1 Supporting Information for Real-Time Tracking of Complex
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UBE2D3 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50Ul [email protected] 100 Ul √ √ Web
TD2261 UBE2D3 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL √ √ Web www.ab-mart.com.cn Description: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys- 22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. -
The HECT Domain Ubiquitin Ligase HUWE1 Targets Unassembled Soluble Proteins for Degradation
OPEN Citation: Cell Discovery (2016) 2, 16040; doi:10.1038/celldisc.2016.40 ARTICLE www.nature.com/celldisc The HECT domain ubiquitin ligase HUWE1 targets unassembled soluble proteins for degradation Yue Xu1, D Eric Anderson2, Yihong Ye1 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA; 2Advanced Mass Spectrometry Core Facility, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA In eukaryotes, many proteins function in multi-subunit complexes that require proper assembly. To maintain complex stoichiometry, cells use the endoplasmic reticulum-associated degradation system to degrade unassembled membrane subunits, but how unassembled soluble proteins are eliminated is undefined. Here we show that degradation of unassembled soluble proteins (referred to as unassembled soluble protein degradation, USPD) requires the ubiquitin selective chaperone p97, its co-factor nuclear protein localization protein 4 (Npl4), and the proteasome. At the ubiquitin ligase level, the previously identified protein quality control ligase UBR1 (ubiquitin protein ligase E3 component n-recognin 1) and the related enzymes only process a subset of unassembled soluble proteins. We identify the homologous to the E6-AP carboxyl terminus (homologous to the E6-AP carboxyl terminus) domain-containing protein HUWE1 as a ubiquitin ligase for substrates bearing unshielded, hydrophobic segments. We used a stable isotope labeling with amino acids-based proteomic approach to identify endogenous HUWE1 substrates. Interestingly, many HUWE1 substrates form multi-protein com- plexes that function in the nucleus although HUWE1 itself is cytoplasmically localized. Inhibition of nuclear entry enhances HUWE1-mediated ubiquitination and degradation, suggesting that USPD occurs primarily in the cytoplasm. -
Diphenhydramine Hydrochloride (CASRN 147-24-0) in F344/N Rats
NATIONAL TOXICOLOGY PROGRAM Technical Report Series No. 355 TOXICOLOGY AND CARCINOGENESIS STUDIES OF DIPHENHYDRAMINE HYDROCHLORIDE (CAS NO. 147-24-0) IN F344/N RATS AND B6C3F1 MICE (FEED STUDIES) LJ.S. DEPARTMENT OF HEALTH AND HUMAN SERVICES Public Health Service National Institutes of Health NTP ‘TECHNICAL REPORT ON THE TOXICOLOGY AND CARCINOGENESIS STUDIES OF DIPHENHYDRAMINE HYDROCHLORIDE (CAS NO. 147-24-0) IN F344/N RATS AND B6C3F1 MICE (FEED STUDIES) R. Melnick, Ph.D., Study Scientist NATIONAL TOXICOLOGY PROGRAM P.O. Box 12233 Research Triangle Park, NC 27709 September 1989 NTP TR 355 NIH Publication No. 89-2810 U.S. DEPARTMENT OF HEALTH AND HUMAN SERVICES Public Health Service National Institutes of Health CONTENTS PAGE ABSTRACT ................................................................ 3 EXPLANATION OF LEVELS OF EVIDENCE OF CARCINOGENIC ACTIVITY .................. 6 CONTRIBUTORS ............................................................ 7 PEERREVIEWPANEL ........................................................ 8 SUMMARY OF PEER REVIEW COMMENTS ......................................... 9 I. INTRODUCTION ........................................................ 11 I1. MATERIALS AND METHODS .............................................. 21 III. RESULTS ............................................................. 35 RATS ............................................................. 36 MICE ............................................................. 45 GENETIC TOXICOLOGY ............................................... 53 IV. -
Defining Functional Interactions During Biogenesis of Epithelial Junctions
