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  1. Article ; Online: An IMiD-inducible degron provides reversible regulation for chimeric antigen receptor expression and activity.

    Carbonneau, Seth / Sharma, Sujata / Peng, Liaomin / Rajan, Vaisakh / Hainzl, Dominik / Henault, Martin / Yang, Chian / Hale, Jacob / Shulok, Janine / Tallarico, John / Porter, Jeff / Brogdon, Jennifer L / Dranoff, Glenn / Bradner, James E / Hild, Marc / Guimaraes, Carla P

    Cell chemical biology

    2021  Volume 28, Issue 4, Page(s) 583

    Language English
    Publishing date 2021-04-16
    Publishing country United States
    Document type Published Erratum
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2021.02.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: An IMiD-inducible degron provides reversible regulation for chimeric antigen receptor expression and activity.

    Carbonneau, Seth / Sharma, Sujata / Peng, Liaomin / Rajan, Vaisakh / Hainzl, Dominik / Henault, Martin / Yang, Chian / Hale, Jacob / Shulok, Janine / Tallarico, John / Porter, Jeff / Brogdon, Jennifer L / Dranoff, Glenn / Bradner, James E / Hild, Marc / Guimaraes, Carla P

    Cell chemical biology

    2020  Volume 28, Issue 6, Page(s) 802–812.e6

    Abstract: The recent development of successful CAR (chimeric antigen receptor) T cell therapies has been accompanied by a need to better control potentially fatal toxicities that can arise from adverse immune reactions. Here we present a ligand-controlled CAR ... ...

    Abstract The recent development of successful CAR (chimeric antigen receptor) T cell therapies has been accompanied by a need to better control potentially fatal toxicities that can arise from adverse immune reactions. Here we present a ligand-controlled CAR system, based on the IKZF3 ZF2 β-hairpin IMiD-inducible degron, which allows for the reversible control of expression levels of type I membrane proteins, including CARs. Testing this system in an established mouse xenotransplantation model for acute lymphoblastic leukemia, we validate the ability of the CAR19-degron to target and kill CD19-positive cells displaying complete control/clearance of the tumor. We also demonstrate that the activity of CAR19-degron can be regulated in vivo when dosing a US Food and Drug Administration-approved drug, lenalidomide.
    MeSH term(s) Adolescent ; Animals ; Cell Line ; Cell Proliferation/drug effects ; Female ; Humans ; Ikaros Transcription Factor/chemistry ; Ikaros Transcription Factor/immunology ; Immunologic Factors/chemistry ; Immunologic Factors/pharmacology ; Male ; Mice ; Mice, Congenic ; Mice, Inbred NOD ; Mice, SCID ; Middle Aged ; Molecular Structure ; Neoplasms, Experimental/drug therapy ; Neoplasms, Experimental/immunology ; Neoplasms, Experimental/pathology ; Receptors, Chimeric Antigen/genetics ; Receptors, Chimeric Antigen/immunology ; T-Lymphocytes/immunology ; Young Adult
    Chemical Substances IKZF3 protein, human ; Immunologic Factors ; Receptors, Chimeric Antigen ; Ikaros Transcription Factor (148971-36-2)
    Language English
    Publishing date 2020-12-16
    Publishing country United States
    Document type Journal Article
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2020.11.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Receptor overexpression or inhibition alters cell surface dynamics of EGF-EGFR interaction: new insights from real-time single molecule analysis.

    Yu, Chenxu / Hale, Jacob / Ritchie, Kenneth / Prasad, Nagendra K / Irudayaraj, Joseph

    Biochemical and biophysical research communications

    2009  Volume 378, Issue 3, Page(s) 376–382

    Abstract: Binding of Epidermal growth factor (EGF) to epidermal growth factor receptor (EGFR) in two types of cancer cells (HeLa; 5 x 10(4) EGFR/cell) and MDA-MB-468; 2 x 10(6) EGFR/cell) was studied using Total Internal Reflectance Fluorescence (TIRF) microscopy ... ...

    Abstract Binding of Epidermal growth factor (EGF) to epidermal growth factor receptor (EGFR) in two types of cancer cells (HeLa; 5 x 10(4) EGFR/cell) and MDA-MB-468; 2 x 10(6) EGFR/cell) was studied using Total Internal Reflectance Fluorescence (TIRF) microscopy at single molecule precision. Mathematical modeling of the binding kinetics revealed that cells respond differently to the same concentration of EGF depending on the expression level of EGFR. Compared to Hela, MDA-MB-468 cells show; (a) higher number of pre-formed dimers, (b) improved EGF-EGFR interaction at lower ligand concentrations, and (c) shorter time-lapse between first and second EGF binding to the dimer. Treatment with a pharmacological inhibitor of EGFR, AG1478, produced strikingly different binding kinetics where the extent of pre-formed EGFR dimers increased substantially. Thus, single molecule approaches produce novel, quantitative information on signaling mechanisms of significant biological importance. Surface kinetics could also serve as surrogate markers to predict biological outcome of signaling pathways.
    MeSH term(s) Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Dimerization ; Epidermal Growth Factor/metabolism ; HeLa Cells ; Humans ; Microscopy, Fluorescence ; Protein Kinase Inhibitors/pharmacology ; Quinazolines ; Receptor, Epidermal Growth Factor/antagonists & inhibitors ; Receptor, Epidermal Growth Factor/biosynthesis ; Receptor, Epidermal Growth Factor/metabolism ; Tyrphostins/pharmacology
    Chemical Substances Protein Kinase Inhibitors ; Quinazolines ; Tyrphostins ; tyrphostin AG 1478 (170449-18-0) ; Epidermal Growth Factor (62229-50-9) ; Receptor, Epidermal Growth Factor (EC 2.7.10.1)
    Language English
    Publishing date 2009-01-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2008.11.018
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
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  4. Article ; Online: Gyromagnetic imaging: dynamic optical contrast using gold nanostars with magnetic cores.

