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molecular chaperone

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https://www.readbyqxmd.com/read/28346090/identifying-inhibitors-of-the-hsp90-aha1-protein-complex-a-potential-target-to-drug-cystic-fibrosis-by-alpha-technology
#1
Verena Ihrig, Wolfgang M J Obermann
Deletion of a single phenylalanine residue at position 508 of the protein CFTR (cystic fibrosis transmembrane conductance regulator), a chloride channel in lung epithelium, is the most common cause for cystic fibrosis. As a consequence, folding of the CFTRΔF508 protein and delivery to the cell surface are compromised, resulting in degradation of the polypeptide. Accordingly, decreased surface presence of CFTRΔF508 causes impaired chloride ion conductivity and is associated with mucus accumulation, a hallmark of cystic fibrosis...
January 1, 2017: SLAS Discov
https://www.readbyqxmd.com/read/28345936/co-registered-molecular-logic-gate-with-a-co-releasing-molecule-triggered-by-light-and-peroxide
#2
Upendar Reddy Gandra, Jörg Axthelm, Patrick Hoffmann, Nandaraj Taye, Steve Glaeser, Helmar Görls, Samantha L Hopkins, Winfried Plass, Ute Neugebauer, Sylvestre Bonnet, Alexander Schiller
Co-registered molecular logic gates combine two different in- and outputs, such as light and matter. We introduce a biocompatible CO-releasing molecule (CORM A) as Mn(I) tricarbonyl complex with the ligand 5-(dimethylamino)-N, N-bis(pyridin-2-ylmethyl) naphthalene-1-sulfonamide (L). CO release is chaperoned by turn-on fluorescence and can be triggered by light (405 nm) as well as with hydrogen peroxide in aqueous phosphate buffer. Complex A behaves as a logic OR gate via co-registering the inputs of irradia-tion (light) and peroxide (matter) into the concomitant outputs fluorescence (light) and CO (matter)...
March 27, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28342889/heteromeric-complexes-of-aldo-keto-reductase-auxiliary-kv%C3%AE-subunits-akr6a-regulate-sarcolemmal-localization-of-kv1-5-in-coronary-arterial-myocytes
#3
Matthew A Nystoriak, Deqing Zhang, Ganapathy Jagatheesan, Aruni Bhatnagar
Redox-sensitive potassium channels consisting of the voltage-gated K(+) (KV) channel pore subunit KV1.5 regulate resting membrane potential and thereby contractility of vascular smooth muscle cells. Members of the KV1 family associate with cytosolic auxiliary β subunits, which are members of the aldo-keto reductase (AKR) superfamily (AKR6A subfamily). The Kvβ subunits have been proposed to regulate Kv1 gating via pyridine nucleotide cofactor binding. However, the molecular identity of KVβ subunits that associate with native KV1...
March 22, 2017: Chemico-biological Interactions
https://www.readbyqxmd.com/read/28342267/the-chaperone-toolbox-at-the-single-molecule-level-from-clamping-to-confining
#4
REVIEW
Mario J Avellaneda, Eline J Koers, Mohsin M Naqvi, Sander J Tans
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the interactions between chaperones and their many clients, as well as the dynamics and heterogeneity of chaperone conformations and the folding process itself. While troublesome for traditional bulk techniques, these properties make an excellent case for the use of single-molecule approaches...
March 25, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28341934/molecular-chaperone-jiv-promotes-the-rna-replication-of-classical-swine-fever-virus
#5
Kangkang Guo, Haimin Li, Xuechao Tan, Mengmeng Wu, Qizhuang Lv, Wei Liu, Yanming Zhang
The nonstructural protein 2 (NS2) of classical swine fever virus (CSFV) is a self-splicing ribozyme wherein the precursor protein NS2-3 is cleaved, and the cleavage efficiency of NS2-3 is crucial to the replication of viral RNA. However, the proteolytic activity of NS2 autoprotease may be achieved through a cellular chaperone called J-domain protein interacting with viral protein (Jiv) or its fragment Jiv90, as evidence suggests that Jiv is required for the proper functioning of the NS2 protein of bovine viral diarrhea virus...
