TY - JOUR AU - Farkas, Anita AU - Zsindely, Nóra AU - Nagy, Gábor AU - Kovács, Levente AU - Deák, Péter AU - Bodai, László TI - The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 13 PY - 2023 IS - 1 PG - 13 SN - 2045-2322 DO - 10.1038/s41598-023-49241-8 UR - https://m2.mtmt.hu/api/publication/34431874 ID - 34431874 AB - Huntington’s disease (HD) is a neurodegenerative disorder caused by a dominant gain-of-function mutation in the huntingtin gene, resulting in an elongated polyglutamine repeat in the mutant Huntingtin (mHtt) that mediates aberrant protein interactions. Previous studies implicated the ubiquitin–proteasome system in HD, suggesting that restoring cellular proteostasis might be a key element in suppressing pathology. We applied genetic interaction tests in a Drosophila model to ask whether modulating the levels of deubiquitinase enzymes affect HD pathology. By testing 32 deubiquitinase genes we found that overexpression of Yod1 ameliorated all analyzed phenotypes, including neurodegeneration, motor activity, viability, and longevity. Yod1 did not have a similar effect in amyloid beta overexpressing flies, suggesting that the observed effects might be specific to mHtt. Yod1 overexpression did not alter the number of mHtt aggregates but moderately increased the ratio of larger aggregates. Transcriptome analysis showed that Yod1 suppressed the transcriptional effects of mHtt and restored the expression of genes involved in neuronal plasticity, vesicular transport, antimicrobial defense, and protein synthesis, modifications, and clearance. Furthermore, Yod1 overexpression in HD flies leads to the upregulation of genes involved in transcriptional regulation and synaptic transmission, which might be part of a response mechanism to mHtt-induced stress. LA - English DB - MTMT ER - TY - JOUR AU - Pai, Yueh-Ling AU - Lin, Yuchieh Jay AU - Peng, Wen-Hsin AU - Huang, Li-Ting AU - Chou, He-Yen AU - Wang, Chien-Hsiang AU - Chien, Cheng-Ting AU - Chen, Guang-Chao TI - The deubiquitinase Leon/USP5 interacts with Atg1/ULK1 and antagonizes autophagy JF - CELL DEATH AND DISEASE J2 - CELL DEATH DIS VL - 14 PY - 2023 IS - 8 PG - 11 SN - 2041-4889 DO - 10.1038/s41419-023-06062-x UR - https://m2.mtmt.hu/api/publication/34131249 ID - 34131249 N1 - Funding Agency and Grant Number: Taiwan National Science and Technology Council [MOST111-2311-B-001-018-MY3]; Academia Sinica Funding text: We thank Jui-Chou Hsu, Thomas Neufeld, the Bloomington Stock Center, Vienna Drosophila RNAi Center, and Fly Core Taiwan for reagents and fly stocks; the National RNAi Core Facility (Academia Sinica, Taiwan) for shRNAs. We thank Hong-Ru Lin for the initiation of the genetic screen. We are grateful to members of the Chen laboratory for helpful discussions during the course of this work. This work was supported by the Taiwan National Science and Technology Council (MOST111-2311-B-001-018-MY3) and by Academia Sinica. AB - Accumulating evidence has shown that the quality of proteins must be tightly monitored and controlled to maintain cellular proteostasis. Misfolded proteins and protein aggregates are targeted for degradation through the ubiquitin proteasome (UPS) and autophagy-lysosome systems. The ubiquitination and deubiquitinating enzymes (DUBs) have been reported to play pivotal roles in the regulation of the UPS system. However, the function of DUBs in the regulation of autophagy remain to be elucidated. In this study, we found that knockdown of Leon/USP5 caused a marked increase in the formation of autophagosomes and autophagic flux under well-fed conditions. Genetic analysis revealed that overexpression of Leon suppressed Atg1-induced cell death in Drosophila. Immunoblotting assays further showed a strong interaction between Leon/USP5 and the autophagy initiating kinase Atg1/ULK1. Depletion of Leon/USP5 