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Human Prion-Like Proteins and Their Relevance in Disease
ADVERTIMENT. Lʼaccés als continguts dʼaquesta tesi queda condicionat a lʼacceptació de les condicions dʼús establertes per la següent llicència Creative Commons: http://cat.creativecommons.org/?page_id=184 ADVERTENCIA. El acceso a los contenidos de esta tesis queda condicionado a la aceptación de las condiciones de uso establecidas por la siguiente licencia Creative Commons: http://es.creativecommons.org/blog/licencias/ WARNING. The access to the contents of this doctoral thesis it is limited to the acceptance of the use conditions set by the following Creative Commons license: https://creativecommons.org/licenses/?lang=en Universitat Autònoma de Barcelona Departament de Bioquímica i Biologia Molecular Institut de Biotecnologia i Biomedicina HUMAN PRION-LIKE PROTEINS AND THEIR RELEVANCE IN DISEASE Doctoral thesis presented by Cristina Batlle Carreras for the degree of PhD in Biochemistry, Molecular Biology and Biomedicine from the Universitat Autònoma de Barcelona. The work described herein has been performed in the Department of Biochemistry and Molecular Biology and in the Institute of Biotechnology and Biomedicine, supervised by Prof. Salvador Ventura i Zamora. Cristina Batlle Carreras Prof. Salvador Ventura i Zamora Bellaterra, 2020 Protein Folding and Conformational Diseases Lab. This work was financed with the fellowship “Formación de Profesorado Universitario” by “Ministerio de Ciencia, Innovación y Universidades”. This work is licensed under a Creative Commons Attributions-NonCommercial-ShareAlike 4.0 (CC BY-NC- SA 4.0) International License. The extent of this license does not apply to the copyrighted publications and images reproduced with permission. (CC BY-NC-SA 4.0) Batlle, Cristina: Human prion-like proteins and their relevance in disease. Doctoral Thesis, Universitat Autònoma de Barcelona (2020) English summary ENGLISH SUMMARY Prion-like proteins have attracted significant attention in the last years. -
Development of VHH- and Antibody- Based
Development of VHH- and Antibody- based Imaging and Diagnostic Tools by Zeyang Li Bachelor of Science in Biochemistry University of Wisconsin-Madison, WI, 2011 Submitted to the Department of Chemistry In Partial Fulfilment of the requirement for the Degree of Doctor of Philosophy at the Massachusetts Institute of Technology June 2018 2018 Massachusetts Institute of Technology All rights reserved Signature redacted Signature of Author........ Department of Chemistry 21 May 2018 Certified by.....................Signature redacted Hidde Ploegh OF TECHNOLOGY Senior Investigator Program in Cellular and Molecular Medicine JUN 2 0 Z018 At Boston Children's Hospital LIBRARIES ARCHIVES Signature redacted A cce pted by ....... .......................................... Robert W. Field Haslam and Dewey Professor of Chemistry Chairman, Departmental Committee for Graduate students This doctoral thesis has been examined by a committee of the Department of Chemistry as follows: ............................Signature redacted ----- Barbara Imperiali Class of 1922 Professor of Biology and Chemistry MacVicar Faculty Fellow Thesis Committee Chair Signature redacted Hidde Ploegh Senior Investigator Program in Cellular and Molecular Medicine Boston Children's Hospital / Z" Thes;Supervisor Signature redacted Bradley L. Pentelute Pfizer-Laubach Career Development Professor of Chemistry Abstract The immune system distinguishes self from non-self to combat pathogenic incursions. Evasion tactics deployed by viruses, microbes, or malignant cells may impede an adequate response. In such cases, therapeutic interventions aid in the elimination of pathogens and the restoration of physiological homeostasis. A major road block in the development of such therapies is the reliance on imperfect detection methods to identify site(s) of infection, or to monitor immune cell recruitment to sites of infection or inflammation in vivo. -
Unique Epitopes on Cεmx in Ige–B Cell Receptors Are Potentially Applicable for Targeting Ige-Committed B Cells
