Bibliographies thématiques / Murine Neuroglobin

Littérature scientifique sur le sujet « Murine Neuroglobin »

Auteur : Grafiati
Publié le 10 mars 2023

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Articles de revues sur le sujet "Murine Neuroglobin"

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Mammen, Pradeep P. A., John M. Shelton, Sean C. Goetsch, S. Clay Williams, James A. Richardson, Mary G. Garry et Daniel J. Garry. « Neuroglobin, A Novel Member of the Globin Family, Is Expressed in Focal Regions of the Brain ». Journal of Histochemistry & ; Cytochemistry 50, no 12 (décembre 2002) : 1591–98. http://dx.doi.org/10.1177/002215540205001203.

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Hemoproteins are widely distributed among unicellular eukaryotes, plants, and animals. In addition to myoglobin and hemoglobin, a third hemoprotein, neuroglobin, has recently been isolated from vertebrate brain. Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity. In this study we utilized in situ hybridization (ISH) and RT-PCR analyses to examine the expression of neuroglobin in the normoxic and hypoxic murine brain. In the normoxic adult mouse, neuroglobin expression was observed in focal regions of the brain, including the lateral tegmental nuclei, the preoptic nucleus, amygdala, locus coeruleus, and nucleus of the solitary tract. Using ISH and RT-PCR techniques, no significant changes in neuroglobin expression in the adult murine brain was observed in response to chronic 10% oxygen. These results support the hypothesis that neuroglobin is a hemoprotein that is expressed in the brain and may have diverse functional roles.
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Schmidt, Marc, Tilmann Laufs, Stefan Reuss, Thomas Hankeln et Thorsten Burmester. « Divergent distribution of cytoglobin and neuroglobin in the murine eye ». Neuroscience Letters 374, no 3 (février 2005) : 207–11. http://dx.doi.org/10.1016/j.neulet.2004.10.071.

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Anselmi, Massimiliano, Maurizio Brunori, Beatrice Vallone et Alfredo Di Nola. « Molecular Dynamics Simulation of Deoxy and Carboxy Murine Neuroglobin in Water ». Biophysical Journal 93, no 2 (juillet 2007) : 434–41. http://dx.doi.org/10.1529/biophysj.106.099648.

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Vallone, Beatrice, Karin Nienhaus, Maurizio Brunori et G. Ulrich Nienhaus. « The structure of murine neuroglobin : Novel pathways for ligand migration and binding ». Proteins : Structure, Function, and Bioinformatics 56, no 1 (7 mai 2004) : 85–92. http://dx.doi.org/10.1002/prot.20113.

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Mejía, M. G. Enríquez, E. Segura Anaya, A. Martínez Gómez, D. Millán Aldaco, M. Palomero Rivero, D. Hinojosa Bobadilla, P. Ó. González Vargas et P. Vieyra Reyes. « Presence of neuroglobin in cerebral areas of a murine model of Parkinson's disease ». Journal of the Neurological Sciences 405 (octobre 2019) : 292–93. http://dx.doi.org/10.1016/j.jns.2019.10.1375.

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Ardiccioni, Chiara, Alessandro Arcovito, Stefano Della Longa, Peter van der Linden, Dominique Bourgeois, Martin Weik, Linda Celeste Montemiglio et al. « Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments ». IUCrJ 6, no 5 (10 juillet 2019) : 832–42. http://dx.doi.org/10.1107/s2052252519008157.

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A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV–visible microspectroscopy in crystallo, solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15–40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions.
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Nienhaus, Karin, Jan M. Kriegl et G. Ulrich Nienhaus. « Structural Dynamics in the Active Site of Murine Neuroglobin and Its Effects on Ligand Binding ». Journal of Biological Chemistry 279, no 22 (11 mars 2004) : 22944–52. http://dx.doi.org/10.1074/jbc.m401561200.

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De Simone, Giovanna, Diego Sbardella, Francesco Oddone, Alessandra Pesce, Massimo Coletta et Paolo Ascenzi. « Structural and (Pseudo-)Enzymatic Properties of Neuroglobin : Its Possible Role in Neuroprotection ». Cells 10, no 12 (30 novembre 2021) : 3366. http://dx.doi.org/10.3390/cells10123366.

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Neuroglobin (Ngb), the third member of the globin family, was discovered in human and murine brains in 2000. This monomeric globin is structurally similar to myoglobin (Mb) and hemoglobin (Hb) α and β subunits, but it hosts a bis-histidyl six-coordinated heme-Fe atom. Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell. The high Ngb levels (~100–200 μM) present in the retinal ganglion cell layer and in the optic nerve facilitate the O2 buffer and delivery. In contrast, the very low levels of Ngb (~1 μM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds. Here, structural and (pseudo-)enzymatic properties of Ngb, which are at the root of tissue and organ protection, are reviewed, envisaging a possible role in the protection from neuronal degeneration of the retina and the optic nerve.
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Milazzo, Lisa, Cécile Exertier, Maurizio Becucci, Ida Freda, Linda Celeste Montemiglio, Carmelinda Savino, Beatrice Vallone et Giulietta Smulevich. « Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy ». FEBS Journal 287, no 18 (27 février 2020) : 4082–97. http://dx.doi.org/10.1111/febs.15241.