    Wei, Qingshan / Song, Hyon-Min / Leonov, Alexei P / Hale, Jacob A / Oh, Dongmyung / Ong, Quy K / Ritchie, Kenneth / Wei, Alexander

    Journal of the American Chemical Society

    2009  Volume 131, Issue 28, Page(s) 9728–9734

    Abstract: Plasmon-resonant nanoparticles with optical scattering in the near-infrared (NIR) are valuable contrast agents for biophotonic imaging and may be detected at the single-particle limit against a dark background, but their contrast is often limited in ... ...

    Abstract Plasmon-resonant nanoparticles with optical scattering in the near-infrared (NIR) are valuable contrast agents for biophotonic imaging and may be detected at the single-particle limit against a dark background, but their contrast is often limited in environments with high noise. Here we consider gyromagnetic imaging as a dynamic mode of optical contrast, using gold nanostars with superparamagnetic cores. The nanostars exhibit polarization-sensitive NIR scattering and can produce a frequency-modulated signal in response to a rotating magnetic field gradient. This periodic "twinkling" can be converted into Fourier-domain images with a dramatic reduction in background. We demonstrate gyromagnetic imaging of nanostars inside of tumor cells, using broadband excitation: while their time-domain signals are obscured by incoherent scattering, their Fourier-domain signals can be clearly resolved in less than a second. The gyromagnetically active nanostars do not cause a loss in viability, and can even have a mild stimulatory effect on cell growth.
    MeSH term(s) Biological Transport ; Gold/chemistry ; Gold/metabolism ; Humans ; KB Cells ; Luminescence ; Magnetics ; Metal Nanoparticles/chemistry ; Motion ; Optical Phenomena ; Rotation ; Time Factors ; Tomography, Optical Coherence
    Chemical Substances Gold (7440-57-5)
    Language English
    Publishing date 2009-05-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/ja901562j
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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  5. Article ; Online: Analysis of the mobilities of band 3 populations associated with ankyrin protein and junctional complexes in intact murine erythrocytes.

    Kodippili, Gayani C / Spector, Jeff / Hale, Jacob / Giger, Katie / Hughes, Michael R / McNagny, Kelly M / Birkenmeier, Connie / Peters, Luanne / Ritchie, Ken / Low, Philip S

    The Journal of biological chemistry

    2011  Volume 287, Issue 6, Page(s) 4129–4138

    Abstract: Current models of the erythrocyte membrane depict three populations of band 3: (i) a population tethered to spectrin via ankyrin, (ii) a fraction attached to the spectrin-actin junctional complex via adducin, and (iii) a freely diffusing population. ... ...

    Abstract Current models of the erythrocyte membrane depict three populations of band 3: (i) a population tethered to spectrin via ankyrin, (ii) a fraction attached to the spectrin-actin junctional complex via adducin, and (iii) a freely diffusing population. Because many studies of band 3 diffusion also distinguish three populations of the polypeptide, it has been speculated that the three populations envisioned in membrane models correspond to the three fractions observed in diffusion analyses. To test this hypothesis, we characterized band 3 diffusion by single-particle tracking in wild-type and ankyrin- and adducin-deficient erythrocytes. We report that ∼40% of total band 3 in wild-type murine erythrocytes is attached to ankyrin, whereas ∼33% is immobilized by adducin, and ∼27% is not attached to any cytoskeletal anchor. More detailed analyses reveal that mobilities of individual ankyrin- and adducin-tethered band 3 molecules are heterogeneous, varying by nearly 2 orders of magnitude and that there is considerable overlap in diffusion coefficients for adducin and ankyrin-tethered populations. Taken together, the data suggest that although the ankyrin- and adducin-immobilized band 3 can be monitored separately, significant heterogeneity still exists within each population, suggesting that structural and compositional properties likely vary considerably within each band 3 complex.
    MeSH term(s) Animals ; Anion Exchange Protein 1, Erythrocyte/genetics ; Anion Exchange Protein 1, Erythrocyte/metabolism ; Ankyrins/genetics ; Ankyrins/metabolism ; Calmodulin-Binding Proteins/genetics ; Calmodulin-Binding Proteins/metabolism ; Erythrocyte Membrane/genetics ; Erythrocyte Membrane/metabolism ; Humans ; Mice ; Mice, Mutant Strains ; Protein Binding/physiology
    Chemical Substances Anion Exchange Protein 1, Erythrocyte ; Ankyrins ; Calmodulin-Binding Proteins ; adducin
    Language English
    Publishing date 2011-12-06
    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.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.294439
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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