led to increased levels of Atg1/ULK1. Our findings indicate that Leon/USP5 is an autophagic DUB that interacts with Atg1/ULK1, negatively regulating the autophagic process. LA - English DB - MTMT ER - TY - JOUR AU - Yan, Bokang AU - Guo, Jiaxing AU - Deng, Shuang AU - Chen, Dongliang AU - Huang, Meiyuan TI - A pan-cancer analysis of the role of USP5 in human cancers JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 13 PY - 2023 IS - 1 PG - 19 SN - 2045-2322 DO - 10.1038/s41598-023-35793-2 UR - https://m2.mtmt.hu/api/publication/34287292 ID - 34287292 AB - Posttranslational modifications (PTM) such as acetylation, deubiquitination, and phosphorylation of proteins, play important roles in various kinds of cancer progression. Ubiquitin-specific proteinase 5 (USP5), a unique member of deubiquitinating enzymes (DUBs) which recognizes unanchored polyubiquitin specifically, could regulate the stability of many tumorigenesis-associated proteins to influence cancer initiation and progression. However, the diverse biological significance of USP5 in pan-cancer has not been systematically and comprehensively studied. Here, we explored the role of USP5 in pan-cancer using The Cancer Genome Atlas (TCGA) and Genotype-Tissue Expression (GTEx) database, and we also acquired and analyzed data via various software and web platforms such as R, GEPIA2.0, HPA, TISIDB, cBioPortal, UALCAN, TIMER 2.0, CancerSEA and BioGRID. USP5 expression was high in most cancers and differed significantly in different molecular and immune subtypes of cancers. In addition, USP5 had certain diagnostic value in multiple cancers, and high expression of USP5 generally predicted poor prognosis for cancer patients. We also found that the most frequent genetic alterations type of USP5 was mutation, and the DNA methylation level of USP5 decreased in various cancers. Furthermore, USP5 expression correlated with cancer-associated fibroblasts (CAFs), endothelial cells (EC) and genetic markers of immunodulators in cancers. Moreover, the result from single cell sequencing showed that USP5 could regulate several tumor biological behaviors such as apoptosis, DNA damage and metastasis. Gene enrichment analysis indicated "spliceosome" and "RNA splicing" may be the critical mechanism for USP5 to involve in cancer. Taken together, our study elucidates the biological significance of USP5 in the diagnosis, prognosis and immune in human pan-cancer. LA - English DB - MTMT ER - TY - JOUR AU - Zhang, X. AU - Zhai, Y. AU - Zhang, D. AU - Che, C. AU - Zhang, Y. AU - Li, Q. AU - Zhang, X. AU - Zhao, L. TI - RNAseq analysis of the drug jian-yan-ling (JYL) using both in vivo and in vitro models JF - HELIYON J2 - HELIYON VL - 9 PY - 2023 IS - 5 SN - 2405-8440 DO - 10.1016/j.heliyon.2023.e16143 UR - https://m2.mtmt.hu/api/publication/34110744 ID - 34110744 N1 - School of Life Sciences, Fudan University, Shanghai, 200438, China Lei Yun Shang Pharmaceutical Group Co.,Ltd., Suzhou, 215009, China Key Laboratory of Growth Regulation and Translational Research of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, 310024, China Export Date: 25 August 2023 Correspondence Address: Zhao, L.; Key Laboratory of Growth Regulation and Translational Research of Zhejiang Province, China; email: zhaolingrui@westlake.edu.cn AB - Ethnopharmacological relevance: Jian-yan-ling (JYL) is a drug used in traditional Chinese medicine (TCM) prescriptions for the treatment of tumors after radiotherapy and chemotherapy, to effectively alleviate leukocytopenia. However, the genetic mechanisms underlying the function of JYL remain unclear. Aim of the study: This study aimed to explore the RNA changes and potential biological processes related to the anti-aging or life-extending effects of JYL treatments. Materials and methods: In vivo treatments were performed using Canton-S