Relevant bibliographies by topics / Neuroserpin

Academic literature on the topic 'Neuroserpin'

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Published: 10 December 2022
Last updated: 10 March 2023

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Journal articles on the topic "Neuroserpin"

1

Galliciotti, Giovanna. "Neuroserpin." Frontiers in Bioscience 11, no. 1 (2006): 33. http://dx.doi.org/10.2741/1778.

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HILL, Rena M., Parmjeet K. PARMAR, Leigh C. COATES, Eva MEZEY, John F. PEARSON, and Nigel P. BIRCH. "Neuroserpin is expressed in the pituitary and adrenal glands and induces the extension of neurite-like processes in AtT-20 cells." Biochemical Journal 345, no. 3 (January 25, 2000): 595–601. http://dx.doi.org/10.1042/bj3450595.

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Two cDNAs encoding the serine protease inhibitor (serpin) neuroserpin were cloned from a rat pituitary cDNA library (rNS-1, 2922 bp; rNS-2, 1599 bp). In situ hybridization histochemistry showed neuroserpin transcripts in the intermediate, anterior and posterior lobes of the pituitary gland and medullary cells in the adrenal gland. Expression of rNS-1 mRNA was restricted to selected cells in the pituitary gland. Analysis of purified secretory-granule fractions from pituitary and adrenal tissues indicated that neuroserpin was found in dense-cored secretory granules. This result suggested that endocrine neuroserpin may regulate intragranular proteases or inhibit enzymes following regulated secretion. To investigate the function of neuroserpin in endocrine tissues we established stable anterior pituitary AtT-20 cell lines expressing neuroserpin. Cells with increased levels of neuroserpin responded by extending neurite-like processes. Extracellular proteolysis by serine protease plasminogen activators has been suggested to regulate neurite outgrowth. As neuroserpin inhibits tissue plasminogen activator (tPA) in vitro, we measured plasminogen-activator levels. Zymographic analysis indicated that AtT-20 cells synthesized and secreted a plasminogen activator identical in size to tPA. A higher-molecular-mass tPA-neuroserpin complex was also observed in AtT-20-cell conditioned culture medium. tPA levels were similar in parent AtT-20 cells and a stable cell line with increased levels of neuroserpin. There was no accumulation of a tPA-neuroserpin complex. Together these results identify endocrine cells as an important source of neuroserpin. Moreover they suggest that neuroserpin is released from dense-cored secretory granules to regulate cell-extracellular matrix interactions through a mechanism that may not directly involve tPA.
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Çinar, Rugül Köse. "Neuroserpin in Bipolar Disorder." Current Topics in Medicinal Chemistry 20, no. 7 (April 23, 2020): 518–23. http://dx.doi.org/10.2174/1568026620666200131125526.

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Objective: Neuroserpin is a serine protease inhibitor predominantly expressed in the nervous system functioning mainly in neuronal migration and axonal growth. Neuroprotective effects of neuroserpin were shown in animal models of stroke, brain, and spinal cord injury. Postmortem studies confirmed the involvement of neuroserpin in Alzheimer’s disease. Since altered adult neurogenesis was postulated as an aetiological mechanism for bipolar disorder, the possible effect of neuroserpin gene expression in the disorder was evaluated. Methods: Neuroserpin mRNA expression levels were examined in the peripheral blood of bipolar disorder type I manic and euthymic patients and healthy controls using the polymerase chain reaction method. The sample comprised of 60 physically healthy, middle-aged men as participants who had no substance use disorder. Results: The gene expression levels of neuroserpin were found lower in the bipolar disorder patients than the healthy controls (p=0.000). The neuroserpin levels did not differ between mania and euthymia (both 96% down-regulated compared to the controls). Conclusion: Since we detected differences between the patients and the controls, not the disease states, the dysregulation in the neuroserpin gene could be interpreted as a result of the disease itself.
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Kennedy, Sarah, Angela van Diepen, Cecilia van den Hurk, Leigh Coates, Tet Woo Lee, Lena Ostrovsky, Elena Miranda, et al. "Expression of the serine protease inhibitor neuroserpin in cells of the human myeloid lineage." Thrombosis and Haemostasis 97, no. 03 (2007): 394–99. http://dx.doi.org/10.1160/th06-09-0543.