March 24, 2017: Virus Genes
https://www.readbyqxmd.com/read/28341401/discovery-of-2-aminophenyl-methanol-as-a-new-molecular-chaperone-that-rescues-the-localization-of-p123s-mutant-pendrin-stably-expressed-in-hek293-cells
#6
Wataru Nabeyama, Kenji Ishihara, Hyun Seung Ban, Hiroshi Wada, Hiroyuki Nakamura
Pendred syndrome is the most common form of syndromic deafness. It is associated with a mutation in the SLC26A4 gene that encodes pendrin, which is thought to maintain the ion concentration of endolymph in the inner ear most likely by acting as a chloride/bicarbonate transporter. Mutations in the SLC26A4 gene are responsible for sensorineural hearing loss. In this study, we established a stable HEK293 cell line expressing P123S mutant pendrin and developed screening methods for compounds that show pharmacological chaperone activity by image analysis using CellInsight™...
March 14, 2017: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/28339608/inhibition-of-arachidonate-15-lipoxygenase-prevents-4-hydroxynonenal-induced-protein-damage-in-male-germ-cells%C3%A2
#7
Elizabeth G Bromfield, Bettina P Mihalas, Matthew D Dun, R John Aitken, Eileen A McLaughlin, Jessica L H Walters, Brett Nixon
Lipid peroxidation products, such as 4-hydroxynonenal (4HNE), are causative agents responsible for extensive protein damage within the male and female germlines. Recently, we have demonstrated that 4HNE production can initiate the proteolytic degradation of the molecular chaperone Heat Shock Protein A2 (HSPA2) in male germ cells. These events may be partially responsible for HSPA2 deficiency in the spermatozoa of patients that repeatedly fail in vitro fertilization. Given this, mechanisms that limit the production of 4HNE will be highly advantageous for the preservation of male fertility...
February 2, 2017: Biology of Reproduction
https://www.readbyqxmd.com/read/28339481/proteomic-analysis-of-injured-storage-roots-in-cassava-manihot-esculenta-crantz-under-postharvest-physiological-deterioration
#8
Yuling Qin, Astride Stéphanie Mouafi Djabou, Feifei An, Kaimian Li, Zhaogui Li, Long Yang, Xiaojing Wang, Songbi Chen
Postharvest physiological deterioration (PPD) is a global challenge in the improvement of cassava value chain. However, how to reduce cassava spoilage and reveal the mechanism of injured cassava storage roots in response to PPD were poorly understood. In the present study, we investigated the activities of antioxidant enzymes of cassava injured storage roots in PPD-susceptible (SC9) and PPD-tolerant (QZ1) genotypes at the time-points from 0h to 120h, and further analyzed their proteomic changes using two-dimensional electrophoresis (2-DE) in combination with MALDI-TOF-MS/MS...
2017: PloS One
https://www.readbyqxmd.com/read/28337643/recombinant-heat-shock-protein-27-hsp27-hspb1-protects-against-cadmium-induced-oxidative-stress-and-toxicity-in-human-cervical-cancer-cells
#9
Daiana G Alvarez-Olmedo, Veronica S Biaggio, Geremy A Koumbadinga, Nidia N Gómez, Chunhua Shi, Daniel R Ciocca, Zarah Batulan, Mariel A Fanelli, Edward R O'Brien
Cadmium (Cd) is a carcinogen with several well-described toxicological effects in humans, but its molecular mechanisms are still not fully understood. Overexpression of heat shock protein 27 (HSP27/HSPB1)-a multifunctional protein chaperone-has been shown to protect cells from oxidative damage and apoptosis triggered by Cd exposure. The aims of this work were to investigate the potential use of extracellular recombinant HSP27 to prevent/counteract Cd-induced cellular toxicity and to evaluate if peroxynitrite was involved in the development of Cd-induced toxicity...
March 24, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28337642/the-small-heat-shock-proteins-%C3%AE-b-crystallin-hspb5-and-hsp27-hspb1-inhibit-the-intracellular-aggregation-of-%C3%AE-synuclein
#10
Dezerae Cox, Heath Ecroyd
Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. Proteostasis is preserved in the face of stress by a complex network of cellular machinery, including the small heat shock molecular chaperone proteins (sHsps), which act to inhibit the aggregation and deposition of misfolded protein intermediates. Despite this, the pathogenesis of several neurodegenerative diseases has been inextricably linked with the amyloid fibrillar aggregation and deposition of α-synuclein (α-syn)...