Drosophila corresponding to three groups: control, low-concentration (low-conc.), and high-concentration (high-conc.) groups. The low-conc. And the high-conc. Groups were treated with 4 mg/mL JYL and 8 mg/mL JYL, respectively. Thirty Drosophila eggs were placed in each vial, and the third instar larvae and adults 7 and 21 days post-eclosion were collected for RNA sequencing, irrespective of the gender. In vitro treatments were conducted using humanized immune cell lines HL60 and Jurkat, which were divided into 3 groups: control (0 μg/mL JYL), low-concentration (40 μg/mL JYL), and high-concentration (80 μg/mL JYL). The cells were collected after 48 h of each JYL drug treatment. Both the Drosophila and cell samples were analyzed using RNA sequencing. Results: The in vivo experiments revealed 74 upregulated genes in the low-concentration group, and CG13078 was a commonly downregulated differential gene, which is involved in ascorbate iron reductase activity. Further analysis of the co-expression map identified the key genes: regulatory particle non-ATPase (RPN), regulatory particle triple-A ATPase (RPT), and tripeptidyl-peptidase II (TPP II). For the in vitro experiments, 19 co-differential genes were compared between different concentrations of the HL 60 cell line, of which three genes were upregulated: LOC107987457 (phostensin-like gene), HSPA1A (heat shock protein family A member 1 A), and H2AC19 (H2A clustered histone 19). In the HL 60 cell line, JYL activated proteasome-related functions. In the Jurkat cell line, there were no common differential genes despite the presence of a dosage-dependent trend. Conclusions: The RNA-seq results showed that the traditional Chinese medicine JYL has longevity and anti-aging effects, indicating that further investigation is required. © 2023 The Authors LA - English DB - MTMT ER - TY - JOUR AU - Páhi, Zoltán Gábor AU - Kovács, Levente AU - Szűcs, Diána AU - Borsos, Barbara Nikolett AU - Deák, Péter AU - Pankotai, Tibor TI - Usp5, Usp34, and Otu1 deubiquitylases mediate DNA repair in Drosophila melanogaster JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 12 PY - 2022 IS - 1 PG - 11 SN - 2045-2322 DO - 10.1038/s41598-022-09703-x UR - https://m2.mtmt.hu/api/publication/32778093 ID - 32778093 N1 - Institute of Pathology, Albert Szent-Györgyi Medical School, University of Szeged, 1 Állomás Street, Szeged, 6725, Hungary Department of Genetics, Faculty of Sciences and Informatics, University of Szeged, 52 Közép fasor, Szeged, 6726, Hungary Divison of Biology and Biological Engineering, California Institute of Tehnology, 1200 East California Boulevard, Pasadena, 91125, United States Cited By :2 Export Date: 29 February 2024 Correspondence Address: Pankotai, T.; Institute of Pathology, 1 Állomás Street, Hungary; email: pankotai.tibor@szte.hu Chemicals/CAS: hydrolase, 9027-41-2; ubiquitin, 60267-61-0; Drosophila Proteins; Hydrolases; Ubiquitin; Ubiquitin-Specific Proteases; USP5 protein, Drosophila Funding details: Magyar Tudományos Akadémia, MTA, BO/27/20, ÚNKP-20-5-SZTE-265, ÚNKP-21-5-SZTE-563 Funding details: National Research, Development and Innovation Office, GINOP-2.2.1-15-2017-00052, GINOP-2.3.2-15-2016-00032, NKFI-FK 132080 Funding text 1: Open access funding provided by University of Szeged. This research was funded by National Research, Development and Innovation Office Grant GINOP-2.2.1-15-2017-00052, GINOP-2.3.2-15-2016-00032 and NKFI-FK 132080, the János Bolyai Research Scholarship of the Hungarian Academy of Sciences BO/27/20, ÚNKP-20-5-SZTE-265 and ÚNKP-21-5-SZTE-563. LA - English DB - MTMT ER - TY - JOUR AU - Sparks, Alison AU - Kelly, Christopher J. AU - Saville, Mark K. TI - Ubiquitin receptors play redundant roles in the proteasomal degradation of the p53 repressor MDM2 JF - FEBS LETTERS J2 - FEBS LETT PY - 2022 PG - 22 SN - 