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  1. Article ; Online: Discovery and Characterization of IFITM

    Das, Tandrila / Hang, Howard C

    Viruses

    2023  Volume 15, Issue 12

    Abstract: Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important host antiviral defense factors. They are active against viruses like the influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute ... ...

    Abstract Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important host antiviral defense factors. They are active against viruses like the influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory syndrome coronavirus (SARS-CoV). In this review, we focus on IFITM3
    MeSH term(s) Humans ; Lipoylation ; Zika Virus Infection ; RNA-Binding Proteins/metabolism ; Zika Virus/metabolism ; Influenza A virus/metabolism ; Antiviral Agents/metabolism ; Lipids ; Membrane Proteins/metabolism
    Chemical Substances RNA-Binding Proteins ; Antiviral Agents ; Lipids ; IFITM3 protein, human ; Membrane Proteins
    Language English
    Publishing date 2023-11-28
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15122329
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Functional analysis of protein post-translational modifications using genetic codon expansion.

    Peng, Tao / Das, Tandrila / Ding, Ke / Hang, Howard C

    Protein science : a publication of the Protein Society

    2023  Volume 32, Issue 4, Page(s) e4618

    Abstract: Post-translational modifications (PTMs) of proteins not only exponentially increase the diversity of proteoforms, but also contribute to dynamically modulating the localization, stability, activity, and interaction of proteins. Understanding the ... ...

    Abstract Post-translational modifications (PTMs) of proteins not only exponentially increase the diversity of proteoforms, but also contribute to dynamically modulating the localization, stability, activity, and interaction of proteins. Understanding the biological consequences and functions of specific PTMs has been challenging for many reasons, including the dynamic nature of many PTMs and the technical limitations to access homogenously modified proteins. The genetic code expansion technology has emerged to provide unique approaches for studying PTMs. Through site-specific incorporation of unnatural amino acids (UAAs) bearing PTMs or their mimics into proteins, genetic code expansion allows the generation of homogenous proteins with site-specific modifications and atomic resolution both in vitro and in vivo. With this technology, various PTMs and mimics have been precisely introduced into proteins. In this review, we summarize the UAAs and approaches that have been recently developed to site-specifically install PTMs and their mimics into proteins for functional studies of PTMs.
    MeSH term(s) Proteins/chemistry ; Protein Processing, Post-Translational ; Amino Acids/chemistry ; Genetic Code ; Codon
    Chemical Substances Proteins ; Amino Acids ; Codon
    Language English
    Publishing date 2023-03-08
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4618
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3407: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 1: Show issues

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  3. Article ; Online: Protein

    Das, Tandrila / Yount, Jacob S / Hang, Howard C

    Open biology

    2021  Volume 11, Issue 3, Page(s) 200411

    Abstract: ... ...

    Abstract S
    MeSH term(s) Adaptive Immunity ; Animals ; Humans ; Immunity, Innate ; Lipoylation ; Protein Processing, Post-Translational ; Receptors, Immunologic/metabolism
    Chemical Substances Receptors, Immunologic
    Language English
    Publishing date 2021-03-03
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.200411
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  4. Article ; Online: Protein S-palmitoylation in immunity

    Tandrila Das / Jacob S. Yount / Howard C. Hang

    Open Biology, Vol 11, Iss

    2021  Volume 3

    Abstract: S-palmitoylation is a reversible posttranslational lipid modification of proteins. It controls protein activity, stability, trafficking and protein–protein interactions. Recent global profiling of immune cells and targeted analysis have identified many S- ...

    Abstract S-palmitoylation is a reversible posttranslational lipid modification of proteins. It controls protein activity, stability, trafficking and protein–protein interactions. Recent global profiling of immune cells and targeted analysis have identified many S-palmitoylated immunity-associated proteins. Here, we review S-palmitoylated immune receptors and effectors, and their dynamic regulation at cellular membranes to generate specific and balanced immune responses. We also highlight how this understanding can drive therapeutic advances to pharmacologically modulate immune responses.
    Keywords s-palmitoylation ; adaptive immunity ; innate immune receptors ; innate immune effectors ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-03-01T00:00:00Z
    Publisher The Royal Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Chemical approaches for investigating site-specific protein S-fatty acylation.

