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  1. Book: Flow cytometry protocols

    Hawley, Teresa S. / Hawley, Robert G.

    (Methods in molecular biology ; 2779 ; Springer protocols)

    2024  

    Author's details edited by Teresa S. Hawley, Robert G. Hawley
    Series title Methods in molecular biology ; 2779
    Springer protocols
    Collection
    Language English
    Size xv, 458 Seiten, Illustrationen
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT030726877
    ISBN 9781071637371 ; 1071637371
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
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  2. Book: Flow cytometry protocols

    Hawley, Robert G. / Hawley, Teresa S.

    (Methods in molecular biology ; 1678 ; Springer protocols ; Chemistry)

    2018  

    Author's details edited by Teresa S. Hawley (Flow Cytometry Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA), Robert G. Hawley (Department of Anatomy and Regenerative Biology, School of Medicine and Health Sciences, George Washington University, Washington, DC, USA)
    Series title Methods in molecular biology ; 1678
    Springer protocols
    Chemistry
    Collection
    Keywords intracellular protein biomarkers ; cytokine staining ; apoptosis analysis ; cell cycle ; FRET ; antibodies ; proteins
    Subject code 570
    Language English
    Size xiv, 492 Seiten, Illustrationen, Diagramme, 25.4 cm x 17.8 cm
    Edition Fourth edition
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT019480557
    ISBN 978-1-4939-7344-6 ; 1-4939-7344-4 ; 9781493973460 ; 1493973460
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

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    Zs A 7042 -1678- verfügbar in Königswinter Königswinter

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  3. Article ; Online: CRISPR-Cas9-Mediated Bioluminescent Tagging of Endogenous Proteins by Fluorescent Protein-Assisted Cell Sorting.

    Hawley, Robert G / Hawley, Teresa S

    Methods in molecular biology (Clifton, N.J.)

    2024  Volume 2779, Page(s) 273–286

    Abstract: Oncogenic fusion genes are attractive therapeutic targets because of their tumor-specific expression and central "driver" roles in various human cancers. However, oncogenic fusions involving transcription factors such as PAX3-FOXO1 in alveolar fusion ... ...

    Abstract Oncogenic fusion genes are attractive therapeutic targets because of their tumor-specific expression and central "driver" roles in various human cancers. However, oncogenic fusions involving transcription factors such as PAX3-FOXO1 in alveolar fusion gene-positive rhabdomyosarcoma (FP-RMS) have been difficult to inhibit due to the apparent lack of tractable drug-like binding sites comparable to that recognized by Gleevec (imatinib mesylate) on the BCR-ABL1 tyrosine kinase fusion protein. Toward the identification of novel small molecules that selectively target PAX3-FOXO1, we used CRISPR-Cas9-mediated knock-in to append the pro-luminescent HiBiT tag onto the carboxy terminus of the endogenous PAX3-FOXO1 fusion protein in two human FP-RMS cell lines (RH4 and SCMC). HiBiT is an 11-amino acid peptide derived from the NanoLuc luciferase that produces a luminescence signal which is ~100-fold brighter than firefly or Renilla luciferases through high-affinity binding to a complementary NanoLuc peptide fragment called LgBiT. To facilitate single-cell clonal isolation of knock-ins, the homology-directed repair template encoding HiBiT was followed by a P2A self-cleaving peptide for coexpression of an mCherry fluorescent protein as a fluorescence-activated cell sorter (FACS)-selectable marker. HiBiT tagging thus allows highly sensitive luminescence detection of endogenous PAX3-FOXO1 levels permitting quantitative high-throughput screening of large compound libraries for the discovery of PAX3-FOXO1 inhibitors and degraders.
    MeSH term(s) Humans ; Paired Box Transcription Factors/genetics ; Paired Box Transcription Factors/metabolism ; CRISPR-Cas Systems ; Rhabdomyosarcoma/genetics ; Peptides/metabolism ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Cell Line, Tumor ; Gene Expression Regulation, Neoplastic ; Red Fluorescent Protein
    Chemical Substances Paired Box Transcription Factors ; mCherry fluorescent protein ; Peptides ; Oncogene Proteins, Fusion ; Red Fluorescent Protein
    Language English
    Publishing date 2024-04-01
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3738-8_12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book: Flow cytometry protocols

    Hawley, Teresa S. / Hawley, Robert G.