ARTICLE Received 11 Dec 2015 | Accepted 13 Oct 2016 | Published 6 Dec 2016 | Updated 5 Jan 2017 DOI: 10.1038/ncomms13542 OPEN Defining functional interactions during biogenesis of epithelial junctions J.C. Erasmus1,*, S. Bruche1,*,w, L. Pizarro1,2,*, N. Maimari1,3,*, T. Poggioli1,w, C. Tomlinson4,J.Lees5, I. Zalivina1,w, A. Wheeler1,w, A. Alberts6, A. Russo2 & V.M.M. Braga1 In spite of extensive recent progress, a comprehensive understanding of how actin cytoskeleton remodelling supports stable junctions remains to be established. Here we design a platform that integrates actin functions with optimized phenotypic clustering and identify new cytoskeletal proteins, their functional hierarchy and pathways that modulate E-cadherin adhesion. Depletion of EEF1A, an actin bundling protein, increases E-cadherin levels at junctions without a corresponding reinforcement of cell–cell contacts. This unexpected result reflects a more dynamic and mobile junctional actin in EEF1A-depleted cells. A partner for EEF1A in cadherin contact maintenance is the formin DIAPH2, which interacts with EEF1A. In contrast, depletion of either the endocytic regulator TRIP10 or the Rho GTPase activator VAV2 reduces E-cadherin levels at junctions. TRIP10 binds to and requires VAV2 function for its junctional localization. Overall, we present new conceptual insights on junction stabilization, which integrate known and novel pathways with impact for epithelial morphogenesis, homeostasis and diseases. 1 National Heart and Lung Institute, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK. 2 Computing Department, Imperial College London, London SW7 2AZ, UK. 3 Bioengineering Department, Faculty of Engineering, Imperial College London, London SW7 2AZ, UK. 4 Department of Surgery & Cancer, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK. -
Role of Dietary Histidine in the Prevention of Obesity and Metabolic Syndrome
Open access Editorial Open Heart: first published as 10.1136/openhrt-2017-000676 on 1 July 2018. Downloaded from Role of dietary histidine in the prevention of obesity and metabolic syndrome James J DiNicolantonio,1 Mark F McCarty,2 James H OKeefe 1 To cite: DiNicolantonio JJ, HISTIDINE SUPPLEMENTATION AMELIORATES histidine dose dependently increases hypo- McCarty MF, OKeefe JH. Role of METABOLIC SYNDROME thalamic levels of histamine as well as hypo- dietary histidine in the prevention of obesity and A recent Chinese supplementation study, in thalamic activity of histidine decarboxylase, metabolic syndrome. Open Heart which obese middle-aged women diagnosed the enzyme which converts histidine to hista- 10 2018;5:e000676. doi:10.1136/ with metabolic syndrome received 12 weeks mine. Such administration also inhibits food openhrt-2017-000676 of supplemental histidine (2 g, twice daily) or consumption—an effect that is blocked in matching placebo, achieved remarkable find- animals pretreated with an irreversible inhib- 1 Accepted 24 April 2018 ings. Insulin sensitivity improved significantly itor of histidine decarboxylase. in the histidine-supplemented subjects, and Neuronal histamine release in the hypo- this may have been partially attributable to thalamus is subject to feedback regulation loss of body fat. Body mass index (BMI), waist by presynaptic H3 receptors. In rodent circumference and body fat declined in the studies, antagonists and inverse agonists for histidine-supplemented group relative to the these receptors have been shown to mark- placebo group; the average fat loss in the histi- edly amplify hypothalamic histamine levels, dine group was a robust 2.71 kg. Markers of suppress feeding, decrease body weight and systemic inflammation such as serum tumour enhance metabolic rate.11–15 Such agents may necrosis factor-alpha (TNF-α) and inter- have clinical potential for managing obesity. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Potential Microrna-Related Targets in Clearance Pathways of Amyloid-Β
Madadi et al. Cell Biosci (2019) 9:91 https://doi.org/10.1186/s13578-019-0354-3 Cell & Bioscience REVIEW Open Access Potential microRNA-related targets in clearance pathways of amyloid-β: novel therapeutic approach for the treatment of Alzheimer’s disease Soheil Madadi1, Heidi Schwarzenbach2, Massoud Saidijam3, Reza Mahjub4 and Meysam Soleimani1* Abstract Imbalance between amyloid-beta (Aβ) peptide synthesis and clearance results in Aβ deregulation. Failure to clear these peptides appears to cause the development of Alzheimer’s disease (AD). In recent years, microRNAs have become established key regulators of biological processes that relate