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SummaryMyeloid progenitors in the bone marrow differentiate into most of the major cell types of the immune system, including macrophages and dendritic cells. These cells play important roles in both innate and adaptive immunity. They express a number of proteases and protease inhibitors including members of the serine proteinase inhibitor or serpin superfamily. In this study we report the differential expression of neuroserpin in cells of the human myeloid lineage. Neuroserpin was highly expressed and secreted following the differentiation of monocytes to macrophages and dendritic cells. Activation of dendritic cells with lipopolysaccharide resulted in increased neuroserpin mRNA levels but no neuroserpin secretion. Confocal immunofluorescence microscopy showed neuroserpin was differentially localised in human myeloid cells. In macrophages and dendritic cells it was concentrated in vesicles located in close proximity to the plasma membrane. The majority of activated dendritic cells also exhibited an intracellular focal concentration of neuroserpin which co-localised with the lysosomal/late endosomal marker LAMP-1. As neuroserpin inhibits tissue plasminogen activator, a comparative analysis of tPA and plasminogen activator inhibitor-1 (PAI-I) expression was undertaken. This analysis revealed differential expression of PAI-I and neuroserpin suggesting they may have different functions in human immune cells.
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Sobrino, Tomás, Elena Miranda, David Brea, Natalia Pérez de la Ossa, Miguel Blanco, Juan Pérez, Laura Dorado, et al. "The natural tissue plasminogen activator inhibitor neuroserpin and acute ischaemic stroke outcome." Thrombosis and Haemostasis 105, no. 03 (2011): 421–29. http://dx.doi.org/10.1160/th10-09-0621.

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SummaryNeuroserpin is a brain-derived natural inhibitor of tissue plasminogen activator (tPA) that has shown neuroprotective effects in animal models of brain ischaemia. Our aim was to investigate the association of neuroserpin levels in blood with functional outcome in patients with acute ischaemic stroke. Due to the potential effect of tPA treatment interfering on neuroserpin levels, we studied two different cohorts: 129 patients not treated with tPA and 80 patients treated with intravenous tPA within 3 hours (h) from symptoms onset. Neuroserpin levels were measured by ELISA. Good functional outcome at three months was defined as Rankin scale score ≤2. In the two cohorts, serum neuroserpin levels on admission were significantly higher than at 24 h, 72 h and in healthy subjects. In non tPA-treated patients, neuroserpin levels decrease at 24 h, but not levels at baseline, were associated with good outcome (for each quartile decrease, adjusted odds ratio [OR] 15.0; 95% confidence interval [CI], 3.5 to 66). In the tPA-treated cohort, high neuroserpin levels before tPA bolus had the stronger effect on favourable outcome (for each quartile, OR 13.5; 95%CI, 3.9 to 47). Furthermore, for each quartile in neuroserpin levels before tPA bolus there was a 80% (95%CI, 48 to 92) reduction in the probability of subsequent parenchymal haematoma. In summary, high serum neuroserpin levels before intravenous tPA and neuroserpin levels decrease at 24 h after ischaemic stroke, independently of tPA treatment, are associated with good functional outcome. These findings support the concept that neuroserpin might play an important role during cerebral ischaemia.
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de Groot, Dorien M., and Gerard J. M. Martens. "Expression of Neuroserpin Is Linked to Neuroendocrine Cell Activation." Endocrinology 146, no. 9 (September 1, 2005): 3791–99. http://dx.doi.org/10.1210/en.2005-0108.

