Relevant bibliographies by topics / Ly6/uPAR proteins

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Academic literature on the topic 'Ly6/uPAR proteins'

Author: Grafiati
Published: 5 June 2025
Last updated: 2 August 2025

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Journal articles on the topic "Ly6/uPAR proteins"

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Yu, Murthy, and Liu. "Relating GPI-Anchored Ly6 Proteins uPAR and CD59 to Viral Infection." Viruses 11, no. 11 (2019): 1060. http://dx.doi.org/10.3390/v11111060.

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The Ly6 (lymphocyte antigen-6)/uPAR (urokinase-type plasminogen activator receptor) superfamily protein is a group of molecules that share limited sequence homology but conserved three-fingered structures. Despite diverse cellular functions, such as in regulating host immunity, cell adhesion, and migration, the physiological roles of these factors in vivo remain poorly characterized. Notably, increasing research has focused on the interplays between Ly6/uPAR proteins and viral pathogens, the results of which have provided new insight into viral entry and virus–host interactions. While LY6E (ly
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Zaigraev, Maxim M., Ekaterina N. Lyukmanova, Alexander S. Paramonov, Zakhar O. Shenkarev, and Anton O. Chugunov. "Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins." International Journal of Molecular Sciences 24, no. 1 (2022): 11. http://dx.doi.org/10.3390/ijms24010011.

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Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single β-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide part
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Bychkov, M. L., A. V. Kirichenko, A. S. Paramonov, M. P. Kirpichnikov та E. N. Lukmanova. "ACCUMULATION OF β-AMYLOID LEADS TO A DECREASE IN LYNX1 AND LYPD6B EXPRESSION IN THE HIPPOCAMPUS AND INCREASED EXPRESSION OF PRO-INFLAMMATORY CYTOKINES IN THE HIPPOCAMPUS AND BLOOD SERUM". Доклады Российской академии наук. Науки о жизни 511, № 1 (2023): 354–59. http://dx.doi.org/10.31857/s2686738922600881.

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Alzheimer’s disease is a rapidly progressive neurodegenerative disease, the development of which is associated with the accumulation of β-amyloid oligomers, dysfunction of the α7-nAChR nicotinic acetylcholine receptor, and activation of inflammation. Previously, we have shown that the neuromodulator Lynx1, which belongs to the Ly6/uPAR family, competes with β-amyloid(1–42) for binding to α7-nAChR. In the present work, we studied the expression and localization of Ly6/uPAR family proteins in the hippocampus of 2xTg-AD transgenic mice that model AD and demonstrate increased amyloidosis in the br
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Bychkov, Maxim L., Aizek B. Isaev, Alexander A. Andreev-Andrievskiy та ін. "Aβ1-42 Accumulation Accompanies Changed Expression of Ly6/uPAR Proteins, Dysregulation of the Cholinergic System, and Degeneration of Astrocytes in the Cerebellum of Mouse Model of Early Alzheimer Disease". International Journal of Molecular Sciences 24, № 19 (2023): 14852. http://dx.doi.org/10.3390/ijms241914852.

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Alzheimer disease (AD) is a widespread neurodegenerative disease characterized by the accumulation of oligomeric toxic forms of β-amyloid (Aβ1-42) and dysfunction of the cholinergic system in the different brain regions. However, the exact mechanisms of AD pathogenesis and the role of the nicotinic acetylcholine receptors (nAChRs) in the disease progression remain unclear. Here, we revealed a decreased expression of a number of the Ly6/uPAR proteins targeting nAChRs in the cerebellum of 2xTg-AD mice (model of early AD) in comparison with non-transgenic mice both at mRNA and protein levels. We
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Leth, Julie Maja, Katrine Zinck Leth-Espensen, Kristian Kølby Kristensen, et al. "Evolution and Medical Significance of LU Domain−Containing Proteins." International Journal of Molecular Sciences 20, no. 11 (2019): 2760. http://dx.doi.org/10.3390/ijms20112760.