among others to the development and progres- sion of neurodegenerative diseases, such as AD. This review article gives an overview on microRNAs that are involved in the Aβ cascade and discusses their inhibitory impact on their target mRNAs whose products participate in Aβ clear- ance. Understanding of the mechanism of microRNA in the associated signal pathways could identify novel therapeu- tic targets for the treatment of AD. Keywords: Ubiquitin–proteasome system, Autophagy, Aβ-degrading proteases, BBB transporters, Phagocytosis, Heat shock proteins, microRNAs Introduction stage, APP is cleaved to non-toxic proteins by α-secretase Alzheimer’s disease (AD)—the most common form of [6]. Aβ has two major forms: Aβ40 and Aβ42, which are dementia—is a devastating diagnosis that accounts for 40 and 42 amino acid-long fragments, respectively. Since 93,541 deaths in the United States in 2014 [1]. Clinical Aβ42 is more hydrophobic than Aβ40, it is more prone to manifestation of AD is often a loss of memory and cog- aggregate and scafold for oligomeric and fbrillar forms nitive skills. -
UBE2E2 Antibody Cat
UBE2E2 Antibody Cat. No.: 29-870 UBE2E2 Antibody Antibody used in WB on recombin ant protein at: 1:500 (Lanes: 1: 40ng HIS- UBE2D1 protein, 2: 40ng HIS- UBE2D2 protein, 3: 40ng HIS- UBE2D3 proteinm, 4: 40ng HIS- UBE2D4 protein, 5: 40ng HIS- UBE2E1 protein, 6: Antibody used in WB on Human Jurkat 0.125 ug/ml. 40ng HIS- UBE2E2 protein, 7: 40ng HIS- UBE2E3 protein, 8: 40ng HIS- UBE2K protein, 9: 40ng HIS- UBE2L3 protein, 10: 40ng HIS- UBE2N protein, 11: 40ng HIS- UBE2V1 protein, 12: 40ng HIS- UBE2V2 protein.). September 24, 2021 1 https://www.prosci-inc.com/ube2e2-antibody-29-870.html Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Dog, Human, Mouse, Rat Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human UBE2E2. TESTED APPLICATIONS: ELISA, IHC, WB UBE2E2 antibody can be used for detection of UBE2E2 by ELISA at 1:1562500. UBE2E2 APPLICATIONS: antibody can be used for detection of UBE2E2 by western blot at 0.125 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000. POSITIVE CONTROL: 1) Cat. No. 1205 - Jurkat Cell Lysate PREDICTED MOLECULAR 22 kDa WEIGHT: Properties PURIFICATION: Antibody is purified by peptide affinity chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% BUFFER: sucrose. CONCENTRATION: batch dependent For short periods of storage (days) store at 4˚C. For longer periods of storage, store STORAGE CONDITIONS: UBE2E2 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. -
Convenient Preparation of Poly(L-Histidine) by the Direct Polymerization of L-Histidine Or Nim Benzyl-L-Histidine with Diphenylphosphoryl Azide
Polymer Journal, Vol. 13, No. 12, pp 1151-1154 (1981) SHORT COMMUNICATION Convenient Preparation of Poly(L-histidine) by the Direct Polymerization of L-Histidine or Nim_Benzyl-L-histidine with Diphenylphosphoryl Azide Takumi NARUSE, Bun-ichiro NAKAJIMA, Akihiro TSUTSUMI, and Norio NISHI Department of Polymer Science, Faculty of Science, Hokkaido University, Nishi 8-chome, Kita 10-jo, Kita-ku, Sapporo 060, Japan. (Received August 14, 1981) KEY WORDS Polymerization I Diphenylphosphoryl Azide (DPPA) I L- Histidine I N'm-Benzyl-L-histidine I Poly(L-histidine) I Poly(N'm-benzyl-L histidine) I IR Spectrum I 13C NMR Spectrum I Intrinsic Viscosity I Poly(L-histidine) is a very interesting poly(a histidine) by the polymerization of L-histidine with amino acid) as a synthetic functional polymer or as iodine-phosphonic acid esters was unsuccessful. The a model for the functional biopolymer such as simplification of the synthetic route for poly(L enzymes. It is known, however, that poly(L histidine) is still necessary. histidine) can not be prepared by the Fuchs Diphenylphosphoryl azide (DPPA) has been used Farthing method 1 which is very popular for prepar as a convenient reagent for racemization-free pep ing poly(a-amino acid)s. A synthetic route with tide synthesis, since it was synthesized by Shioiri et several steps involving the synthesis of NCA (a a!. in 1972.6 Recently, we reported that this reagent amino acid N-carboxyanhydride) by the rather can also be used successfully for the polymerization classical Leuchs method/ have been used for the of amino acids or peptides. -