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Abstract Inhibitors of serine proteases (serpins) are important regulators of intracellular and extracellular proteolytic pathways, and they function by forming an irreversible complex with their substrate. Neuroserpin represents a neuroendocrine-specific serpin family member that is expressed in brain regions displaying synaptic plasticity. In this study, we explored the biosynthesis of endogenous neuroserpin in a neuroendocrine model system, namely the melanotrope cells of Xenopus intermediate pituitary. The biosynthetic activity of these cells can be physiologically manipulated (high and low production of the prohormone proopiomelanocortin in black and white animals, respectively), resulting from a synaptic plasticity in innervating hypothalamic neurons. We found that neuroserpin was also differentially expressed in the Xenopus intermediate, but not anterior, pituitary with a 3-fold higher mRNA and more than 30-fold higher protein expression in the active vs. the inactive melanotrope cells. Two newly synthesized glycosylated forms of the neuroserpin protein (47 and 50 kDa) were produced and secreted by the active cells. Intriguingly, neuroserpin was found in an approximately 130-kDa sodium dodecyl sulfate-stable complex in the active, but not in the inactive, melanotrope cells, which correlated with the high and low proopiomelanocortin expression levels, respectively. In conclusion, we report on the biosynthesis of neuroserpin in a physiological context, and we find that the induction of neuroserpin expression and the formation of the 130-kDa neuroserpin-containing complex are linked to neuroendocrine cell activation.
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Yepes, Manuel, Maria Sandkvist, Mike K. K. Wong, Timothy A. Coleman, Elizabeth Smith, Stanley L. Cohan, and Daniel A. Lawrence. "Neuroserpin reduces cerebral infarct volume and protects neurons from ischemia-induced apoptosis." Blood 96, no. 2 (July 15, 2000): 569–76. http://dx.doi.org/10.1182/blood.v96.2.569.

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Abstract Neuroserpin, a recently identified inhibitor of tissue-type plasminogen activator (tPA), is primarily localized to neurons within the central nervous system, where it is thought to regulate tPA activity. In the present study neuroserpin expression and its potential therapeutic benefits were examined in a rat model of stroke. Neuroserpin expression increased in neurons surrounding the ischemic core (ischemic penumbra) within 6 hours of occlusion of the middle cerebral artery and remained elevated during the first week after the ischemic insult. Injection of neuroserpin directly into the brain immediately after infarct reduced stroke volume by 64% at 72 hours compared with control animals. In untreated animals both tPA and urokinase-type plasminogen activator (uPA) activity was significantly increased within the region of infarct by 6 hours after reperfusion. Activity of tPA then decreased to control levels by 72 hours, whereas uPA activity continued to rise and was dramatically increased by 72 hours. Both tPA and uPA activity were significantly reduced in neuroserpin-treated animals. Immunohistochemical staining of basement membrane laminin with a monoclonal antibody directed toward a cryptic epitope suggested that proteolysis of the basement membrane occurred as early as 10 minutes after reperfusion and that intracerebral administration of neuroserpin significantly reduced this proteolysis. Neuroserpin also decreased apoptotic cell counts in the ischemic penumbra by more than 50%. Thus, neuroserpin may be a naturally occurring neuroprotective proteinase inhibitor, whose therapeutic administration decreases stroke volume most likely by inhibiting proteinase activity and subsequent apoptosis associated with focal cerebral ischemia/reperfusion.
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Yepes, Manuel, Maria Sandkvist, Mike K. K. Wong, Timothy A. Coleman, Elizabeth Smith, Stanley L. Cohan, and Daniel A. Lawrence. "Neuroserpin reduces cerebral infarct volume and protects neurons from ischemia-induced apoptosis." Blood 96, no. 2 (July 15, 2000): 569–76. http://dx.doi.org/10.1182/blood.v96.2.569.014k35_569_576.