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Proteins containing Ly6/uPAR (LU) domains exhibit very diverse biological functions and have broad taxonomic distributions in eukaryotes. In general, they adopt a characteristic three-fingered folding topology with three long loops projecting from a disulfide-rich globular core. The majority of the members of this protein domain family contain only a single LU domain, which can be secreted, glycolipid anchored, or constitute the extracellular ligand binding domain of type-I membrane proteins. Nonetheless, a few proteins contain multiple LU domains, for example, the urokinase receptor uPAR, C4.
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Vasilyeva, N. A., E. V. Loktyushov, M. L. Bychkov, Z. O. Shenkarev, and E. N. Lyukmanova. "Three-finger proteins from the Ly6/uPAR family: Functional diversity within one structural motif." Biochemistry (Moscow) 82, no. 13 (2017): 1702–15. http://dx.doi.org/10.1134/s0006297917130090.

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Kriegbaum, Mette C., Ole P. F. Clausen, Ole D. Lærum, and Michael Ploug. "Expression of the Ly6/uPAR-Domain Proteins C4.4A and Haldisin in Non-Invasive and Invasive Skin Lesions." Journal of Histochemistry & Cytochemistry 63, no. 2 (2014): 142–54. http://dx.doi.org/10.1369/0022155414563107.

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8

Shulepko, M. A., E. N. Lyukmanova, Z. O. Shenkarev, et al. "Towards universal approach for bacterial production of three-finger Ly6/uPAR proteins: Case study of cytotoxin I from cobra N. oxiana." Protein Expression and Purification 130 (February 2017): 13–20. http://dx.doi.org/10.1016/j.pep.2016.09.021.

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9

Lyukmanova, Ekaterina N., Maxim L. Bychkov, Andrei M. Chernikov, et al. "In Search of the Role of Three-Finger Starfish Proteins." Marine Drugs 22, no. 11 (2024): 488. http://dx.doi.org/10.3390/md22110488.

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Three-finger proteins (TFPs), or Ly6/uPAR proteins, are characterized by the beta-structural LU domain containing three protruding “fingers” and stabilized by four conserved disulfide bonds. TFPs were initially characterized as snake alpha-neurotoxins, but later many studies showed their regulatory roles in different organisms. Despite a known expression of TFPs in vertebrates, they are poorly studied in other taxa. The presence of TFPs in starfish was previously shown, but their targets and functional role still remain unknown. Here, we analyzed expression, target, and possible function of th
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Shelukhina, Irina, Andrei Siniavin, Igor Kasheverov, Lucy Ojomoko, Victor Tsetlin та Yuri Utkin. "α7- and α9-Containing Nicotinic Acetylcholine Receptors in the Functioning of Immune System and in Pain". International Journal of Molecular Sciences 24, № 7 (2023): 6524. http://dx.doi.org/10.3390/ijms24076524.

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Nicotinic acetylcholine receptors (nAChRs) present as many different subtypes in the nervous and immune systems, muscles and on the cells of other organs. In the immune system, inflammation is regulated via the vagus nerve through the activation of the non-neuronal α7 nAChR subtype, affecting the production of cytokines. The analgesic properties of α7 nAChR-selective compounds are mostly based on the activation of the cholinergic anti-inflammatory pathway. The molecular mechanism of neuropathic pain relief mediated by the inhibition of α9-containing nAChRs is not fully understood yet, but the
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Book chapters on the topic "Ly6/uPAR proteins"

1

Lalezari, Parviz, and Behnaz Bayat. "Neutrophil-Specific Antigens: Immunobiology, Genetics and Roles in Clinical Disorders." In Blood Groups - More Than Inheritance of Antigenic Substances [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102431.

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Neutrophils are the most abundant nucleated cells in blood circulation and play important roles in the innate and adaptive immune responses. Neutrophil-specific antigens, only expressed on neutrophils, are glycoproteins originally identified in studies on neonatal neutropenia due to fetal-maternal incompatibility and autoimmune neutropenia of infancy. The most investigated neutrophil–specific antigens are the NA and NB antigens that their incompatibilities also cause transfusion-induced febrile reactions and acute lung injury, a potentially fatal reaction, and in bone marrow transplantation, c
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