UBE2C Is Upregulated by Estrogen and Promotes Epithelial–Mesenchymal Transition Via P53 in Endometrial Cancer
Published OnlineFirst October 29, 2019; DOI: 10.1158/1541-7786.MCR-19-0561 MOLECULAR CANCER RESEARCH | CANCER GENES AND NETWORKS UBE2C Is Upregulated by Estrogen and Promotes Epithelial–Mesenchymal Transition via p53 in Endometrial Cancer Yan Liu1, Rong Zhao1, Shuqi Chi1, Wei Zhang1, Chengyu Xiao1, Xing Zhou1, Yingchao Zhao2, and Hongbo Wang1 ABSTRACT ◥ Ubiquitin-conjugating enzyme E2C (UBE2C) plays important inhibited endometrial cancer cell proliferation, migration, invasion, roles in tumor progression; nevertheless, its function in endometrial and epithelial–mesenchymal transition (EMT), whereas UBE2C cancer remains unclear. This study elucidated the impact of UBE2C overexpression exerted the opposite effects. UBE2C downregulation on endometrial cancer and its underlying mechanism. Human increased p53 and its downstream p21 expression, with p53 over- endometrial cancer and normal endometrial tissues were acquired expression reversing the EMT-promoting effects of UBE2C. UBE2C from patients at Wuhan Union Hospital and UBE2C expression was enhanced p53 ubiquitination to facilitate its degradation in endo- detected by Western blotting and qRT-PCR. Endometrial cancer metrial cancer cells. Estradiol (E2) induced UBE2C expression via cells were transfected with a UBE2C overexpression plasmid or estrogen receptor a, which binds directly to the UBE2C promoter UBE2C-specific short hairpin RNA (shRNA) to up- or downregu- element. Silencing of UBE2C inhibited E2-promoted migration, late UBE2C expression, respectively. CCK8 and transwell assays -
Title Structure of the Human Histamine H1 Receptor Complex With
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Kyoto University Research Information Repository Structure of the human histamine H1 receptor complex with Title doxepin. Shimamura, Tatsuro; Shiroishi, Mitsunori; Weyand, Simone; Tsujimoto, Hirokazu; Winter, Graeme; Katritch, Vsevolod; Author(s) Abagyan, Ruben; Cherezov, Vadim; Liu, Wei; Han, Gye Won; Kobayashi, Takuya; Stevens, Raymond C; Iwata, So Citation Nature (2011), 475(7354): 65-70 Issue Date 2011-07-07 URL http://hdl.handle.net/2433/156845 © 2011 Nature Publishing Group, a division of Macmillan Right Publishers Limited. Type Journal Article Textversion author Kyoto University Title: Structure of the human histamine H1 receptor in complex with doxepin. Authors Tatsuro Shimamura 1,2,3*, Mitsunori Shiroishi 1,2,4*, Simone Weyand 1,5,6, Hirokazu Tsujimoto 1,2, Graeme Winter 6, Vsevolod Katritch7, Ruben Abagyan7, Vadim Cherezov3, Wei Liu3, Gye Won Han3, Takuya Kobayashi 1,2‡, Raymond C. Stevens3‡and So Iwata1,2,5,6,8‡ 1. Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. 2. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-Ku, Kyoto 606-8501, Japan. 3. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. 4. Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. 5. Division of Molecular Biosciences, Membrane Protein Crystallography Group, Imperial College, London SW7 2AZ, UK. 6. Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Didcot, Oxfordshire OX11 0DE, UK. -
Characterization of the Cellular Network of Ubiquitin Conjugating and Ligating Enzymes Ewa Katarzyna Blaszczak
Characterization of the cellular network of ubiquitin conjugating and ligating enzymes Ewa Katarzyna Blaszczak To cite this version: Ewa Katarzyna Blaszczak. Characterization of the cellular network of ubiquitin conjugating and ligating enzymes. Cellular Biology. Université Rennes 1, 2015. English. NNT : 2015REN1S116. tel-01547616 HAL Id: tel-01547616 https://tel.archives-ouvertes.fr/tel-01547616 Submitted on 27 Jun 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ANNÉE 2015 THÈSE / UNIVERSITÉ DE RENNES 1 sous le sceau de l’Université Européenne de Bretagne pour le grade de DOCTEUR DE L’UNIVERSITÉ DE RENNES 1 Mention : BIOLOGIE École doctorale Vie-Agro-Santé présentée par Ewa Katarzyna Blaszczak Préparée à l’unité de recherche UMR 6290, IGDR Institut de Génétique et Développement de Rennes Université Rennes 1 Thèse soutenue à Rennes le 26.06.2015 Characterization of devant le jury composé de : Aude ECHALIER-GLAZER the cellular network Maître de conférence University of Leicester / rapporteur of ubiquitin Lionel PINTARD Directeur de recherche