0014-5793 DO - 10.1002/1873-3468.14436 UR - https://m2.mtmt.hu/api/publication/33181464 ID - 33181464 N1 - Export Date: 8 February 2023 CODEN: FEBLA AB - Much remains to be determined about the participation of ubiquitin receptors in proteasomal degradation and their potential as therapeutic targets. Suppression of the ubiquitin receptor S5A/PSMD4/hRpn10 alone stabilises p53/TP53 but not the key p53 repressor MDM2. Here, we observed S5A and the ubiquitin receptors ADRM1/PSMD16/hRpn13 and RAD23A and B functionally overlap in MDM2 degradation. We provide further evidence that degradation of only a subset of ubiquitinated proteins is sensitive to S5A knockdown because ubiquitin receptor redundancy is commonplace. p53 can be upregulated by S5A modulation while degradation of substrates with redundant receptors is maintained. Our observations and analysis of Cancer Dependency Map (DepMap) screens show S5A depletion/loss substantially reduces cancer cell line viability. This and selective S5A dependency of proteasomal substrates make S5A a target of interest for cancer therapy. LA - English DB - MTMT ER - TY - JOUR AU - Koyuncu, Seda AU - Loureiro, Rute AU - Lee, Hyun Ju AU - Wagle, Prerana AU - Krueger, Marcus AU - Vilchez, David TI - Rewiring of the ubiquitinated proteome determines ageing in C. elegans JF - NATURE J2 - NATURE VL - 596 PY - 2021 IS - 7871 SP - 285 EP - + PG - 32 SN - 0028-0836 DO - 10.1038/s41586-021-03781-z UR - https://m2.mtmt.hu/api/publication/32368712 ID - 32368712 AB - Ageing is driven by a loss of cellular integrity(1). Given the major role of ubiquitin modifications in cell function(2), here we assess the link between ubiquitination and ageing by quantifying whole-proteome ubiquitin signatures in Caenorhabditis elegans. We find a remodelling of the ubiquitinated proteome during ageing, which is ameliorated by longevity paradigms such as dietary restriction and reduced insulin signalling. Notably, ageing causes a global loss of ubiquitination that is triggered by increased deubiquitinase activity. Because ubiquitination can tag proteins for recognition by the proteasome(3), a fundamental question is whether deficits in targeted degradation influence longevity. By integrating data from worms with a defective proteasome, we identify proteasomal targets that accumulate with age owing to decreased ubiquitination and subsequent degradation. Lowering the levels of age-dysregulated proteasome targets prolongs longevity, whereas preventing their degradation shortens lifespan. Among the proteasomal targets, we find the IFB-2 intermediate filament(4) and the EPS-8 modulator of RAC signalling(5). While increased levels of IFB-2 promote the loss of intestinal integrity and bacterial colonization, upregulation of EPS-8 hyperactivates RAC in muscle and neurons, and leads to alterations in the actin cytoskeleton and protein kinase JNK. In summary, age-related changes in targeted degradation of structural and regulatory proteins across tissues determine longevity. LA - English DB - MTMT ER - TY - JOUR AU - Blount, Jessica R. AU - Libohova, Kozeta AU - Silva, Gustavo M. AU - Todi, Sokol V TI - Isoleucine 44 Hydrophobic Patch Controls Toxicity of Unanchored, Linear Ubiquitin Chains through NF-kappa B Signaling JF - CELLS J2 - CELLS-BASEL VL - 9 PY - 2020 IS - 6 PG - 21 SN - 2073-4409 DO - 10.3390/cells9061519 UR - https://m2.mtmt.hu/api/publication/31467834 ID - 31467834 AB - Ubiquitination is a post-translational modification that regulates cellular processes by altering the interactions of proteins to which ubiquitin, a small protein adduct, is conjugated. Ubiquitination yields various products, including mono- and poly-ubiquitinated substrates, as well as unanchored poly-ubiquitin chains whose accumulation is considered toxic. We previously showed that transgenic, unanchored