    Garst, Emma H / Das, Tandrila / Hang, Howard C

    Current opinion in chemical biology

    2021  Volume 65, Page(s) 109–117

    Abstract: Protein S-fatty acylation or S-palmitoylation is a reversible and regulated lipid post-translational modification (PTM) in eukaryotes. Loss-of-function mutagenesis studies have suggested important roles for protein S-fatty acylation in many fundamental ... ...

    Abstract Protein S-fatty acylation or S-palmitoylation is a reversible and regulated lipid post-translational modification (PTM) in eukaryotes. Loss-of-function mutagenesis studies have suggested important roles for protein S-fatty acylation in many fundamental biological pathways in development, neurobiology, and immunity that are also associated with human diseases. However, the hydrophobicity and reversibility of this PTM have made site-specific gain-of-function studies more challenging to investigate. In this review, we summarize recent chemical biology approaches and methods that have enabled site-specific gain-of-function studies of protein S-fatty acylation and the investigation of the mechanisms and significance of this PTM in eukaryotic biology.
    MeSH term(s) Acylation ; Humans ; Lipoylation ; Protein Processing, Post-Translational ; Protein S/metabolism
    Chemical Substances Protein S
    Language English
    Publishing date 2021-07-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2021.06.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4986: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: S

    Das, Tandrila / Yang, Xinglin / Lee, Hwayoung / Garst, Emma H / Valencia, Estefania / Chandran, Kartik / Im, Wonpil / Hang, Howard C

    ACS chemical biology

    2022  Volume 17, Issue 8, Page(s) 2109–2120

    Abstract: Interferon-induced transmembrane proteins (IFITM1, 2, and 3) are important antiviral proteins that are active against many viruses, including influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV), and severe acute ... ...

    Abstract Interferon-induced transmembrane proteins (IFITM1, 2, and 3) are important antiviral proteins that are active against many viruses, including influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV), and severe acute respiratory syndrome coronavirus (SARS-CoV). IFITM proteins exhibit specificity in activity, but their distinct mechanisms of action and regulation are unclear. Since
    MeSH term(s) Animals ; Antiviral Agents/pharmacology ; Cholesterol/metabolism ; Influenza A virus ; Lipoylation ; Membrane Proteins/metabolism ; Membrane Proteins/pharmacology ; SARS-CoV-2 ; Sterols/metabolism ; Zika Virus
    Chemical Substances Antiviral Agents ; Membrane Proteins ; Sterols ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2022-07-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.2c00176
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: S-palmitoylation and sterol interactions mediate antiviral specificity of IFITM isoforms.

    Das, Tandrila / Yang, Xinglin / Lee, Hwayoung / Garst, Emma / Valencia, Estefania / Chandran, Kartik / Im, Wonpil / Hang, Howard

    Research square

    2021  

    Abstract: Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important antiviral proteins that are active against many viruses, including influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory ... ...

    Abstract Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important antiviral proteins that are active against many viruses, including influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory syndrome coronavirus (SARS-CoV). IFITMs exhibit isoform-specific activity, but their distinct mechanisms of action and regulation are unclear. Since
    Language English
    Publishing date 2021-12-29
    Publishing country United States
    Document type Preprint
    DOI 10.21203/rs.3.rs-1179000/v1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity.

    Garst, Emma H / Lee, Hwayoung / Das, Tandrila / Bhattacharya, Shibani / Percher, Avital / Wiewiora, Rafal / Witte, Isaac P / Li, Yumeng / Peng, Tao / Im, Wonpil / Hang, Howard C

    ACS chemical biology

    2021  Volume 16, Issue 5, Page(s) 844–856

    Abstract: Interferon-induced transmembrane proteins (IFITMs) ... ...

