keyword
MENU ▼
Read by QxMD icon Read
search

misfolding

keyword
https://www.readbyqxmd.com/read/28740603/an-atr-ftir-sensor-unraveling-the-drug-intervention-of-methylene-blue-congo-red-and-berberine-on-human-tau-and-a%C3%AE
#1
Jonas Schartner, Andreas Nabers, Brian Budde, Julia Lange, Nina Hoeck, Jens Wiltfang, Carsten Kötting, Klaus Gerwert
Alzheimer's disease affects millions of human beings worldwide. The disease progression is characterized by the formation of plaques and neurofibrillary tangles in the brain, which are based on aggregation processes of the Aβ peptide and tau protein. Today there is no cure and even no in vitro assay available for the identification of drug candidates, which provides direct information concerning the protein secondary structure label-free. Therefore, we developed an attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) sensor, which uses surface bound antibodies to immobilize a desired target protein...
July 13, 2017: ACS Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/28739800/cell-free-production-of-a-functional-oligomeric-form-of-a-chlamydia-major-outer-membrane-protein-momp-for-vaccine-development
#2
Wei He, Martina Felderman, Angela C Evans, Jia Geng, David Homan, Feliza Bourguet, Nicholas O Fischer, Yuanpei Li, Kit S Lam, Aleksandr Noy, Li Xing, R Holland Cheng, Amy Rasley, Craig D Blanchette, Kurt Kamrud, Nathanial Wang, Heather Gouvis, Todd C Peterson, Bolyn Hubby, Matthew A Coleman
Chlamydia is a prevalent sexually transmitted disease that infects more than 100 million people worldwide. Although most individuals infected with Chlamydia trachomatis are initially asymptomatic, symptoms can arise if left undiagnosed. Long-term infection can result in debilitating conditions such as pelvic inflammatory disease, infertility, and blindness. Chlamydia infection, therefore, constitutes a significant public health threat, underscoring the need for a Chlamydia-specific vaccine. Chlamydia strains express a major outer-membrane protein (MOMP) that has been shown to be an effective vaccine antigen...
July 24, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28739313/cardiac-amyloidosis-an-update-on-pathophysiology-diagnosis-and-treatment
#3
REVIEW
Omar K Siddiqi, Frederick L Ruberg
The amyloidoses are a group of systemic diseases characterized by organ deposition of misfolded protein fragments of diverse origins. The natural history of the disease, involvement of other organs, and treatment options vary significantly based on the protein of origin. In AL amyloidosis, amyloid protein is derived from immunoglobulin light chains, and most often involves the kidneys and the heart. ATTR amyloidosis is categorized as mutant or wild-type depending on the genetic sequence of the transthyretin (TTR) protein produced by the liver...
July 13, 2017: Trends in Cardiovascular Medicine
https://www.readbyqxmd.com/read/28737514/bag3-plays-a-central-role-in-proteostasis-in-the-heart
#4
Wataru Mizushima, Junichi Sadoshima
Proteinopathies are characterized by the accumulation of misfolded proteins, which ultimately interfere with normal cell function. While neurological diseases, such as Huntington disease and Alzheimer disease, are well-characterized proteinopathies, cardiac diseases have recently been associated with alterations in proteostasis. In this issue of the JCI, Fang and colleagues demonstrate that mice with cardiac-specific deficiency of the co-chaperone protein BCL2-associated athanogene 3 (BAG3) develop dilated cardiomyopathy that is associated with a destabilization of small HSPs as the result of a disrupted interaction between BAG3 and HSP70...
July 24, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/28736891/heat-induced-native-dimerization-prevents-amyloid-formation-by-variable-domain-from-immunoglobulin-light-chain-rei
#5
Marina Nawata, Hirotaka Tsutsumi, Yuta Kobayashi, Satoru Unzai, Shouhei Mine, Tsutomu Nakamura, Koichi Uegaki, Hironari Kamikubo, Mikio Kataoka, Daizo Hamada
Amyloid light chain (AL) amyloidosis is a protein-misfolding disease characterized by accumulation of immunoglobulin light chains (LCs) into amyloid fibrils. Dimerization of full length or variable domain (VL ) of LC serves to stabilize the native state and prevent the formation of amyloid fibrils. We here analyzed the thermodynamic properties of dimerization and unfolding reactions by nonamyloidogenic VL from REI LC or its monomeric Y96K mutant using sedimentation velocity and circular dichroism. The data indicate that the equilibrium shifts to native dimerization for wild type REI VL by elevating temperature due to the negative enthalpy change for dimer dissociation (-81...
