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Book: Viruses, vaccines, and antivirals

Chari, Raj S. / Rozas, Isabel

why politics matters

(Viral politics ; 1)

2022

Author's details	Raj Chari, Isabel Rozas
Series title	Viral politics ; 1
Collection
Keywords	COVID-19 ; Pandemics ; Antivirals ; Viral Politics ; Vaccines ; Pandemie ; Virale Politik ; Impfungen ; Antiviral ; Virustatikum
Language	English
Size	X, 129 Seiten, 10 Illustrationen, 23 cm x 15.5 cm
Publisher	De Gruyter
Publishing place	Berlin, Boston
Publishing country	Germany
Document type	Book
HBZ-ID	HT021221743
ISBN	978-3-11-074358-6 ; 978-3-11-076484-0 ; 9783110743722 ; 9783110743609 ; 3-11-074358-2 ; 3-11-076484-9 ; 3110743728 ; 3110743604
Database	Catalogue ZB MED Medicine, Health

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Shelf mark	Loan status	Location
2022 A 201	available for loan (reading room)	Lesesaal EG

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Article: Disc Large Homolog 1 Is Critical for Early T Cell Receptor Micro Cluster Formation and Activation in Human T Cells.

Guha, June / Chari, Raj

Vaccines

2021 Volume 9, Issue 12

Abstract: T cell activation by antigen involves multiple sequential steps, including T cell receptor-microcluster TCR-(MC) formation, immunological synapse formation, and phosphorylation of mediators downstream of the TCR. The adaptor protein, Disc Large Homolog 1 ...

Abstract	T cell activation by antigen involves multiple sequential steps, including T cell receptor-microcluster TCR-(MC) formation, immunological synapse formation, and phosphorylation of mediators downstream of the TCR. The adaptor protein, Disc Large Homolog 1 (DLG1), is known to regulate proximal TCR signaling and, in turn, T cell activation, acting as a molecular chaperone that organizes specific kinases downstream of antigen recognition. In this study, we used knockdown and knockout technologies in human primary T cells and a human T cell line to demonstrate the role of DLG1 in proximal T cell signaling. High-end confocal microscopy was used for pictorial representation of T cell micro-clusters and colocalization studies. From all these studies, we could demonstrate that DLG1 functions even earlier than immunological synapse formation, to regulate T cell activation by promoting TCR-MC formation. Moreover, we found that DLG1 can act as a bridge between the TCR-ζ chain and ZAP70 while inhibiting binding of the phosphatase SHP1 to TCR-ζ. Together, these effects drive dysregulation of T cell activation in DLG1-deficient T cells. Overall, the activation and survival status of T cell is a critical determinant of effective vaccine response, and DLG1-mediated T cell signaling events can be a driving factor for improving vaccine-designing strategies.
Language	English
Publishing date	2021-12-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines9121446
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The ubiquitin ligase HUWE1 enhances WNT signaling by antagonizing destruction complex-mediated β-catenin degradation and through a mechanism independent of β-catenin stability.

McKenna, Joseph K / Wu, Yalan / Sonkusre, Praveen / Chari, Raj / Lebensohn, Andres M

bioRxiv : the preprint server for biology

2024

Abstract: WNT/β-catenin signaling is mediated by the transcriptional coactivator β-catenin (CTNNB1). CTNNB1 abundance is regulated by phosphorylation and proteasomal degradation promoted by a destruction complex composed of the scaffold proteins APC and AXIN1 or ... ...

Abstract	WNT/β-catenin signaling is mediated by the transcriptional coactivator β-catenin (CTNNB1). CTNNB1 abundance is regulated by phosphorylation and proteasomal degradation promoted by a destruction complex composed of the scaffold proteins APC and AXIN1 or AXIN2, and the kinases CSNK1A1 and GSK3A or GSK3B. Loss of CSNK1A1 increases CTNNB1 abundance, resulting in hyperactive WNT signaling. Previously, we demonstrated that the HECT domain ubiquitin ligase HUWE1 is necessary for hyperactive WNT signaling in HAP1 haploid human cells lacking CSNK1A1. Here, we investigate the mechanism underlying this requirement. In the absence of CSNK1A1, GSK3A/GSK3B still phosphorylated a fraction of CTNNB1, promoting its degradation. HUWE1 loss enhanced GSK3A/GSK3B-dependent CTNNB1 phosphorylation, further reducing CTNNB1 abundance. However, the reduction in CTNNB1 caused by HUWE1 loss was disproportionately smaller than the reduction in WNT target gene transcription. To test if the reduction in WNT signaling resulted from reduced CTNNB1 abundance alone, we engineered the endogenous
Language	English
Publishing date	2024-03-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.02.578552
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Generation of murine tumor models refractory to αPD-1/-L1 therapies due to defects in antigen processing/presentation or IFNγ signaling using CRISPR/Cas9.