    (Methods in molecular biology ; 699 ; Springer protocols ; Life sciences)

    2011  

    Author's details ed. by Teresa S. Hawley ; Robert G. Hawley
    Series title Methods in molecular biology ; 699
    Springer protocols
    Life sciences
    Collection
    Keywords Flow Cytometry / methods
    Language English
    Size XII, 485 S. : Ill., graph. Darst.
    Edition 3. ed.
    Publisher Humana Press
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT016570518
    ISBN 978-1-61737-949-9 ; 9781617379505 ; 1-61737-949-2 ; 1617379506
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2011 A 94 order for loan Magazin

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  5. Book: Flow cytometry protocols

    Hawley, Teresa S.

    (Methods in molecular biology ; 263)

    2004  

    Author's details ed. by Teresa S. Hawley
    Series title Methods in molecular biology ; 263
    Collection
    Keywords Flow Cytometry / methods ; Durchflusscytometrie ; Labortechnik
    Subject Laboratorium ; Laboratoriumstechnik ; Labormethode ; Flow cytometry ; Durchflusszytometrie ; Flowzytometrie
    Language English
    Size XIII, 434 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Humana Press
    Publishing place Totowa, NJ
    Publishing country United States
    Document type Book
    HBZ-ID HT013973587
    ISBN 1-58829-235-5 ; 1-58829-234-7 ; 978-1-58829-235-3 ; 978-1-58829-234-6
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2004 A 3060 order for loan Magazin

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  6. Article ; Online: Fluorescent Proteins for Flow Cytometry.

    Hawley, Teresa S / Hawley, Robert G / Telford, William G

    Current protocols in cytometry

    2017  Volume 80, Page(s) 9.12.1–9.12.20

    Abstract: Fluorescent proteins have become standard tools for cell and molecular biologists. The color palette of fluorescent proteins spans the ultraviolet, visible, and near-infrared spectrum. Utility of fluorescent proteins has been greatly facilitated by the ... ...

    Abstract Fluorescent proteins have become standard tools for cell and molecular biologists. The color palette of fluorescent proteins spans the ultraviolet, visible, and near-infrared spectrum. Utility of fluorescent proteins has been greatly facilitated by the availability of compact and affordable solid state lasers capable of providing various excitation wavelengths. In theory, the plethora of fluorescent proteins and lasers make it easy to detect multiple fluorescent proteins simultaneously. However, in practice, heavy spectral overlap due to broad excitation and emission spectra presents a challenge. In conventional flow cytometry, careful selection of excitation wavelengths and detection filters is necessary. Spectral flow cytometry, an emerging methodology that is not confined by the "one color, one detector" paradigm, shows promise in the facile detection of multiple fluorescent proteins. This chapter provides a synopsis of fluorescent protein development, a list of commonly used fluorescent proteins, some practical considerations and strategies for detection, and examples of applications. © 2017 by John Wiley & Sons, Inc.
    MeSH term(s) Biosensing Techniques ; Biotinylation ; Flow Cytometry/methods ; Genetic Vectors/metabolism ; Lasers ; Luminescent Proteins/metabolism ; Protein Interaction Mapping
    Chemical Substances Luminescent Proteins
    Language English
    Publishing date 2017-04-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2179050-4
    ISSN 1934-9300 ; 1934-9297
    ISSN (online) 1934-9300
    ISSN 1934-9297
    DOI 10.1002/cpcy.17
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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  7. Article: Methods for collection, handling, and analysis of sea urchin coelomocytes.

    Smith, L Courtney / Hawley, Teresa S / Henson, John H / Majeske, Audrey J / Oren, Matan / Rosental, Benyamin

    Methods in cell biology

    2019  Volume 150, Page(s) 357–389

    Abstract: Sea urchin coelomocytes can be collected in large numbers from adult sea urchins of the species, Strongylocentrotus purpuratus, which typically has 12-40mL of coelomic fluid. Coelomocytes are used for analysis of immune reactions and immune gene ... ...