July 24, 2017: FEBS Journal
https://www.readbyqxmd.com/read/28733641/influence-of-c-terminal-truncation-of-murine-serum-amyloid-a-on-fibril-structure
#6
Matthies Rennegarbe, Inga Lenter, Angelika Schierhorn, Romy Sawilla, Christian Haupt
Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist mainly of C-terminally truncated SAA fragments, termed AA proteins. For yet unknown reasons, phenotypic variations in the AA amyloid distribution pattern are clearly associated with specific AA proteins. Here we describe a bacterial expression system and chromatographic strategies to obtain significant amounts of C-terminally truncated fragments of murine SAA1...
July 21, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28733623/crystal-structure-of-a-low-molecular-weight-activator-blm-pep-with-yeast-20s-proteasome-insights-into-the-enzyme-activation-mechanism
#7
Julia Witkowska, Małgorzata Giżyńska, Przemysław Grudnik, Przemysław Golik, Przemysław Karpowicz, Artur Giełdoń, Grzegorz Dubin, Elżbieta Jankowska
Proteasomes are responsible for protein turnover in eukaryotic cells, degrading short-lived species but also removing improperly folded or oxidatively damaged ones. Dysfunction of a proteasome results in gradual accumulation of misfolded/damaged proteins, leading to their aggregation. It has been postulated that proteasome activators may facilitate removal of such aggregation-prone proteins and thus prevent development of neurodegenerative disorders. However, the discovery of pharmacologically relevant compounds is hindered by insufficient structural understanding of the activation process...
July 21, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28733489/interaction-of-misfolded-proteins-and-mitochondria-in-neurodegenerative-disorders
#8
REVIEW
Andrey Y Abramov, Alexey V Berezhnov, Evgeniya I Fedotova, Valery P Zinchenko, Ludmila P Dolgacheva
The number of the people affected by neurodegenerative disorders is growing dramatically due to the ageing of population. The major neurodegenerative diseases share some common pathological features including the involvement of mitochondria in the mechanism of pathology and misfolding and the accumulation of abnormally aggregated proteins. Neurotoxicity of aggregated β-amyloid, tau, α-synuclein and huntingtin is linked to the effects of these proteins on mitochondria. All these misfolded aggregates affect mitochondrial energy metabolism by inhibiting diverse mitochondrial complexes and limit ATP availability in neurones...
July 21, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28733196/proteasome-subunit-beta-type-1-p11a-polymorphism-is-a-new-prognostic-marker-in-multiple-myeloma
#9
Gergely Varga, Gábor Mikala, Katalin Piroska Kiss, Éva Kosóczki, Edit Szabó, Nóra Meggyesi, Katalin Balassa, Petra Kövy, Bálint Tegze, Gergely Szombath, Attila Tordai, Hajnalka Andrikovics, László Homolya, Tamás Masszi
BACKGROUND: Proteasome subunit beta type 1 (PSMB1) rs12717 polymorphism, a single nucleotide polymorphism with unknown functional effect, was recently reported to influence response to bortezomib-based therapy in follicular lymphoma. PATIENTS AND METHODS: We retrospectively analyzed the prognostic impact of this polymorphism in 211 consecutively diagnosed multiple myeloma cases, and performed in vitro experiments to look into its functional consequences. RESULTS: On univariate analysis, patients carrying the variant G allele showed significantly shorter progression-free survival (PFS) with a pattern suggestive of a gene-dose effect (PFS 26...
June 30, 2017: Clinical Lymphoma, Myeloma & Leukemia
https://www.readbyqxmd.com/read/28731447/chromatin-bound-oxidized-%C3%AE-synuclein-causes-strand-breaks-in-neuronal-genomes-in-in-vitro-models-of-parkinson-s-disease
#10
Velmarini Vasquez, Joy Mitra, Pavana M Hegde, Arvind Pandey, Shiladitya Sengupta, Sankar Mitra, K S Rao, Muralidhar L Hegde
Alpha-synuclein (α-Syn) overexpression and misfolding/aggregation in degenerating dopaminergic neurons have long been implicated in Parkinson's disease (PD). The neurotoxicity of α-Syn is enhanced by iron (Fe) and other pro-oxidant metals, leading to generation of reactive oxygen species in PD brain. Although α-Syn is predominantly localized in presynaptic nerve terminals, a small fraction exists in neuronal nuclei. However, the functional and/or pathological role of nuclear α-Syn is unclear. Following up on our earlier report that α-Syn directly binds DNA in vitro, here we confirm the nuclear localization and chromatin association of α-Syn in neurons using proximity ligation and chromatin immunoprecipitation analysis...