poly-ubiquitin is not problematic inDrosophila melanogaster. In the fruit fly, free chains exist in various lengths and topologies and are degraded by the proteasome; they are also conjugated onto other proteins as one unit, eliminating them from the free ubiquitin chain pool. Here, to further explore the notion of unanchored chain toxicity, we examined when free poly-ubiquitin might become problematic. We found that unanchored chains can be highly toxic if they resemble linear poly-ubiquitin that cannot be modified into other topologies. These species upregulate NF-kappa B signaling, and modulation of the levels of NF-kappa B components reduces toxicity. In additional studies, we show that toxicity from untethered, linear chains is regulated by isoleucine 44, which anchors a key interaction site for ubiquitin. We conclude that free ubiquitin chains can be toxic, but only in uncommon circumstances, such as when the ability of cells to modify and regulate them is markedly restricted. LA - English DB - MTMT ER - TY - JOUR AU - Blount, Jessica R. AU - Johnson, Sean L. AU - Todi, Sokol V. TI - Unanchored Ubiquitin Chains, Revisited JF - FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY J2 - FRONT CELL DEV BIOL VL - 8 PY - 2020 PG - 24 SN - 2296-634X DO - 10.3389/fcell.2020.582361 UR - https://m2.mtmt.hu/api/publication/31689866 ID - 31689866 AB - The small modifier protein, ubiquitin, holds a special place in eukaryotic biology because of its myriad post-translational effects that control normal cellular processes and are implicated in various diseases. By being covalently conjugated onto other proteins, ubiquitin changes their interaction landscape - fostering new interactions as well as inhibiting others - and ultimately deciding the fate of its substrates and controlling pathways that span most cell physiology. Ubiquitin can be attached onto other proteins as a monomer or as a poly-ubiquitin chain of diverse structural topologies. Among the types of poly-ubiquitin species generated are ones detached from another substrate - comprising solely ubiquitin as their constituent - referred to as unanchored, or free chains. Considered to be toxic byproducts, these species have recently emerged to have specific physiological functions in immune pathways and during cell stress. Free chains also do not appear to be detrimental to multi-cellular organisms; they can be active members of the ubiquitination process, rather than corollary species awaiting disassembly into mono-ubiquitin. Here, we summarize past and recent studies on unanchored ubiquitin chains, paying special attention to their emerging roles as second messengers in several signaling pathways. These investigations paint complex and flexible outcomes for free ubiquitin chains, and present a revised model of unanchored poly-ubiquitin biology that is in need of additional investigation. LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Levente AU - Nagy, Ágota AU - Pál, Margit AU - Deák, Péter TI - Usp14 is required for spermatogenesis and ubiquitin stress responses in Drosophila melanogaster. JF - JOURNAL OF CELL SCIENCE J2 - J CELL SCI VL - 133 PY - 2020 IS - 2 PG - 6 SN - 0021-9533 DO - 10.1242/jcs.237511 UR - https://m2.mtmt.hu/api/publication/31158977 ID - 31158977 AB - Deubiquitylating (DUB) enzymes free covalently linked ubiquitin moieties from ubiquitin-ubiquitin and ubiquitin-protein conjugates, and thereby maintain the equilibrium between free and conjugated ubiquitin moieties and regulate ubiquitin-mediated cellular processes. Here, we performed genetic analyses of mutant phenotypes in Drosophila melanogaster and demonstrate that loss of Usp14 function results in male sterility, with defects in spermatid individualization and reduced testicular free monoubiquitin levels. These phenotypes were rescued by germline-specific