/striatal circuitry. SUMOylation is a post-translational modification with broad cellular effects including via modification of synaptic proteins. Here, we used an optimised SUMO protein-enrichment and mass spectrometry method to identify the protein SUMOylation/SUMO interaction proteome in the context of HD using R6/2 transgenic and non-transgenic (NT) mice. Significant changes in enrichment of

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