July 17, 2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28731040/er-stress-and-the-unfolded-protein-response-in-neurodegeneration
#11
REVIEW
Claudio Hetz, Smita Saxena
The clinical manifestation of neurodegenerative diseases is initiated by the selective alteration in the functionality of distinct neuronal populations. The pathology of many neurodegenerative diseases includes accumulation of misfolded proteins in the brain. In physiological conditions, the proteostasis network maintains normal protein folding, trafficking and degradation; alterations in this network - particularly disturbances to the function of endoplasmic reticulum (ER) - are thought to contribute to abnormal protein aggregation...
July 21, 2017: Nature Reviews. Neurology
https://www.readbyqxmd.com/read/28729486/comment-on-the-4fe4s-cluster-of-human-dna-primase-functions-as-a-redox-switch-using-dna-charge-transport
#12
Luca Pellegrini
O'Brien et al (Research Article, 24 February 2017, eaag1789) report that the iron-sulfur cluster of primase has a redox role in enzyme activity. Their analysis is based on a partially misfolded structure of the iron-sulfur cluster domain of primase. In the correctly folded structure, two of the three tyrosines putatively involved in electron transfer, Y345 and Y347, contact the RNA/DNA helix, providing an alternative explanation for the data of O'Brien et al.
July 21, 2017: Science
https://www.readbyqxmd.com/read/28725274/news-in-al-amyloidosis-ash-2016-a%C3%A2-rapidly-evolving-field-of-investigation
#13
REVIEW
Hermine Agis
Amyloidosis is a rare but life-threatening protein misfolding disease. The early diagnosis and enrollment of patients into multicentre trials is of great importance, as is the need for intensive collaboration between multiple medical departments and experienced specialists. In the following review, the most interesting abstracts from the annual American Society of Hematology (ASH) meeting in 2016 are presented. The topics include the limitations of established biomarkers in risk assessment and response evaluation, the introduction of a new biomarker, the comparison of different treatment sequences and the efficacy of a multiple drug regimen in light-chain (AL) amyloidosis...
2017: Memo
https://www.readbyqxmd.com/read/28724957/heterologous-prion-forming-proteins-interact-to-cross-seed-aggregation-in-saccharomyces-cerevisiae
#14
Kathryn M Keefer, Kevin C Stein, Heather L True
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed. Cross-seeding, where one aggregated protein templates the misfolding of a heterologous protein, is one mechanism proposed to stimulate protein aggregation and facilitate disease pathogenesis. Here, we demonstrate the existence of cross-seeding as a crucial step in the formation of the yeast prion [PSI (+)], formed by the translation termination factor Sup35...
July 19, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28724625/amplification-of-misfolded-prion-proteins-in-blood-and-cerebrospinal-fluid-for-detection-of-creutzfeldt-jakob-disease
#15
Mari L DeMarco
No abstract text is available yet for this article.
July 19, 2017: Clinical Chemistry
https://www.readbyqxmd.com/read/28724527/the-spread-of-prion-like-proteins-by-lysosomes-and-tunneling-nanotubes-implications-for-neurodegenerative-diseases
#16
REVIEW
Guiliana Soraya Victoria, Chiara Zurzolo
Progression of pathology in neurodegenerative diseases is hypothesized to be a non-cell-autonomous process that may be mediated by the productive spreading of prion-like protein aggregates from a "donor cell" that is the source of misfolded aggregates to an "acceptor cell" in which misfolding is propagated by conversion of the normal protein. Although the proteins involved in the various diseases are unrelated, common pathways appear to be used for their intercellular propagation and spreading. Here, we summarize recent evidence of the molecular mechanisms relevant for the intercellular trafficking of protein aggregates involved in prion, Alzheimer's, Huntington's, and Parkinson's diseases...