March 23, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28336682/molecular-mechanism-of-mrna-repression-in-trans-by-a-proq-dependent-small-rna
#11
Alexandre Smirnov, Chuan Wang, Lisa L Drewry, Jörg Vogel
Research into post-transcriptional control of mRNAs by small noncoding RNAs (sRNAs) in the model bacteria Escherichia coli and Salmonella enterica has mainly focused on sRNAs that associate with the RNA chaperone Hfq. However, the recent discovery of the protein ProQ as a common binding partner that stabilizes a distinct large class of structured sRNAs suggests that additional RNA regulons exist in these organisms. The cellular functions and molecular mechanisms of these new ProQ-dependent sRNAs are largely unknown...
March 23, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28334762/missense-uros-mutations-causing-congenital-erythropoietic-porphyria-reduce-uros-homeostasis-that-can-be-rescued-by-proteasome-inhibition
#12
Jean-Marc Blouin, Ganeko Bernardo-Seisdedos, Emma Sasso, Julie Esteve, Cécile Ged, Magalie Lalanne, Arantza Sanz-Parra, Pedro Urquiza, Hubert de Verneuil, Oscar Millet, Emmanuel Richard
Congenital erythropoietic porphyria (CEP) is an inborn error of heme biosynthesis characterized by uroporphyrinogen III synthase (UROS) deficiency resulting in deleterious porphyrin accumulation in blood cells responsible for hemolytic anemia and cutaneous photosensitivity. We analyzed here the molecular basis of UROS impairment associated with twenty nine UROS missense mutations actually described in CEP patients. Using a computational and biophysical joint approach we predicted that most disease-causing mutations would affect UROS folding and stability...
February 21, 2017: Human Molecular Genetics
https://www.readbyqxmd.com/read/28333306/protein-aggregation-in-ehrlichia-chaffeensis-during-infection-of-mammalian-cells
#13
Dorota Kuczynska-Wisnik, Chuanmin Cheng, Roman R Ganta, Michal Zolkiewski
Ehrlichia chaffeensis is an obligatory intracellular pathogen transmitted through infected ticks to humans and other vertebrates. We investigated the extent of protein aggregation in E. chaffeensis during infection of canine macrophage cell line, DH82. We discovered that the size of the aggregated fraction of E. chaffeensis proteins increased during the first 48 h post infection. We also incubated the infected cells with guanidinium chloride (GuHCl), a known inhibitor of the protein-disaggregating molecular chaperone ClpB...
March 15, 2017: FEMS Microbiology Letters
https://www.readbyqxmd.com/read/28333162/the-endoplasmic-reticulum-chaperone-grp78-bip-modulates-prion-propagation-in-vitro-and-in-vivo
#14
Kyung-Won Park, Gyoung Eun Kim, Rodrigo Morales, Fabio Moda, Ines Moreno-Gonzalez, Luis Concha-Marambio, Amy S Lee, Claudio Hetz, Claudio Soto
Prion diseases are fatal neurodegenerative disorders affecting several mammalian species, characterized by the accumulation of the misfolded form of the prion protein, which is followed by the induction of endoplasmic reticulum (ER) stress and the activation of the unfolded protein response (UPR). GRP78, also called BiP, is a master regulator of the UPR, reducing ER stress levels and apoptosis due to an enhancement of the cellular folding capacity. Here, we studied the role of GRP78 in prion diseases using several in vivo and in vitro approaches...
March 23, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28327546/missense-mutations-near-the-n-glycosylation-site-of-the-a2-domain-lead-to-various-intracellular-trafficking-defects-in-coagulation-factor-viii
#15
Wei Wei, Chunlei Zheng, Min Zhu, Xiaofan Zhu, Renchi Yang, Saurav Misra, Bin Zhang
Missense mutation is the most common mutation type in hemophilia. However, the majority of missense mutations remain uncharacterized. Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking. N582 is located in the middle of a short 310-helical turn (D580-S584), in which most amino acids have multiple hemophilia mutations. All 14 missense mutations found in this 310-helix reduced secretion levels of the A2 domain and full-length FVIII...