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Yang, Yinshan, Frédéric Allemand, Ewelina Guca, Beatrice Vallone, Stephane Delbecq et Christian Roumestand. « 1H, 15N and 13C Backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide ». Biomolecular NMR Assignments 9, no 1 (16 mai 2014) : 153–56. http://dx.doi.org/10.1007/s12104-014-9563-1.

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Thèses sur le sujet "Murine Neuroglobin"

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Milazzo, Lisa. « How resonance Raman spectroscopy can give valuable insights into diverse aspects of heme protein structure and function ». Doctoral thesis, 2019. http://hdl.handle.net/2158/1154362.

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Resonance Raman (RR) spectroscopy complemented by UV-Vis absorption spectroscopy is a very powerful technique to investigate the structure-function relationships of heme proteins, a widely distributed and biological relevant class of proteins which can play different biological functions. Since the protein activity is tightly linked to the structure of the heme active site, my study has been devoted to the investigation of several heme proteins involved in important biological processes, to obtain a comprehensive spectroscopic signature, with the aim to highlight the relationship between the heme pocket architecture and the protein function. The studies were carried out on native proteins and selected site-directed mutants, at both room (298 K) and low (80 K) temperature, at various pH, and in presence of various exogenous ligands, spanning the excitation wavelengths from UV to the visible region.
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Livres sur le sujet "Murine Neuroglobin"

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MARROQUÍN-DE JESÚS, Ángel, Juan Manuel OLIVARES-RAMÍREZ, Marisela CRUZ-RAMÍREZ et Luis Eduardo CRUZ-CARPIO. CIERMMI Women in Science Medicine and Health Sciences Handbooks T-XIII. ECORFAN-Mexico, S.C., 2021. http://dx.doi.org/10.35429/h.2021.13.1.130.

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As the first chapter, Terán, Cisneros and Gutiérrez present Knowledge of health personnel about HPV screening tests: a systematic review, as second chapter, González, Meraz, Chávez and González will discuss Health Risk Behaviors and Emotional State of Medical Students as third chapter, Aguilar, Morado, Villada and Tovar present Early trauma as conditioning of psychopathology in adult women, as fourth chapter, Torre, Therio, Carrillo and Mendoza propose Growth and development of the craniofacial region and the stomatognathic apparatus, as the fifth chapter, Villarreal, Enriquez, Hernández and Medina, perform Assessment of physical activity, sedentary behaviors and physical fitness in perimenopausal women, as the sixth chapter, Díaz, González, Uvalle and Mederos develop Pro-Inflammatory cytokines: Leptin and visfatin associated to obesity in young university students, as seventh chapter, Enríquez, Vieyra, Ramos and Trujillo, will discuss Presence of neuroglobin in the substantia nigra in a murine model of parkinson's disease: an immunohistochemical study, in eighth chapter, Martínez, Tavizon, Carlos and Mauricio present Prevalence of ectopic eruption and intercanine distance in children aged 6 to 12 years. Cycle 2019-2020, as the ninth chapter, Caceres, Zárate, Flores and Bustillos, performed Anxiety in medical students, during a COVID-19 pandemic and as the last chapter, González, Hernández, Martínez and González, focus on Overwiev of general plant toxicology uses and adverse effects.
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Chapitres de livres sur le sujet "Murine Neuroglobin"

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ENRÍQUEZ-MEJIA, María Guadalupe, Patricia VIEYRA-REYES, Diana Carolina RAMOS-BERUMEN et Virgilio Eduardo TRUJILLO-CONDES. « Presence of neuroglobin in the substantia nigra in a murine model of Parkinson's disease : an immunohistochemical study ». Dans CIERMMI Women in Science Medicine and Health Sciences Handbooks T-XIII, 89–99. ECORFAN-Mexico, S.C., 2021. http://dx.doi.org/10.35429/h.2021.13.89.99.

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Neuroglobin (NGB) is a protein with antioxidant and antiapoptotic activity against conditions such as oxidative stress, oxygen / glucose deprivation and neuronal apoptosis. Its presence has been documented in different brain areas including the midbrain, a site of key importance for global motor control by the presence of dopaminergic neurons in the substantia nigra located inside and whose progressive loss culminates in the most common neurodegenerative movement disorder, Parkinson's disease (PD). PD is a condition characterized by motor disturbances such as resting tremor, muscle rigidity, bradykinesia and deterioration gait and balance. There are few studies that inquire about the role of this protein in this disease, including its expression in the substantia nigra. The present study evaluated the presence of NGB in a murine model of PD induced by 6-OHDA injury using immunohistochemistry. The results show a significant difference of NGB aggregates in the substantia nigra in compared to controls (p=0.003) These findings provide the first in vivo experimental evidence of an adaptive NGB response in a model of PD, supporting its probable neuroprotective action in the main area involved in the pathophysiology of this disease.
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