    Abstract Interferon-induced transmembrane proteins (IFITMs) are
    MeSH term(s) Amino Acid Sequence ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Binding Sites ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Computational Biology ; Drug Design ; Humans ; Interferons/chemistry ; Interferons/pharmacology ; Lipids/chemistry ; Lipoylation ; Lysosomes/metabolism ; Membrane Proteins/metabolism ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; RNA-Binding Proteins/metabolism ; Signal Transduction
    Chemical Substances Antiviral Agents ; IFITM3 protein, human ; Lipids ; Membrane Proteins ; RNA-Binding Proteins ; Interferons (9008-11-1)
    Language English
    Publishing date 2021-04-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.1c00013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Vacancy-Engineered Nanoceria: Enzyme Mimetic Hotspots for the Degradation of Nerve Agents.

    Vernekar, Amit A / Das, Tandrila / Mugesh, Govindasamy

    Angewandte Chemie (International ed. in English)

    2016  Volume 55, Issue 4, Page(s) 1412–1416

    Abstract: Organophosphorus-based nerve agents, such as paraoxon, parathion, and malathion, inhibit acetylcholinesterase, which results in paralysis, respiratory failure, and death. Bacteria are known to use the enzyme phosphotriesterase (PTE) to break down these ... ...

    Abstract Organophosphorus-based nerve agents, such as paraoxon, parathion, and malathion, inhibit acetylcholinesterase, which results in paralysis, respiratory failure, and death. Bacteria are known to use the enzyme phosphotriesterase (PTE) to break down these compounds. In this work, we designed vacancy-engineered nanoceria (VE CeO2 NPs) as PTE mimetic hotspots for the rapid degradation of nerve agents. We observed that the hydrolytic effect of the nanomaterial is due to the synergistic activity between both Ce(3+) and Ce(4+) ions located in the active site-like hotspots. Furthermore, the catalysis by nanoceria overcomes the product inhibition generally observed for PTE and small molecule-based PTE mimetics.
    MeSH term(s) Biodegradation, Environmental ; Cerium/chemistry ; Enzymes/metabolism ; Microscopy, Electron, Transmission ; Molecular Mimicry ; Nerve Agents/metabolism ; Organophosphorus Compounds/metabolism ; X-Ray Diffraction
    Chemical Substances Enzymes ; Nerve Agents ; Organophosphorus Compounds ; Cerium (30K4522N6T) ; ceric oxide (619G5K328Y)
    Language English
    Publishing date 2016-01-22
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201510355
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  10. Article ; Online: A Remarkably Efficient MnFe2 O4 -based Oxidase Nanozyme.

    Vernekar, Amit A / Das, Tandrila / Ghosh, Sourav / Mugesh, Govindasamy

    Chemistry, an Asian journal

    2016  Volume 11, Issue 1, Page(s) 72–76

    Abstract: Nanomaterials-based enzyme mimetics (nanozymes) have attracted considerable interest due to their applications in imaging, diagnostics, and therapeutic treatments. Particularly, metal-oxide nanozymes have been shown to mimic the interesting redox ... ...

    Abstract Nanomaterials-based enzyme mimetics (nanozymes) have attracted considerable interest due to their applications in imaging, diagnostics, and therapeutic treatments. Particularly, metal-oxide nanozymes have been shown to mimic the interesting redox properties and biological activities of metalloenzymes. Here we describe an efficient synthesis of MnFe2 O4 nanomaterials and show how the morphology can be controlled by using a simple co-precipitation method. The nanomaterials prepared by this method exhibit a remarkable oxidase-like activity. Interestingly, the activity is morphology-dependent, with nanooctahedra (NOh) exhibiting a catalytic efficiency of 2.21×10(9)  m(-1)  s(-1) , the highest activity ever reported for a nanozyme.
    MeSH term(s) Iron/chemistry ; Iron/metabolism ; Manganese/chemistry ; Manganese/metabolism ; Nanostructures/chemistry ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Oxygen/chemistry ; Oxygen/metabolism ; Particle Size ; Surface Properties
    Chemical Substances Manganese (42Z2K6ZL8P) ; Iron (E1UOL152H7) ; Oxidoreductases (EC 1.-) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2016-01
    Publishing country Germany
    Document type Journal Article
    ISSN 1861-471X
    ISSN (online) 1861-471X
    DOI 10.1002/asia.201500942
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