overexpression of wild-type Usp14. Synergistic genetic interactions with Ubi-p63E and cycloheximide sensitivity suggest that ubiquitin shortage is a primary cause of male sterility. In addition, Usp14 is predominantly expressed in testes in Drosophila, indicating a higher demand for this DUB in testes that is also reflected by testis-specific loss-of-function Usp14 phenotypes. Collectively, these results suggest a major role of Usp14 in maintaining normal steady state free monoubiquitin levels during the later stages of Drosophila spermatogenesis.This article has an associated First Person interview with the first author of the paper. LA - English DB - MTMT ER - TY - JOUR AU - Krishnan, G AU - Paul, V AU - Biswas, T K AU - Chouhan, V S AU - Das, P J AU - Sejian, V TI - Adaptation strategies of yak to seasonally driven environmental temperatures in its natural habitat JF - INTERNATIONAL JOURNAL OF BIOMETEOROLOGY J2 - INT J BIOMETEOROL VL - 62 PY - 2018 SP - 1 SN - 0020-7128 DO - 10.1007/s00484-018-1549-8 UR - https://m2.mtmt.hu/api/publication/27371354 ID - 27371354 LA - English DB - MTMT ER - TY - JOUR AU - Krishnan, G AU - Paul, V AU - Biswas, TK AU - Chouhan, VS AU - Das, PJ AU - Sejian, V TI - Diurnal variation and oscillatory patterns in physiological responses and HSP70 profile in heat stressed yaks at high altitude JF - BIOLOGICAL RHYTHM RESEARCH J2 - BIOL RHYTHM RES VL - 49 PY - 2018 SP - 1 SN - 0929-1016 DO - 10.1080/09291016.2018.1424770 UR - https://m2.mtmt.hu/api/publication/27126443 ID - 27126443 LA - English DB - MTMT ER - TY - JOUR AU - Mikuš, Tomislav AU - Radeski, Miroslav AU - Toma Cziszter, Ludovic AU - Dimitrov, Ivan AU - Jurkovich, Viktor AU - Nenadović, Katarina AU - Ostović, Mario AU - Zupan, Manja AU - Katharina Kirchner, Marlene TI - The Danube Region—On Stream with Animal Welfare Assessment in the Last 35 Years: A Review of Research on Animal Welfare Assessment in a Multi-lingual Area in Europe JF - JOURNAL OF AGRICULTURAL & ENVIRONMENTAL ETHICS J2 - J AGR ENVIRON ETHIC VL - 31 PY - 2018 IS - 4 SP - 511 EP - 526 PG - 16 SN - 1187-7863 DO - 10.1007/s10806-018-9737-4 UR - https://m2.mtmt.hu/api/publication/3383871 ID - 3383871 AB - This review presents first ever literature survey on historical development of farm animal welfare indicators and assessment in the Danube region. This area, encompassing European Eastern countries and the Balkans, is to a large extent heterogeneous in terms of culture and language. However, international (English) publications were disproportionally small compared to the amount of research institutions and animal welfare activities present in the region. Therefore, the authors aimed at investigating the published literature, focusing on country level and on native languages. Data were collected for the 1980-2015 period referring to scientific papers published in international and national journals, papers and abstracts in proceedings of the international and national conferences, reviews, monographs, short communications, Ph.D., Master and Graduation theses. Welfare assessment of all farm animal species was observed including fish. Over 180 papers were in line with the preselected index. Data collected showed that publishing dynamics grew rapidly towards the last decade. Most of the studies were focused on animal welfare indicators such as stress, injuries and mutilations, behaviour, body condition and management practices. Cattle, chickens, pigs and sheep were the predominant species investigated. The study revealed that experts from the region were greatly involved in the studies of animal welfare indicators and assessment, contributing to development of the currently most widely used animal welfare assessment protocols, thus having an important role in animal welfare research and protection. LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Ágota