Unique Epitopes on CεmX in IgE−B Cell Receptors Are Potentially Applicable for Targeting IgE-Committed B Cells This information is current as Jiun-Bo Chen, Pheidias C. Wu, Alfur Fu-Hsin Hung, of October 1, 2021. Chia-Yu Chu, Tsen-Fang Tsai, Hui-Ming Yu, Hwan-You Chang and Tse Wen Chang J Immunol 2010; 184:1748-1756; Prepublished online 18 January 2010; doi: 10.4049/jimmunol.0902437 http://www.jimmunol.org/content/184/4/1748 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2010/01/13/jimmunol.090243 Material 7.DC1 http://www.jimmunol.org/ References This article cites 52 articles, 19 of which you can access for free at: http://www.jimmunol.org/content/184/4/1748.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on October 1, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2010 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Unique Epitopes on C«mX in IgE–B Cell Receptors Are Potentially Applicable for Targeting IgE-Committed B Cells Jiun-Bo Chen,*,† Pheidias C. -
S1 Supplemental Materials Supplemental Methods Supplemental Figure 1. Immune Phenotype of Mcd19 Targeted CAR T and Dose Titratio
Supplemental Materials Supplemental Methods Supplemental Figure 1. Immune phenotype of mCD19 targeted CAR T and dose titration of in vivo efficacy. Supplemental Figure 2. Gene expression of fluorescent-protein tagged CAR T cells. Supplemental Figure 3. Fluorescent protein tagged CAR T cells function similarly to non-tagged counterparts. Supplemental Figure 4. Transduction efficiency and immune phenotype of mCD19 targeted CAR T cells for survival study (Figure 2D). Supplemental Figure 5. Transduction efficiency and immune phenotype of CAR T cells used in irradiated CAR T study (Fig. 3B-C). Supplemental Figure 6. Differential gene expression of CD4+ m19-humBBz CAR T cells. Supplemental Figure 7. CAR expression and CD4/CD8 subsets of human CD19 targeted CAR T cells for Figure 5E-G. Supplemental Figure 8. Transduction efficiency and immune phenotype of mCD19 targeted wild type (WT) and TRAF1-/- CAR T cells used for in vivo study (Figure 6D). Supplemental Figure 9. Mutated m19-musBBz CAR T cells have increased NF-κB signaling, improved cytokine production, anti-apoptosis, and in vivo function. Supplemental Figure 10. TRAF and CAR co-expression in human CD19-targeted CAR T cells. Supplemental Figure 11. TRAF2 over-expressed h19BBz CAR T cells show similar in vivo efficacy to h19BBz CAR T cells in an aggressive leukemia model. S1 Supplemental Table 1. Probesets increased in m19z and m1928z vs m19-musBBz CAR T cells. Supplemental Table 2. Probesets increased in m19-musBBz vs m19z and m1928z CAR T cells. Supplemental Table 3. Probesets differentially expressed in m19z vs m19-musBBz CAR T cells. Supplemental Table 4. Probesets differentially expressed in m1928z vs m19-musBBz CAR T cells. -
World Premier International Research Center Initiative (WPI) Executive Summary (For Extension Application Screening)
World Premier International Research Center Initiative (WPI) Executive Summary (For Extension application screening) Host Institution Osaka University Host Institution Head Toshio Hirano Research Center Immunology Frontier Research Center Center Director Shizuo Akira A. Progress Report of the WPI Center I. Summary In 2007, IFReC set out to integrate imaging and informatics technologies with immunology (IFReC’s three Is), aiming to unveil spatio-temporal and collective behavior of immune cells and molecules in vivo for comprehensive understanding of immune dynamism. While overcoming intellectual and technical perplexities encountered at early stages in collaboration of researchers in different fields or with different backgrounds, through strategical establishment of platforms for such interdisciplinary research, our all-out effort has ultimately resulted in a number of immunologically important discoveries as well as publication of more than 800 papers with an average number of citations of 29.2. Above all, new insight into the immune-regulating mechanism is the foremost achievement attained so fa r, w hich is expected to produce new seeds of clinical immunology for diagnosis, therapy and prevention of immune-related diseases. II. Items 1. Overall Image of Your Center IFReC has become a globally visible stronghold of top-class immunologists, and imaging and informatics researchers, rallying to comprehensively understand immune dynamism, while advancing frontier researches in their own fields. Considering the spacious laboratories, animal resource facilities, and instalment of highly advanced instruments, the entire research environment of IFReC is of the highest international level. The research support/administration system is also arranged for smooth and effective operation, enabling IFReC researchers to concentrate on research as well as supporting overseas researchers. -