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Neuroserpin, a recently identified inhibitor of tissue-type plasminogen activator (tPA), is primarily localized to neurons within the central nervous system, where it is thought to regulate tPA activity. In the present study neuroserpin expression and its potential therapeutic benefits were examined in a rat model of stroke. Neuroserpin expression increased in neurons surrounding the ischemic core (ischemic penumbra) within 6 hours of occlusion of the middle cerebral artery and remained elevated during the first week after the ischemic insult. Injection of neuroserpin directly into the brain immediately after infarct reduced stroke volume by 64% at 72 hours compared with control animals. In untreated animals both tPA and urokinase-type plasminogen activator (uPA) activity was significantly increased within the region of infarct by 6 hours after reperfusion. Activity of tPA then decreased to control levels by 72 hours, whereas uPA activity continued to rise and was dramatically increased by 72 hours. Both tPA and uPA activity were significantly reduced in neuroserpin-treated animals. Immunohistochemical staining of basement membrane laminin with a monoclonal antibody directed toward a cryptic epitope suggested that proteolysis of the basement membrane occurred as early as 10 minutes after reperfusion and that intracerebral administration of neuroserpin significantly reduced this proteolysis. Neuroserpin also decreased apoptotic cell counts in the ischemic penumbra by more than 50%. Thus, neuroserpin may be a naturally occurring neuroprotective proteinase inhibitor, whose therapeutic administration decreases stroke volume most likely by inhibiting proteinase activity and subsequent apoptosis associated with focal cerebral ischemia/reperfusion.
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Yepes, Manuel, and Daniel Lawrence. "Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system." Thrombosis and Haemostasis 91, no. 03 (2004): 457–64. http://dx.doi.org/10.1160/th03-12-0766.

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SummaryNeuroserpin is a member of the serine proteinase inhibitor (serpin) gene family that reacts preferentially with tissue-type plasminogen activator (tPA) and is primarily localized to neurons in regions of the brain where tPA is also found. Outside of the central nervous system (CNS) tPA is predominantly found in the blood where its primary function is as a thrombolytic enzyme. However, tPA is also expressed within the CNS where it has a very different function, promoting events associated not only with synaptic plasticity but also with cell death in a number of settings, such as cerebral ischemia and seizures. Neuroserpin is released from neurons in response to neuronal depolarization and plays an important role in the development of synaptic plasticity. Following the onset of cerebral ischemia there is an increase in both tPA activity and neuroserpin expression in the area surrounding the necrotic core (ischemic penumbra), and treatment with neuroserpin following ischemic stroke or overexpression of the neuroserpin gene results in a significant decrease in the volume of the ischemic area as well as in the number of apoptotic cells. TPA activity and neuroserpin expression are also increased in specific areas of the brain by seizures, and treatment with neuroserpin slows the progression of seizure activity throughout the CNS and results in significant neuronal survival in the hippocampus. Mutations in human neuroserpin result in a form of autosomal dominant inherited dementia which is characterized by the presence of intraneuronal inclusion bodies and is known as Familial Encephalopathy with Neuroserpin Inclusion Bodies.
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Vezzani, Annamaria. "Tissue Plasminogen Activator, Neuroserpin, and Seizures." Epilepsy Currents 5, no. 4 (July 2005): 130–32. http://dx.doi.org/10.1111/j.1535-7511.2005.00041.x.