Chariou, Paul L / Minnar, Christine M / Tandon, Mayank / Guest, Mary R / Chari, Raj / Schlom, Jeffrey / Gameiro, Sofia R

PloS one

2024 Volume 19, Issue 3, Page(s) e0287733

Abstract: Immune checkpoint blockade (ICB) targeting the programmed cell death protein 1 (PD-1) and its ligand 1 (PD-L1) fails to provide clinical benefit for most cancer patients due to primary or acquired resistance. Drivers of ICB resistance include tumor ... ...

Abstract	Immune checkpoint blockade (ICB) targeting the programmed cell death protein 1 (PD-1) and its ligand 1 (PD-L1) fails to provide clinical benefit for most cancer patients due to primary or acquired resistance. Drivers of ICB resistance include tumor antigen processing/presentation machinery (APM) and IFNγ signaling mutations. Thus, there is an unmet clinical need to develop alternative therapies for these patients. To this end, we have developed a CRISPR/Cas9 approach to generate murine tumor models refractory to PD-1/-L1 inhibition due to APM/IFNγ signaling mutations. Guide RNAs were employed to delete B2m, Jak1, or Psmb9 genes in ICB-responsive EMT6 murine tumor cells. B2m was deleted in ICB-responsive MC38 murine colon cancer cells. We report a detailed development and validation workflow including whole exome and Sanger sequencing, western blotting, and flow cytometry to assess target gene deletion. Tumor response to ICB and immune effects of gene deletion were assessed in syngeneic mice. This workflow can help accelerate the discovery and development of alternative therapies and a deeper understanding of the immune consequences of tumor mutations, with potential clinical implications.
MeSH term(s)	Animals ; Mice ; Antigen Presentation ; B7-H1 Antigen ; Cell Line, Tumor ; CRISPR-Cas Systems/genetics ; Programmed Cell Death 1 Receptor/genetics ; RNA, Guide, CRISPR-Cas Systems ; Signal Transduction
Chemical Substances	B7-H1 Antigen ; Programmed Cell Death 1 Receptor ; RNA, Guide, CRISPR-Cas Systems
Language	English
Publishing date	2024-03-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0287733
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book: Life after privatization

Chari, Raj

2015

Abstract: This book offers a refreshing and original theoretical conceptualization of what happened to state-owned enterprises after they were privatized from the late 1970s onwards. Some privatized firms have become today's European and global giants, 'Alphas', ... ...

Author's details	Raj Chari
Abstract	This book offers a refreshing and original theoretical conceptualization of what happened to state-owned enterprises after they were privatized from the late 1970s onwards. Some privatized firms have become today's European and global giants, 'Alphas', merging with or acquiring other firms, whereas other firms, 'Beta's, have been taken over by Alphas or other sectoral leaders. The book raises questions such as which privatized firms in the airline, automobile, and the electricity sectors in the UK, France, Germany, Italy and Spain are Alphas and Betas today? And why? Building on a variety of themes from both Political Science and Business Studies, it considers a comprehensive set of explanations both internal and external to the firm, to analysis why a firm may become an Alpha or a Beta. The evidence shows that while internal factors are important, the more external, political, factors are necessary and sufficient to explain why a firm becomes an Alpha or a Beta. This includes the impact of liberalization, the roles of states, and the actions of regulators that are lobbied by firms. Based on the evidence, Life After Privatization concludes with a novel inductive theory, which offers a significant step forward for social science scholars' and practitioners' understanding of the 'politics' businesses face in global markets
Keywords	Privatization ; Spanien ; Öffentliches Unternehmen ; Privatisierung ; Fluggesellschaft ; Kfz-Industrie ; Elektrizitätswirtschaft ; Großbritannien ; Frankreich ; Deutschland ; Italien
Language	English
Size	XIII, 289 S., graph. Darst.
Publisher	Oxford Univ. Press
Publishing place	Oxford u.a.
Document type	Book
ISBN	0199658315 ; 9780199658312
Database	ECONomics Information System

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Article ; Online: An engineered cell line with a hRpn1-attached handle to isolate proteasomes.

Negi, Hitendra / Osei-Amponsa, Vasty / Ibrahim, Bishoy / Evans, Christine N / Sullenberger, Catherine / Loncarek, Jadranka / Chari, Raj / Walters, Kylie J

The Journal of biological chemistry

2023 Volume 299, Issue 8, Page(s) 104948

Abstract: Regulated protein degradation in eukaryotes is performed by the 26S proteasome, which contains a 19-subunit regulatory particle (RP) that binds, processes, and translocates substrates to a 28-subunit hollow core particle (CP) where proteolysis occurs. In ...