Proteogenomic Analysis of Inhibitor of Differentiation 4 (ID4) in Basal-Like Breast Cancer Laura A
Baker et al. Breast Cancer Research (2020) 22:63 https://doi.org/10.1186/s13058-020-01306-6 RESEARCH ARTICLE Open Access Proteogenomic analysis of Inhibitor of Differentiation 4 (ID4) in basal-like breast cancer Laura A. Baker1,2, Holly Holliday1,2†, Daniel Roden1,2†, Christoph Krisp3,4†, Sunny Z. Wu1,2, Simon Junankar1,2, Aurelien A. Serandour5, Hisham Mohammed5, Radhika Nair6, Geetha Sankaranarayanan5, Andrew M. K. Law1,2, Andrea McFarland1, Peter T. Simpson7, Sunil Lakhani7,8, Eoin Dodson1,2, Christina Selinger9, Lyndal Anderson9,10, Goli Samimi11, Neville F. Hacker12, Elgene Lim1,2, Christopher J. Ormandy1,2, Matthew J. Naylor13, Kaylene Simpson14,15, Iva Nikolic14, Sandra O’Toole1,2,9,10, Warren Kaplan1, Mark J. Cowley1,2, Jason S. Carroll5, Mark Molloy3 and Alexander Swarbrick1,2* Abstract Background: Basal-like breast cancer (BLBC) is a poorly characterised, heterogeneous disease. Patients are diagnosed with aggressive, high-grade tumours and often relapse with chemotherapy resistance. Detailed understanding of the molecular underpinnings of this disease is essential to the development of personalised therapeutic strategies. Inhibitor of differentiation 4 (ID4) is a helix-loop-helix transcriptional regulator required for mammary gland development. ID4 is overexpressed in a subset of BLBC patients, associating with a stem-like poor prognosis phenotype, and is necessary for the growth of cell line models of BLBC through unknown mechanisms. Methods: Here, we have defined unique molecular insights into the function of ID4 in BLBC and the related disease high-grade serous ovarian cancer (HGSOC), by combining RIME proteomic analysis, ChIP-seq mapping of genomic binding sites and RNA-seq. -
Cell Biology from an Immune Perspective in This Lecture We Will
Harvard-MIT Division of Health Sciences and Technology HST.176: Cellular and Molecular Immunology Course Director: Dr. Shiv Pillai Cell Biology from an Immune Perspective In this lecture we will very briefly review some aspects of cell biology which are required as background knowledge in order to understand how the immune system works. These will include: 1. A brief overview of protein trafficking 2. Signal transduction 3. The cell cycle Some of these issues will be treated in greater depth in later lectures. Protein Trafficking/The Secretory Pathway: From an immune perspective the secretory compartment and structures enclosed by vesicles are “seen” in different ways from proteins that reside in the cytosol or the nucleus. We will briefly review the secretory and endocytic pathways and discuss the biogenesis of membrane proteins. Some of the issues that will be discussed are summarized in Figures 1-3. Early endosomes Late endosomes Lysosomes Golgi Vesiculo-Tubular Compartment ER Figure 1. An overview of the secretory pathway Early endosomes Late endosomes Multivesicular and multilamellar bodies Golgi ER Proteasomes Figure 2. Protein degradation occurs mainly in lysosomes and proteasomes Proteins that enter the cell from the environment are primarily degraded in lysosomes. Most cytosolic and nuclear proteins are degraded in organelles called proteasomes. Intriguingly these two sites of degradation are each functionally linked to distinct antigen presentation pathways, different kinds of MHC molecules and the activation of different categories of T cells. Integral membrane proteins maybe inserted into the membrane in a number of ways, the two most common of these ways being considered in Figure 3. -
Optimized Fluorescent Labeling to Identify Memory B Cells Specific for Neisseria Meningitidis Serogroup B Vaccine Antigens Ex Vivo