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Ethanol-withdrawal Seizures Are Controlled by Tissue Plasminogen Activator via Modulation of NR2B-containing NMDA Receptors Pawlak R, Melchor JP, Matys T, Skrzypiec AE, Strickland S Proc Natl Acad Sci USA 2005;102:443–448 Chronic ethanol abuse causes upregulation of N-methyl-D-aspartate (NMDA) receptors, which underlies seizures and brain damage on ethanol withdrawal (EW). Here we show that tissue plasminogen activator (tPA), a protease implicated in neuronal plasticity and seizures, is induced in the limbic system by chronic ethanol consumption, temporally coinciding with upregulation of NMDA receptors. tPA interacts with NR2B-containing NMDA receptors and is required for upregulation of the NR2B subunit in response to ethanol. As a consequence, tPA-deficient mice have reduced NR2B, extracellular signal-regulated kinase 1/2 phosphorylation, and seizures after EW. tPA-mediated facilitation of EW seizures is abolished by NR2B-specific NMDA antagonist ifenprodil. These results indicate that tPA mediates the development of physical dependence on ethanol by regulating NR2B-containing NMDA receptors. Neuroserpin Portland (Ser52Arg) Is Trapped as an Inactive Intermediate That Rapidly Forms Polymers: Implications for the Epilepsy Seen in the Dementia FENIB Belorgey D, Sharp LK, Crowther DC, Onda M, Johansson J, Lomas DA Eur J Biochem 2004;271:3360–3367 The dementia, familial encephalopathy with neuroserpin inclusion bodies (FENIB), is caused by point mutations in the neuroserpin gene. We have shown a correlation between the predicted effect of the mutation and the number of intracerebral inclusions, and an inverse relation with the age at onset of disease. Our previous work has shown that the intraneuronal inclusions in FENIB result from the sequential interaction between the reactive center loop of one neuroserpin molecule with β-sheet A of the next. We show here that neuroserpin Portland (Ser52Arg), which causes a severe form of FENIB, also forms loop-sheet polymers but at a faster rate, in keeping with the more severe clinical phenotype. The Portland mutant has a normal unfolding transition in urea and a normal melting temperature but is inactive as a proteinase inhibitor. This results in part from the reactive loop being in a less accessible conformation to bind to the target enzyme, tissue plasminogen activator. These results, with those of the CD analysis, are in keeping with the reactive center loop of neuroserpin Portland being partially inserted into β-sheet A to adopt a conformation similar to an intermediate on the polymerization pathway. Our data provide an explanation for the number of inclusions and the severity of dementia in FENIB associated with neuroserpin Portland. Moreover, the inactivity of the mutant may result in uncontrolled activity of tissue plasminogen activator, and so explain the epileptic seizures seen in individuals with more severe forms of the disease.
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Dissertations / Theses on the topic "Neuroserpin"

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Davies, Mark James. "The cytopathology of familial encephalopathy with neuroserpin inclusion bodies (FENIB)." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598334.

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Neuroserpin is a 55 kDa glycoprotein that is secreted from axons of the central and peripheral nervous system. Point mutations within the neuroserpin gene underlie the novel inclusion body dementia Familial Encephalopathy with the Neuroserpin Inclusion Bodies (FENIB).  These point mutations destabilise the molecule resulting in the formation of intracellular polymers by sequential insertion of the reactive centre loop of one molecule into β-sheet A of another. Here I postulate that endoplasmic reticulum (ER) inclusions of mutant serpins contribute to the molecular pathogenesis by directing a novel ER stress response. To assess this hypothesis I generated conditional PC-12 Tet-on cell lines expressing wild type neuroserpin, the Ser52Arg and Gly392Glu mutants that underlie FENIB and a novel-misfolding mutant (DeltaNS) predicted to stimulate the unfolded protein response (UPR). The mutants that cause FENIB accumulate within the ER as polymers that I can demonstrate by Western blot analysis and fluorescence confocal microscopy with novel monoclonal antibodies that detect the polymeric conformer of neuroserpin. Despite accumulating, the mutant neuroserpin does not elicit a UPR. However I demonstrate that the ER accumulation of mutant neuroserpin elicits an ER stress response resulting in activation of NF-κB, and this activation is calcium dependent.  Taken together, I have used the disease-related neuroserpin inclusions to define and characterise a novel ER derived signalling cascade involved in sensing protein accumulation within the ER.
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MacLeod, Ian. "A Drosophila model of familial encephalopathy with neuroserpin inclusion bodies." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611439.