Abstract	Regulated protein degradation in eukaryotes is performed by the 26S proteasome, which contains a 19-subunit regulatory particle (RP) that binds, processes, and translocates substrates to a 28-subunit hollow core particle (CP) where proteolysis occurs. In addition to its intrinsic subunits, myriad proteins interact with the proteasome transiently, including factors that assist and/or regulate its degradative activities. Efforts to identify proteasome-interacting components and/or to solve its structure have relied on over-expression of a tagged plasmid, establishing stable cell lines, or laborious purification protocols to isolate native proteasomes from cells. Here, we describe an engineered human cell line, derived from colon cancer HCT116 cells, with a biotin handle on the RP subunit hRpn1/PSMD2 (proteasome 26S subunit, non-ATPase 2) for purification of 26S proteasomes. A 75-residue sequence from Propionibacterium shermanii that is biotinylated in mammalian cells was added following a tobacco etch virus protease cut site at the C terminus of hRpn1. We tested and found that 26S proteasomes can be isolated from this modified HCT116 cell line by using a simple purification protocol. More specifically, biotinylated proteasomes were purified from the cell lysates by using neutravidin agarose resin and released from the resin following incubation with tobacco etch virus protease. The purified proteasomes had equivalent activity in degrading a model ubiquitinated substrate, namely ubiquitinated p53, compared to commercially available bovine proteasomes that were purified by fractionation. In conclusion, advantages of this approach to obtain 26S proteasomes over others is the simple purification protocol and that all cellular proteins, including the tagged hRpn1 subunit, remain at endogenous stoichiometry.
MeSH term(s)	Animals ; Cattle ; Humans ; Cell Line ; Cytoplasm/metabolism ; Mammals/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Ubiquitin/metabolism ; Cytological Techniques/methods
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Ubiquitin
Language	English
Publishing date	2023-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104948
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Beyond editing to writing large genomes.

Chari, Raj / Church, George M

Nature reviews. Genetics

2017 Volume 18, Issue 12, Page(s) 749–760

Abstract: Recent exponential advances in genome sequencing and engineering technologies have enabled an unprecedented level of interrogation into the impact of DNA variation (genotype) on cellular function (phenotype). Furthermore, these advances have also ... ...

Abstract	Recent exponential advances in genome sequencing and engineering technologies have enabled an unprecedented level of interrogation into the impact of DNA variation (genotype) on cellular function (phenotype). Furthermore, these advances have also prompted realistic discussion of writing and radically re-writing complex genomes. In this Perspective, we detail the motivation for large-scale engineering, discuss the progress made from such projects in bacteria and yeast and describe how various genome-engineering technologies will contribute to this effort. Finally, we describe the features of an ideal platform and provide a roadmap to facilitate the efficient writing of large genomes.
MeSH term(s)	Animals ; Gene Editing/methods ; Genetic Engineering/methods ; Genome ; Humans ; Nanotechnology/methods ; Plants/genetics ; Yeasts
Language	English
Publishing date	2017-08-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2035157-4
ISSN	1471-0064 ; 1471-0056
ISSN (online)	1471-0064
ISSN	1471-0056
DOI	10.1038/nrg.2017.59
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Article ; Online: Uncovering receptor-ligand interactions using a high-avidity CRISPR activation screening platform.

Yang, Liping / Sheets, Timothy P / Feng, Yang / Yu, Guojun / Bajgain, Pradip / Hsu, Kuo-Sheng / So, Daeho / Seaman, Steven / Lee, Jaewon / Lin, Ling / Evans, Christine N / Guest, Mary R / Chari, Raj / St Croix, Brad

Science advances

2024 Volume 10, Issue 7, Page(s) eadj2445

Abstract: The majority of clinically approved drugs target proteins that are secreted or cell surface bound. However, further advances in this area have been hindered by the challenging nature of receptor deorphanization, as there are still many secreted and cell- ... ...

