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Relevant bibliographies by topics / Neu4

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Journal articles

Academic literature on the topic 'Neu4'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Neu4"

1

Manzoni, Marta, Paolo Colombi, Nadia Papini, et al. "Molecular cloning and biochemical characterization of sialidases from zebrafish (Danio rerio)." Biochemical Journal 408, no. 3 (2007): 395–406. http://dx.doi.org/10.1042/bj20070627.

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Sialidases remove sialic acid residues from various sialo-derivatives. To gain further insights into the biological roles of sialidases in vertebrates, we exploited zebrafish (Danio rerio) as an animal model. A zebrafish transcriptome- and genome-wide search using the sequences of the human NEU polypeptides as templates revealed the presence of seven different genes related to human sialidases. neu1 and neu4 are the putative orthologues of the mammalian sialidases NEU1 and NEU4 respectively. Interestingly, the remaining genes are organized in clusters located on chromosome 21 and are all more

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2

Zhang, Jun-Yuan, Qian-Qian Chen, Jia Li, Lei Zhang, and Lian-Wen Qi. "Neuraminidase 1 and its Inhibitors from Chinese Herbal Medicines: An Emerging Role for Cardiovascular Diseases." American Journal of Chinese Medicine 49, no. 04 (2021): 843–62. http://dx.doi.org/10.1142/s0192415x21500403.

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Neuraminidase, also known as sialidase, is ubiquitous in animals and microorganisms. It is predominantly distributed in the cell membrane, cytoplasmic vesicles, and lysosomes. Neuraminidase generally recognizes the sialic acid glycosidic bonds at the ends of glycoproteins or glycolipids and enzymatically removes sialic acid. There are four types of neuraminidases, named as Neu1, Neu2, Neu3, and Neu4. Among them, Neu1 is the most abundant in mammals. Recent studies have revealed the involvement of Neu1 in several diseases, including cardiovascular diseases, diabetes, cancers, and neurological d

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3

Magesh, Sadagopan, Tohru Suzuki, Taeko Miyagi, Hideharu Ishida, and Makoto Kiso. "Homology modeling of human sialidase enzymes NEU1, NEU3 and NEU4 based on the crystal structure of NEU2: Hints for the design of selective NEU3 inhibitors." Journal of Molecular Graphics and Modelling 25, no. 2 (2006): 196–207. http://dx.doi.org/10.1016/j.jmgm.2005.12.006.

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4

Sodeoka, Mikiko, Go Hirai, Toru Watanabe, and Taeko Miyagi. "A strategy for constructing C-sialosides based on Ireland-Claisen rearrangement and its application for synthesis of CF2-linked ganglioside GM4 analog." Pure and Applied Chemistry 81, no. 2 (2009): 205–15. http://dx.doi.org/10.1351/pac-con-08-09-14.

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Sialidase-resistant ganglioside analogs having similar biological activities to natural gangliosides are expected to be important probes for clarifying the biological functions of gangliosides. Focusing on difluoromethylene-linked (CF2-linked) and methylene-linked (CH2-linked) α(2,3)sialylgalactose as a core structure of sialidase-resistant ganglioside mimics, we have developed novel, stereocontrolled, and efficient methodologies to synthesize C-sialosides based on Ireland-Claisen rearrangement. These methods were employed to synthesize CF2-linked GM4. The CF2-linked GM4 inhibited human sialid

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5

Yamaguchi, Kazunori, Keiko Hata, Koichi Koseki, et al. "Evidence for mitochondrial localization of a novel human sialidase (NEU4)." Biochemical Journal 390, no. 1 (2005): 85–93. http://dx.doi.org/10.1042/bj20050017.

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Based on the human cDNA sequence predicted to represent the NEU4 sialidase gene in public databases, a cDNA covering the entire coding sequence was isolated from human brain and expressed in mammalian cells. The cDNA encodes two isoforms: one possessing an N-terminal 12-amino-acid sequence that is predicted to be a mitochondrial targeting sequence, and the other lacking these amino acids. Expression of the isoforms is tissuespecific, as assessed by reverse transcription–PCR. Brain, muscle and kidney contained both isoforms; liver showed the highest expression, and the short form was predominan

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6

SEYRANTEPE, Volkan, and Murat DELMAN. "Characterization of the human sialidase Neu4 gene promoter." TURKISH JOURNAL OF BIOLOGY 38 (2014): 574–80. http://dx.doi.org/10.3906/biy-1401-63.

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7

Silvestri, I., F. Testa, R. Zappasodi, et al. "Sialidase NEU4 is involved in glioblastoma stem cell survival." Cell Death & Disease 5, no. 8 (2014): e1381-e1381. http://dx.doi.org/10.1038/cddis.2014.349.

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8

Comelli, Elena M., Margarida Amado, Sarah R. Lustig, and James C. Paulson. "Identification and expression of Neu4, a novel murine sialidase." Gene 321 (December 2003): 155–61. http://dx.doi.org/10.1016/j.gene.2003.08.005.

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9

Sundararaj, Kamala, Jessalyn I. Rodgers, Subathra Marimuthu, Leah J. Siskind, Evelyn Bruner, and Tamara K. Nowling. "Neuraminidase activity mediates IL-6 production by activated lupus-prone mesangial cells." American Journal of Physiology-Renal Physiology 314, no. 4 (2018): F630—F642. http://dx.doi.org/10.1152/ajprenal.00421.2017.

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The development of nephritis is a leading cause of morbidity and mortality in lupus patients. Although the general pathophysiological progression of lupus nephritis is known, the molecular mediators and mechanisms are incompletely understood. Previously, we demonstrated that the glycosphingolipid (GSL) catabolic pathway is elevated in the kidneys of MRL/lpr lupus mice and human lupus patients with nephritis. Specifically, the activity of neuraminidase (NEU) and expression of Neu1, an enzyme in the GSL catabolic pathway is significantly increased. To better understand the role and mechanisms by

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10

Albohy, Amgad, Yi Zhang, Victoria Smutova, Alexey V. Pshezhetsky, and Christopher W. Cairo. "Identification of Selective Nanomolar Inhibitors of the Human Neuraminidase, NEU4." ACS Medicinal Chemistry Letters 4, no. 6 (2013): 532–37. http://dx.doi.org/10.1021/ml400080t.

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