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Schipanski, Angela [Verfasser], and Markus [Akademischer Betreuer] Glatzel. "Mechanism of neuronal death in familial encephalopathy with neuroserpin inclusion bodies (FENIB) : Implications for mutant neuroserpin degradation ; a study in mus musculus / Angela Schipanski. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2011. http://d-nb.info/1020458119/34.

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Sharp, Lynda Karen. "The biochemical characterisation of mutants of neuroserpin that cause the dementia FENIB." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614202.

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Kinghorn, Kerri Jane. "The role of neuroserpin and Aβ in the pathogenesis of Alzheimer's disease." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614058.

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Marik, Sergej [Verfasser], and Markus [Akademischer Betreuer] Glatzel. "Mannose-6-Phosphat abhängiger Transport von Neuroserpin / Sergej Marik. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2013. http://d-nb.info/1045024236/34.

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Takehara, Sayaka. "Studies on the mechanism for the formation of neuroserpin polymers causing dementia." Kyoto University, 2011. http://hdl.handle.net/2433/142314.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第16116号
農博第1852号
新制||農||988(附属図書館)
学位論文||H23||N4586(農学部図書室)
28695
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 三上 文三, 教授 植田 和光, 教授 植田 充美
学位規則第4条第1項該当
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Lai, Christine Chieh-Lin. "Molecular and cellular studies of Drosophila neuroserpin Spn4A and its polymer-forming mutants." Thesis, University of British Columbia, 2010. http://hdl.handle.net/2429/27742.

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Serpins (Serine Protease Inhibitors) are expressed by most organisms and perform a variety of functions. Most serpins inhibit proteases by undergoing a unique conformational change. They are clinically relevant in two ways. First, introduction of single amino acid point mutations transforms the serpins’ labile conformations into pathogenic, inactive polymers causing “serpinopathies”. In particular, human neuroserpin is a brain-specific serpin that, when mutated, causes a debilitating early onset dementia through unknown cellular pathways. Second, serpins are currently under investigation as therapeutic inhibitors of proprotein convertases (PCs). PCs are associated with some bacterial and viral infections as well as cancer. However, no comprehensive investigation into the cellular effects of PC inhibitor expression in mammalian cells has been performed. This thesis details the use of the Drosophila serpin, Spn4A, to address the cellular pathways mediated by serpin polymers or PC inhibition. Spn4A is a neuron-specific, secretory pathway serpin that inhibits Drosophila or human PCs. We hypothesized that Spn4A mutants, encoding homologous disease-causing mutations in human neuroserpin, would form pathogenic polymers and represent an ideal candidate for generating a cell-based and transgenic Drosophila serpinopathy model. Further, we hypothesized that we could evaluate the cellular response to PC inhibition and polymer accumulation by transcriptome profiling of H4 human neuroglioma cells expressing Spn4A wild-type and mutants. We established an expression system using Spn4A and its mutants in H4s. Subsequently, we used microarray analysis to simultaneously address how serpin polymers may induce cytotoxicity as well as the effects of proprotein processing inhibition in neuroglioma cells. We demonstrated that Spn4A mutants formed polymers, were retained in the endoplasmic reticulum, and lacked inhibitory function, but induced few changes on the transcriptome (under 20 genes differentially regulated). To this end, we have developed transgenic Drosophila overexpressing Spn4A variants to further investigate the biological impact of Spn4A mutants. Next, we analyzed the response to the PC inhibitor, Spn4A, and found marked changes in genes related to malignancy. Our genome-wide gene expression studies have provided novel insights into cellular changes in response to polymeric or PC-inhibiting serpins, and establish the foundation for future functional studies.
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Karlsson, Li Susanna Monika. "Structural characterisation of the conformational transitions of neuroserpin that underlie the dementia FENIB." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611426.