AU - Kovács, Levente AU - Lipinszki, Zoltán AU - Pál, Margit AU - Deák, Péter TI - Developmental- and tissue-specific changes of ubiquitin forms in Drosophila melanogaster JF - PLOS ONE J2 - PLOS ONE VL - 13 PY - 2018 IS - 12 PG - 10 SN - 1932-6203 DO - 10.1371/journal.pone.0209080 UR - https://m2.mtmt.hu/api/publication/30343721 ID - 30343721 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office [OTKA-K116372, OTKA-PD115404]; Ministry for National Economy of Hungary [GINOP-2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00032]; Hungarian Academy of Sciences [bo_329_15, LP2017-7/2017] Funding text: This work was funded by grants from the National Research, Development and Innovation Office (OTKA-K116372 and OTKA-PD115404), Ministry for National Economy of Hungary (GINOP-2.3.2-15-2016-00001 and GINOP-2.3.2-15-2016-00032) and Hungarian Academy of Sciences (Bolyai Fellowship (bo_329_15) and Lendulet Program Grant (LP2017-7/2017)). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Department of Genetics, University of Szeged, Szeged, Hungary Institute of Biochemistry, Biological Research Centre, Szeged, Hungary MTA SZBK Lendület Laboratory of Cell Cycle Regulation, Biological Research Centre, Szeged, Hungary Department of Genetics, University of Cambridge, Cambridge, United Kingdom Export Date: 11 February 2020 CODEN: POLNC Correspondence Address: Deák, P.; Department of Genetics, University of SzegedHungary; email: deakp@bio.u-szeged.hu LA - English DB - MTMT ER - TY - JOUR AU - Simoes, Tania AU - Schuster, Ramona AU - den Brave, Fabian AU - Escobar-Henriques, Mafalda TI - Cdc48 regulates a deubiquitylase cascade critical for mitochondrial fusion JF - ELIFE J2 - ELIFE VL - 7 PY - 2018 PG - 29 SN - 2050-084X DO - 10.7554/eLife.30015 UR - https://m2.mtmt.hu/api/publication/27523982 ID - 27523982 LA - English DB - MTMT ER - TY - JOUR AU - Wang, Zhao AU - Zhang, Hong AU - Liu, Caiyun AU - Xing, Junjie AU - Chen, Xiao-Lin TI - A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae JF - FRONTIERS IN MICROBIOLOGY J2 - FRONT MICROBIOL VL - 9 PY - 2018 PG - 14 SN - 1664-302X DO - 10.3389/fmicb.2018.00769 UR - https://m2.mtmt.hu/api/publication/27523981 ID - 27523981 LA - English DB - MTMT ER - TY - JOUR AU - Ling, Xuemei AU - Huang, Qinzhu AU - Xu, Yanqin AU - Jin, Yuxiao AU - Feng, Ying AU - Shi, Weijie AU - Ye, Xiaolei AU - Lin, Yi AU - Hou, Ling AU - Lin, Xinhua TI - The deubiquitinating enzyme Usp5 regulates Notch and RTK signaling during Drosophila eye development JF - FEBS LETTERS J2 - FEBS LETT VL - 591 PY - 2017 IS - 6 SP - 875 EP - 888 PG - 14 SN - 0014-5793 DO - 10.1002/1873-3468.12580 UR - https://m2.mtmt.hu/api/publication/26535174 ID - 26535174 LA - English DB - MTMT ER - TY - JOUR AU - Sinenko, SA TI - Proapoptotic function of deubiquitinase DUSP31 in Drosophila JF - ONCOTARGET J2 - ONCOTARGET VL - 8 PY - 2017 IS - 41 SP - 70452 EP - 70462 PG - 11 SN - 1949-2553 DO - 10.18632/oncotarget.19715 UR - https://m2.mtmt.hu/api/publication/27123717 ID - 27123717 LA - English DB - MTMT ER - TY - JOUR AU - Ristic, Gorica AU - Tsou, Wei-Ling AU - Guzi, Ermal AU - Kanack, Adam J AU - Scaglione, Kenneth Matthew AU - Todi, Sokol V TI - USP5 Is Dispensable for Monoubiquitin Maintenance in Drosophila JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 291 PY - 2016 IS - 17 SP - 9161 EP - 9172 PG - 12 SN - 0021-9258 DO - 10.1074/jbc.M115.703504 UR - https://m2.mtmt.hu/api/publication/25792644 ID - 25792644 LA - English DB - MTMT ER - TY - JOUR AU - Deák, Péter AU - Boros, Imre Miklós TI - Ubiquitylation: its role and medical significance JF - ACTA BIOLOGICA SZEGEDIENSIS J2 - ACTA BIOL SZEGED VL - 59 PY - 2015 IS - Suppl 2 SP - 261 EP - 273 PG - 13 SN - 1588-385X UR - https://m2.mtmt.hu/api/publication/2961801 ID - 2961801 LA - English DB - MTMT ER -