Abstract	The majority of clinically approved drugs target proteins that are secreted or cell surface bound. However, further advances in this area have been hindered by the challenging nature of receptor deorphanization, as there are still many secreted and cell-bound proteins with unknown binding partners. Here, we developed an advanced screening platform that combines CRISPR-CAS9 guide-mediated gene activation (CRISPRa) and high-avidity bead-based selection. The CRISPRa platform incorporates serial enrichment and flow cytometry-based monitoring, resulting in substantially improved screening sensitivity for well-known yet weak interactions of the checkpoint inhibitor family. Our approach has successfully revealed that siglec-4 exerts regulatory control over T cell activation through a low affinity trans-interaction with the costimulatory receptor 4-1BB. Our highly efficient screening platform holds great promise for identifying extracellular interactions of uncharacterized receptor-ligand partners, which is essential to develop next-generation therapeutics, including additional immune checkpoint inhibitors.
MeSH term(s)	Ligands ; Membrane Proteins/genetics ; Transcriptional Activation ; CRISPR-Cas Systems
Chemical Substances	Ligands ; Membrane Proteins
Language	English
Publishing date	2024-02-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adj2445
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Endogenous EWSR1 Exists in Two Visual Modalities That Reflect Its Associations with Nucleic Acids and Concentration at Sites of Active Transcription.

Sundara Rajan, Soumya / Ebegboni, Vernon J / Pichling, Patricio / Ludwig, Katelyn R / Jones, Tamara L / Chari, Raj / Tran, Andy / Kruhlak, Michael J / Loncarek, Jadranka / Caplen, Natasha J

Molecular and cellular biology

2024 Volume 44, Issue 3, Page(s) 103–122

Abstract: EWSR1 is a member of the FET family of nucleic acid binding proteins that includes FUS and TAF15. Here, we report the systematic analysis of endogenous EWSR1's cellular organization in human cells. We demonstrate that EWSR1, which contains low complexity ...

Abstract	EWSR1 is a member of the FET family of nucleic acid binding proteins that includes FUS and TAF15. Here, we report the systematic analysis of endogenous EWSR1's cellular organization in human cells. We demonstrate that EWSR1, which contains low complexity and nucleic acid binding domains, is present in cells in faster and slower-recovering fractions, indicative of a protein undergoing both rapid exchange and longer-term interactions. The employment of complementary high-resolution imaging approaches shows EWSR1 exists in two visual modalities, a distributed state which is present throughout the nucleoplasm, and a concentrated state consistent with the formation of foci. Both EWSR1 visual modalities localize with nascent RNA. EWSR1 foci concentrate in regions of euchromatin, adjacent to protein markers of transcriptional activation, and significantly colocalize with phosphorylated RNA polymerase II. Our results contribute to bridging the gap between our understanding of the biophysical and biochemical properties of FET proteins, including EWSR1, their functions as transcriptional regulators, and the participation of these proteins in tumorigenesis and neurodegenerative disease.
MeSH term(s)	Humans ; Neurodegenerative Diseases ; Nucleic Acids/chemistry ; Nucleic Acids/metabolism ; RNA Polymerase II/metabolism ; RNA-Binding Protein EWS/genetics ; RNA-Binding Protein EWS/metabolism
Chemical Substances	EWSR1 protein, human ; Nucleic Acids ; RNA Polymerase II (EC 2.7.7.-) ; RNA-Binding Protein EWS
Language	English
Publishing date	2024-03-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1080/10985549.2024.2315425
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: CPAP insufficiency leads to incomplete centrioles that duplicate but fragment.

Vásquez-Limeta, Alejandra / Lukasik, Kimberly / Kong, Dong / Sullenberger, Catherine / Luvsanjav, Delgermaa / Sahabandu, Natalie / Chari, Raj / Loncarek, Jadranka

The Journal of cell biology

2022 Volume 221, Issue 5

Abstract: Centrioles are structures that assemble centrosomes. CPAP is critical for centrosome assembly, and its mutations are found in patients with diseases such as primary microcephaly. CPAP's centrosomal localization, its dynamics, and the consequences of its ... ...

Abstract	Centrioles are structures that assemble centrosomes. CPAP is critical for centrosome assembly, and its mutations are found in patients with diseases such as primary microcephaly. CPAP's centrosomal localization, its dynamics, and the consequences of its insufficiency in human cells are poorly understood. Here we use human cells genetically engineered for fast degradation of CPAP, in combination with superresolution microscopy, to address these uncertainties. We show that three independent centrosomal CPAP populations are dynamically regulated during the cell cycle. We confirm that CPAP is critical for assembly of human centrioles, but not for recruitment of pericentriolar material on already assembled centrioles. Further, we reveal that CPAP insufficiency leads to centrioles with incomplete microtubule triplets that can convert to centrosomes, duplicate, and form mitotic spindle poles, but fragment owing to loss of cohesion between microtubule blades. These findings further our basic understanding of the role of CPAP in centrosome biogenesis and help understand how CPAP aberrations can lead to human diseases.
MeSH term(s)	Cell Division ; Centrioles/genetics ; Centrosome ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubules/genetics ; Spindle Poles
Chemical Substances	CENPJ protein, human ; Microtubule-Associated Proteins
Language	English
Publishing date	2022-04-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202108018
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