Gotowe bibliografie tematyczne / Myelin protein zero

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Gotowa bibliografia na temat „Myelin protein zero”

Autor: Grafiati

Data publikacji: 2 czerwca 2025

Data aktualizacji: 31 lipca 2025

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Artykuły w czasopismach na temat "Myelin protein zero"

Choe, Senyon. "Packing of Myelin Protein Zero." Neuron 17, no. 3 (1996): 363–65. http://dx.doi.org/10.1016/s0896-6273(00)80167-1.

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Raasakka, Arne, and Petri Kursula. "How Does Protein Zero Assemble Compact Myelin?" Cells 9, no. 8 (2020): 1832. http://dx.doi.org/10.3390/cells9081832.

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Myelin protein zero (P0), a type I transmembrane protein, is the most abundant protein in peripheral nervous system (PNS) myelin—the lipid-rich, periodic structure of membrane pairs that concentrically encloses long axonal segments. Schwann cells, the myelinating glia of the PNS, express P0 throughout their development until the formation of mature myelin. In the intramyelinic compartment, the immunoglobulin-like domain of P0 bridges apposing membranes via homophilic adhesion, forming, as revealed by electron microscopy, the electron-dense, double “intraperiod line” that is split by a narrow,

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Spiryda, Lisa. "Myelin protein zero and membrane adhesion." Journal of Neuroscience Research 54, no. 2 (1998): 137–46. http://dx.doi.org/10.1002/(sici)1097-4547(19981015)54:2<137::aid-jnr2>3.0.co;2-f.

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Raasakka, Arne, Oda C. Krokengen, Robert Schneider, and Petri Kursula. "Myelin protein zero - the structural foundation behind peripheral compact myelin." Biophysical Journal 122, no. 3 (2023): 500a. http://dx.doi.org/10.1016/j.bpj.2022.11.2669.

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Fernandez-Valle, C., N. Fregien, P. M. Wood, and M. B. Bunge. "Expression of the protein zero myelin gene in axon-related Schwann cells is linked to basal lamina formation." Development 119, no. 3 (1993): 867–80. http://dx.doi.org/10.1242/dev.119.3.867.

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A Schwann cell has the potential to differentiate into either a myelinating or ensheathing cell depending upon signals received from the axon that it contacts. Studies focusing on the pathway leading to myelination demonstrated that Schwann cells must form a basal lamina in order to myelinate an axon. In this report, we describe studies that indicate that initiation of basal lamina synthesis is required for Schwann cells to distinguish between myelination-inducing axons and axons that do not induce myelination, and to respond by undergoing the appropriate genetic and cellular changes. We have

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Warner, Laura E., Benjamin B. Roa, and James R. Lupski. "Settling the myelin protein zero question in CMT1B." Nature Genetics 11, no. 2 (1995): 119–20. http://dx.doi.org/10.1038/ng1095-119.

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D’Urso, Donatella, Peter Ehrhardt, and Hans Werner Müller. "Peripheral Myelin Protein 22 and Protein Zero: a Novel Association in Peripheral Nervous System Myelin." Journal of Neuroscience 19, no. 9 (1999): 3396–403. http://dx.doi.org/10.1523/jneurosci.19-09-03396.1999.

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Gould, Robert M., Todd Oakley, Jared V. Goldstone, Jason C. Dugas, Scott T. Brady, and Alexander Gow. "Myelin sheaths are formed with proteins that originated in vertebrate lineages." Neuron Glia Biology 4, no. 2 (2008): 137–52. http://dx.doi.org/10.1017/s1740925x09990238.

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All vertebrate nervous systems, except those of agnathans, make extensive use of the myelinated fiber, a structure formed by coordinated interplay between neuronal axons and glial cells. Myelinated fibers, by enhancing the speed and efficiency of nerve cell communication allowed gnathostomes to evolve extensively, forming a broad range of diverse lifestyles in most habitable environments. The axon-covering myelin sheaths are structurally and biochemically novel as they contain high portions of lipid and a few prominent low molecular weight proteins often considered unique to myelin. Here we se

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Peirano, Reto I., Derk E. Goerich, Dieter Riethmacher, and Michael Wegner. "Protein Zero Gene Expression Is Regulated by the Glial Transcription Factor Sox10." Molecular and Cellular Biology 20, no. 9 (2000): 3198–209. http://dx.doi.org/10.1128/mcb.20.9.3198-3209.2000.