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Ingwersen, Thies Frieder [Verfasser]. "Using small chemical compounds to inhibit polymerization of neuroserpin in FENIB / Thies Frieder Ingwersen." Hamburg : Staats- und Universitätsbibliothek Hamburg Carl von Ossietzky, 2020. http://d-nb.info/122853778X/34.

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Book chapters on the topic "Neuroserpin"

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Davis, Richard L., and George H. Collins. "Familial Encephalopathy with Neuroserpin Inclusion Bodies." In Neurodegeneration: The Molecular Pathology of Dementia and Movement Disorders, 456–60. Oxford, UK: Wiley-Blackwell, 2011. http://dx.doi.org/10.1002/9781444341256.ch48.

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Yepes, Manuel, and Daniel A. Lawrence. "Neuroserpin in Neurological Disease." In Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity, 593–617. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812707543_0024.

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Lomas, David A. "α‎1-Antitrypsin deficiency and the serpinopathies." In Oxford Textbook of Medicine, edited by Timothy M. Cox, 2235–42. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0242.

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α‎1-Antitrypsin is an acute phase glycoprotein synthesized by the liver that functions as an inhibitor of a range of proteolytic enzymes, most importantly neutrophil elastase in the lung. Ninety-five per cent of severe plasma deficiency of α‎1-antitrypsin results from homozygosity for the Z allele (Glu342Lys), which causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes as periodic acid–Schiff-positive, diastase-resistant inclusions. Clinical features— all adults homozygous for the Z allele of α‎1-antitrypsin have a minor degree of portal fibrosis that is often subclinical, but up to 50% have clinically evident cirrhosis and occasionally hepatocellular carcinoma. They also develop panlobular emphysema that typically affects the lung bases and is greatly exacerbated by smoking. Cor pulmonale and polycythaemia are late features. Diagnosis and management—severe genetic deficiency of α‎1-antitrypsin is readily diagnosed by low plasma levels and the virtual absence of the α‎1-band on protein electrophoresis. Patients should abstain from smoking and avoid agents that cause hepatic injury, such as excessive alcohol and obesity. Emphysema is treated along conventional lines. α‎1-Antitrypsin replacement therapy is widely used in North America to slow the progression of the lung disease and has recently been licensed by the European Medicines Agency, but its clinical efficacy remains contentious and it has no effect on liver disease. Clinical trials are underway to ‘knock down’ the expression of mutant Z α‎1-antitrypsin within hepatocytes to try to prevent cirrhosis. Other serpinopathies—the polymerization that underlies α‎1-antitrypsin deficiency is found in other members of the serine protease inhibitor (or serpin) superfamily to cause diseases as diverse as thrombosis (antithrombin), angio-oedema (C1 inhibitor), and dementia (neuroserpin).
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Conference papers on the topic "Neuroserpin"

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Srikeerthana, Kuchi, and Patrick De Causmaecker. "Comparative sequence and structural analyses of neuroserpin." In the International Symposium. New York, New York, USA: ACM Press, 2010. http://dx.doi.org/10.1145/1722024.1722031.

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GHETTI, BERNARDINO, MASAKI TAKAO, MASAHIDE YAZAKI, MARTIN R. FARLOW, FREDERICK W. UNVERZAGT, PEDRO PICCARDO, JILL R. MURRELL, and MERRILL D. BENSON. "NEUROPATHOLOGY AT THE CROSSROADS OF NEUROPSYCHIATRY AND GENETICS: NEW INSIGHTS INTO NEUROSERPIN ENCEPHALOPATHY." In Proceedings of the International Seminar on Nuclear War and Planetary Emergencies — 27th Session. WORLD SCIENTIFIC, 2003. http://dx.doi.org/10.1142/9789812705150_0065.

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Ramnefjell, Maria, Lars Helgeland, and Lars A. Akslen. "Abstract 4329: Expression of serpin B2, neuroserpin and L1CAM in association with metastasis and survival in non-small cell lung cancer." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4329.

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