July 19, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28724440/bottleneck-in-secretion-of-%C3%AE-amylase-in-bacillus-subtilis
#17
REVIEW
Shaomin Yan, Guang Wu
Amylase plays an important role in biotechnology industries, and Gram-positive bacterium Bacillus subtilis is a major host to produce heterogeneous α-amylases. However, the secretion stress limits the high yield of α-amylase in B. subtilis although huge efforts have been made to address this secretion bottleneck. In this question-oriented review, every effort is made to answer the following questions, which look simple but are long-standing, through reviewing of literature: (1) Does α-amylase need a specific and dedicated chaperone? (2) What signal sequence does CsaA recognize? (3) Does CsaA require ATP for its operation? (4) Does an unfolded α-amylase is less soluble than a folded one? (5) Does α-amylase aggregate before transporting through Sec secretion system? (6) Is α-amylase sufficient stable to prevent itself from misfolding? (7) Does α-amylase need more disulfide bonds to be stabilized? (8) Which secretion system does PrsA pass through? (9) Is PrsA ATP-dependent? (10) Is PrsA reused after folding of α-amylase? (11) What is the fate of PrsA? (12) Is trigger factor (TF) ATP-dependent? The literature review suggests that not only the most of those questions are still open to answers but also it is necessary to calculate ATP budget in order to better understand how B...
July 19, 2017: Microbial Cell Factories
https://www.readbyqxmd.com/read/28723621/cancer-associated-mutations-in-the-canonical-cleavage-site-do-not-influence-cd99-shedding-by-the-metalloprotease-meprin-%C3%AE-but-alter-cell-migration-in-vitro
#18
Tillmann Bedau, Neele Schumacher, Florian Peters, Johannes Prox, Philipp Arnold, Tomas Koudelka, Ole Helm, Frederike Schmidt, Björn Rabe, Marlene Jentzsch, Philip Rosenstiel, Susanne Sebens, Andreas Tholey, Stefan Rose-John, Christoph Becker-Pauly
Transendothelial cell migration (TEM) is crucial for inflammation and metastasis. The adhesion molecule CD99 was shown to be important for correct immune cell extravasation and is highly expressed on certain cancer cells. Recently, we demonstrated that ectodomain shedding of CD99 by the metalloprotease meprin β promotes TEM in vitro. In this study, we employed an acute inflammation model (air pouch/carrageenan) and found significantly less infiltrated cells in meprin β knock-out animals validating the previously observed pro-inflammatory activity...
July 4, 2017: Oncotarget
https://www.readbyqxmd.com/read/28722658/the-golgi-localized-gamma-ear-containing-arf-binding-gga-protein-family-alters-alpha-synuclein-%C3%AE-syn-oligomerization-and-secretion
#19
Bjoern von Einem, Judith Eschbach, Martin Kiechle, Anke Wahler, Dietmar R Thal, Pamela J McLean, Jochen H Weishaupt, Albert C Ludolph, Christine A F von Arnim, Karin M Danzer
Several age-related neurodegenerative disorders are associated with protein misfolding and aggregation of toxic peptides. α-synuclein (α-syn) aggregation and the resulting cytotoxicity is a hallmark of Parkinson's disease (PD) as well as dementia with Lewy bodies. Rising evidence points to oligomeric and pre-fibrillar forms as the pathogenic species, and oligomer secretion seems to be crucial for the spreading and progression of PD pathology. Recent studies implicate that dysfunctions in endolysosomal/autophagosomal pathways increase α-syn secretion...
July 15, 2017: Aging
https://www.readbyqxmd.com/read/28722340/a-novel-small-molecule-inhibitor-of-prion-replication-and-mutant-prion-protein-toxicity
#20
Tania Massignan, Valeria Sangiovanni, Silvia Biggi, Claudia Stincardini, Saioa R Elezgarai, Giulia Maietta, Ivan A Andreev, Nina K Ratmanova, Dmitry S Belov, Evgeny R Lukyanenko, Grigory M Belov, Maria Letizia Barreca, Andrea Altieri, Alexander V Kurkin, Emiliano Biasini
Prion diseases are a class of neurodegenerative disorders characterized by the accumulation in the brain of a self-replicating, misfolded isoform (PrPSc) of the cellular prion protein (PrPC), a cell-surface glycoprotein of uncertain function. Emerging evidence suggests that PrPC may passively serve as a substrate for the replication of PrPSc, and actively transduce its toxic effects to neuronal cells. The vast majority of previous drug screening campaigns have only targeted PrPSc replication, with largely unsuccessful results...
July 19, 2017: ChemMedChem
keyword
keyword
38813
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"