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ABSTRACT Myelinating glia express high levels of a unique set of genes which code for structural proteins of the myelin sheath. Few transcription factors have so far been implicated in the regulation of any myelin gene. Here we show that the protein zero (P0) gene, a myelin gene exclusively expressed in the Schwann cell lineage of the peripheral nervous system, is controlled in its expression by the high-mobility-group domain protein Sox10 both in tissue culture and in vivo. Induction of wild-type Sox10, but not of other transcription factors or Sox10 mutants, strongly increased endogenous P0e

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Georgiou, John, and Milton P. Charlton. "Non-myelin-forming perisynaptic Schwann cells express protein zero and myelin-associated glycoprotein." Glia 27, no. 2 (1999): 101–9. http://dx.doi.org/10.1002/(sici)1098-1136(199908)27:2<101::aid-glia1>3.0.co;2-h.

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Rozprawy doktorskie na temat "Myelin protein zero"

Shames, Igor. "Phenotypic differences between Peripheral Myelin Protein-22 (PMP-22) and Protein Zero (PO) mutations associated with Charcot-Marie-Tooth related diseases." Thesis, McGill University, 2002. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=79122.

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Many hereditary peripheral neuropathies are characterized by abnormal myelination in peripheral nerves. Two structural myelin proteins, PMP22, a polytopic myelin protein, and P0, an Ig-like transmembrane protein, play a major role in myelin formation. A large number of mutations have been identified in P0 and PMP22 genes. Neuropathies associated with PMP22 and P0 mutations have varying severities suggesting their effects are pleiotropic. It is of great importance to explore molecular pathogenesis of mutated P0 and PMP22 proteins in order to understand the basic process of myelination an

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PFEND, GILLES. "Etude du transport de la proteine zero de la myeline (po) et de certaines formes tronquees dans des cellules gliales en culture." Université Louis Pasteur (Strasbourg) (1971-2008), 2000. http://www.theses.fr/2000STR13106.

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La proteine p0 de la myeline appartient a la famille des immunoglobulines et est impliquee dans les processus de reconnaissance intercellulaire et de compaction de la myeline. Cette glycoproteine membranaire est synthetisee par les cellules de schwann et represente pres de 50% des proteines du systeme nerveux peripherique. Des mutations du domaine extracellulaire de p0 entrainent l'apparition de neuropathies peripheriques. Dans le but de correler ces mutations avec un probleme de transport intracellulaire de la proteine p0 mutee, nous avons etudie le triage cellulaire de p0 dont le domaine ext

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Części książek na temat "Myelin protein zero"

Kamholz, John A., Michelle Brucal, Jun Li, and Michael Shy. "Myelin Protein Zero and CMT1B: A Tale of Two Phenotypes." In Molecular Neurology. Elsevier, 2007. http://dx.doi.org/10.1016/b978-012369509-3.50031-7.

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Filbin, Marie T., Donatella D'Urso, Keija Zhang, Manhar Wong, Joseph P. Doyle, and David R. Colman. "Protein Zero of Peripheral Nerve Myelin: Adhesion Properties and Functional Models." In Advances in Molecular and Cell Biology. Elsevier, 1996. http://dx.doi.org/10.1016/s1569-2558(08)60066-1.

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Baraitser, Michael. "The neuropathies." In The Genetics of Neurological Disorders. Oxford University PressNew York, NY, 1997. http://dx.doi.org/10.1093/oso/9780192628145.003.0021.

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Abstract HMSN type I—refers to those families with markedly slow conduction velocities: (a) those linked to 17p (mostly duplications) and those with mutations at the PMP 22 gene on 17p; those linked to chromosome 1 (the myelin protein zero gene); HMSN type II—the axonal type with only moderately slowed conduction; HMSN type III—(a) classic Dejerine-Sottas disease with onion bulb formation; (b) with amyelination; (c) with basal lamina onion bulb formation; HMSN type IV—Refsum’s disease; HMSN type V—with spasticity; HMSN type VI—with optic atrophy/deafness; HMSN X-linked.

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Streszczenia konferencji na temat "Myelin protein zero"

Kender, Z., J. Morgenstern, L. Alvarez Ramos, et al. "Circulating messenger RNA of the protein Myelin Protein Zero as a non-invasive marker for sensory loss of the upper extremity in patients with type 2 diabetes." In Diabetes Kongress 2021 – 55. Jahrestagung der DDG. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1727460.

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