March 22, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28326013/molecular-chaperone-calnexin-regulates-the-function-of-drosophila-sodium-channel-paralytic
#16
Xi Xiao, Changyan Chen, Tian-Ming Yu, Jiayao Ou, Menglong Rui, Yuanfen Zhai, Yijing He, Lei Xue, Margaret S Ho
Neuronal activity mediated by voltage-gated channels provides the basis for higher-order behavioral tasks that orchestrate life. Chaperone-mediated regulation, one of the major means to control protein quality and function, is an essential route for controlling channel activity. Here we present evidence that Drosophila ER chaperone Calnexin colocalizes and interacts with the α subunit of sodium channel Paralytic. Co-immunoprecipitation analysis indicates that Calnexin interacts with Paralytic protein variants that contain glycosylation sites Asn313, 325, 343, 1463, and 1482...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28324209/molecular-cloning-structural-modeling-and-the-production-of-soluble-triple-mutated-diphtheria-toxoid-k51e-g52e-e148k-co-expressed-with-molecular-chaperones-in-recombinant-escherichia-coli
#17
Naphatsamon Uthailak, Pornpimol Mahamad, Pamorn Chittavanich, Somchai Yanarojana, Wassana Wijagkanalan, Jean Petre, Watanalai Panbangred
CRM197 is a diphtheria toxin (DT) mutant (G52E) which has been used as a carrier protein for conjugate vaccines. However, it still possesses cytotoxicity toward mammalian cells. The goal of this project was to produce a non-toxic and soluble CRM197EK through introduction of triple amino acid substitutions (K51E/G52E/E148K) in Escherichia coli. The expression of CRM197EKTrxHis was optimized and co-expressed with different molecular chaperones. The soluble CRM197EKTrxHis was produced at a high concentration (97...
March 21, 2017: Molecular Biotechnology
https://www.readbyqxmd.com/read/28323215/identification-and-characterization-of-a-novel-calreticulin-involved-in-the-immune-response-of-the-zhikong-scallop-chlamys-farreri
#18
Guanghua Wang, Zengjie Jiang, Ning Yang, Dongfa Zhu, Min Zhang
Calreticulin (CRT) is a multifunctional calcium-binding chaperone shared among vertebrates and invertebrates. In this study, a novel CRT (CfCRT) was identified in the Zhikong scallop Chlamys farreri by rapid amplification of cDNA ends. The full-length cDNA was composed of 1345 bp, which included a 1158 bp open reading frame, a 25 bp 5'-untranslated region (UTR) and a 162 bp 3'-UTR. The predicted molecular mass of CfCRT was 44.8 kDa. CfCRT contained three highly conserved domains (N-, P- and C-domains) essential to the function of CRT...
March 18, 2017: Fish & Shellfish Immunology
https://www.readbyqxmd.com/read/28323023/internalization-axonal-transport-and-release-of-fibrillar-forms-of-alpha-synuclein
#19
Gregor Bieri, Aaron D Gitler, Michel Brahic
Intra-neuronal protein aggregates made of fibrillar alpha-synuclein (α-syn) are the hallmark of Parkinson's disease (PD). With time, these aggregates spread through the brain following axonal projections. Understanding the mechanism of this spread is central to the study of the progressive nature of PD. Here we review data relevant to the uptake, transport and release of α-syn fibrils. We summarize several cell surface receptors that regulate the uptake of α-syn fibrils by neurons. The aggregates are then transported along axons, both in the anterograde and retrograde direction...
March 16, 2017: Neurobiology of Disease
https://www.readbyqxmd.com/read/28322792/molecular-chaperones-of-the-hsp70-family-assist-in-the-assembly-of-20s-proteasomes
#20
Lindsay J Hammack, Kyle Firestone, William Chang, Andrew R Kusmierczyk
The eukaryotic 26S proteasome is a large protease comprised of two major sub assemblies, the 20S proteasome, or core particle (CP), and the 19S regulatory particle (RP). Assembly of the CP and RP is assisted by an expanding list of dedicated assembly factors. For the CP, this includes Ump1 and the heterodimeric Pba1-Pba2 and Pba3-Pba4 proteins. It is not known how many additional proteins that assist in proteasome biogenesis remain to be discovered. Here, we demonstrate that two members of the Hsp70 family in yeast, Ssa1 and Ssa2, play a direct role in CP assembly...
March 17, 2017: Biochemical and Biophysical Research Communications
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