Optimized fluorescent labeling to identify memory B cells specific for Neisseria meningitidis serogroup B vaccine antigens ex vivo The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Nair, Nitya, Ludovico Buti, Elisa Faenzi, Francesca Buricchi, Sandra Nuti, Chiara Sammicheli, Simona Tavarini, et al. “ Optimized Fluorescent Labeling to Identify Memory B Cells Specific for Neisseria Meningitidis Serogroup B Vaccine Antigens Ex Vivo .” Immun. Inflamm. Dis. 1, no. 1 (October 2013): 3–13. As Published http://dx.doi.org/10.1002/iid3.3 Publisher Wiley Blackwell Version Final published version Citable link http://hdl.handle.net/1721.1/92523 Terms of Use Creative Commons Attribution Detailed Terms http://creativecommons.org/licenses/by/3.0/ ORIGINAL RESEARCH Optimized fluorescent labeling to identify memory B cells specific for Neisseria meningitidis serogroup B vaccine antigens ex vivo Nitya Nair1†, Ludovico Buti1,2‡, Elisa Faenzi1, Francesca Buricchi1, Sandra Nuti1, Chiara Sammicheli1, Simona Tavarini1, Maximilian W.L. Popp2,3,4, Hidde Ploegh2,4, Francesco Berti1, Mariagrazia Pizza1, Flora Castellino1, Oretta Finco1, Rino Rappuoli1, Giuseppe Del Giudice1, Grazia Galli1, & Monia Bardelli1 1Novartis Vaccines & Diagnostics, Siena, Italy 2Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 3University of Rochester, School of Medicine & Dentistry, Rochester, New York 4Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts Keywords Abstract Antigen-specific memory B cells, flow cytometry, Neisseria meningitidis MenB, Antigen-specific memory B cells generate anamnestic responses and high affinity sortagging, vaccination antibodies upon re-exposure to pathogens. Attempts to isolate rare antigen- specific memory B cells for in-depth functional analysis at the single-cell level have Correspondence been hindered by the lack of tools with adequate sensitivity. -
Tyr1 Phosphorylation Promotes Phosphorylation of Ser2 on the C-Terminal Domain
1 Tyr1 phosphorylation promotes phosphorylation of Ser2 on the C-terminal domain 2 of eukaryotic RNA polymerase II by P-TEFb 3 Joshua E. Mayfield1† *, Seema Irani2*, Edwin E. Escobar3, Zhao Zhang4, Nathanial T. 4 Burkholder1, Michelle R. Robinson3, M. Rachel Mehaffey3, Sarah N. Sipe3,Wanjie Yang1, 5 Nicholas A. Prescott1, Karan R. Kathuria1, Zhijie Liu4, Jennifer S. Brodbelt3, Yan Zhang1,5 6 1 Department of Molecular Biosciences, 2Department of Chemical Engineering, 7 3 Department of Chemistry and 5 Institute for Cellular and Molecular Biology, University of 8 Texas, Austin 9 4 Department of Molecular Medicine, Institute of Biotechnology, University of Texas 10 Health Science Center at San Antonio 11 †Current Address: Department of Pharmacology, University of California, San Diego, La 12 Jolla 13 * These authors contributed equally to this paper. 14 Correspondence: Yan Zhang ([email protected]) 15 16 1 17 Summary 18 The Positive Transcription Elongation Factor b (P-TEFb) phosphorylates 19 Ser2 residues of C-terminal domain (CTD) of the largest subunit (RPB1) of RNA 20 polymerase II and is essential for the transition from transcription initiation to 21 elongation in vivo. Surprisingly, P-TEFb exhibits Ser5 phosphorylation activity in 22 vitro. The mechanism garnering Ser2 specificity to P-TEFb remains elusive and 23 hinders understanding of the transition from transcription initiation to elongation. 24 Through in vitro reconstruction of CTD phosphorylation, mass spectrometry 25 analysis, and chromatin immunoprecipitation sequencing (ChIP-seq) analysis, we 26 uncover a mechanism by which Tyr1 phosphorylation directs the kinase activity of 27 P-TEFb and alters its specificity from Ser5 to Ser2. -
Adracalin (AAAS) Rabbit Polyclonal Antibody – TA349454 | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA349454 Adracalin (AAAS) Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: IHC, WB Recommended Dilution: ELISA: 1000-2000, WB: 200-1000, IHC: 50-200 Reactivity: Human, Mouse Host: Rabbit Isotype: IgG Clonality: Polyclonal Immunogen: Fusion protein of human AAAS Formulation: pH7.4 PBS, 0.05% NaN3, 40% Glyceroln Concentration: lot specific Purification: Antigen affinity purification Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 60 kDa Gene Name: aladin WD repeat nucleoporin Database Link: NP_056480 Entrez Gene 223921 MouseEntrez Gene 8086 Human Q9NRG9 Background: The protein encoded by this gene is a member of the WD-repeat family of regulatory proteins and may be involved in normal development of the peripheral and central nervous system. The encoded protein is part of the nuclear pore complex and is anchored there by NDC1. Defects in this gene are a cause of achalasia-addisonianism-alacrima syndrome (AAAS), also called triple-A syndrome or Allgrove syndrome. Two transcript variants encoding different isoforms have been found for this gene. Synonyms: AAA; AAASb; ADRACALA; ADRACALIN; ALADIN; GL003 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 -