    Abstract Sea urchin coelomocytes can be collected in large numbers from adult sea urchins of the species, Strongylocentrotus purpuratus, which typically has 12-40mL of coelomic fluid. Coelomocytes are used for analysis of immune reactions and immune gene expression in addition to basic functions of cells, in particular for understanding structure and modifications of the cytoskeleton in phagocytes. The methods described here include coelomocyte isolation, blocking the clotting reaction, establishing and maintaining primary cultures, separation of different types of coelomocytes into fractions, processing live coelomocytes for light microscopy, fixation and staining for light and electron microscopy, analysis of coelomocyte populations by flow cytometry, and sorting single cells for more detailed follow-up analyses including transcriptomics or genomic characteristics. These methods are provided to make working with coelomocytes accessible to researchers who are unfamiliar with these cells and perhaps to aid others who have worked extensively with invertebrate cells.
    MeSH term(s) Animals ; Cell Separation/methods ; Flow Cytometry/methods ; Gene Expression/physiology ; Genomics/methods ; Leukocytes/cytology ; Phagocytes/cytology ; Sea Urchins/cytology ; Sea Urchins/genetics ; Specimen Handling/methods ; Transcriptome/genetics
    Language English
    Publishing date 2019-01-09
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0091-679X
    ISSN 0091-679X
    DOI 10.1016/bs.mcb.2018.11.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: KLF4-SQSTM1/p62-associated prosurvival autophagy contributes to carfilzomib resistance in multiple myeloma models.

    Riz, Irene / Hawley, Teresa S / Hawley, Robert G

    Oncotarget

    2015  Volume 6, Issue 17, Page(s) 14814–14831

    Abstract: Multiple myeloma (MM) is an incurable clonal plasma cell malignancy. Because of a high rate of immunoglobulin synthesis, the endoplasmic reticulum of MM cells is subjected to elevated basal levels of stress. Consequently, proteasome inhibitors, which ... ...

    Abstract Multiple myeloma (MM) is an incurable clonal plasma cell malignancy. Because of a high rate of immunoglobulin synthesis, the endoplasmic reticulum of MM cells is subjected to elevated basal levels of stress. Consequently, proteasome inhibitors, which exacerbate this stress by inhibiting ubiquitin-proteasome-mediated protein degradation, are an important new class of chemotherapeutic agents being used to combat this disease. However, MM cells still develop resistance to proteasome inhibitors such as carfilzomib. Toward this end, we have established carfilzomib-resistant derivatives of MM cell lines. We found that resistance to carfilzomib was associated with elevated levels of prosurvival autophagy, and Kruppel-like factor 4 (KLF4) was identified as a contributing factor. Expression levels as well as nuclear localization of KLF4 protein were elevated in MM cells with acquired carfilzomib resistance. Chromatin immunoprecipitations indicated that endogenous KLF4 bound to the promoter regions of the SQSTM1 gene encoding the ubiquitin-binding adaptor protein sequestosome/p62 that links the proteasomal and autophagic protein degradation pathways. Ectopic expression of KLF4 induced upregulation of SQSTM1. On the other hand, inhibitors of autophagy sensitized MM cells to carfilzomib, even in carfilzomib-resistant derivatives having increased expression of the multidrug resistance protein P-glycoprotein. Thus, we report here a novel function for KLF4, one of the Yamanaka reprogramming factors, as being a contributor to autophagy gene expression which moderates preclinical proteasome inhibitor efficacy in MM.
    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Autophagy/drug effects ; Autophagy/genetics ; Cell Line, Tumor ; Cell Survival/drug effects ; Cell Survival/genetics ; Chloroquine/pharmacology ; Drug Resistance, Neoplasm/genetics ; Gene Expression Profiling/methods ; Gene Expression Regulation, Neoplastic/drug effects ; Histone-Lysine N-Methyltransferase/genetics ; Histone-Lysine N-Methyltransferase/metabolism ; Humans ; Kruppel-Like Transcription Factors/genetics ; Kruppel-Like Transcription Factors/metabolism ; Microscopy, Confocal ; Multiple Myeloma/genetics ; Multiple Myeloma/metabolism ; Multiple Myeloma/pathology ; Oligopeptides/pharmacology ; Prognosis ; Promoter Regions, Genetic/genetics ; Protein Binding ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Sequestosome-1 Protein ; Survival Analysis
    Chemical Substances Adaptor Proteins, Signal Transducing ; GKLF protein ; Kruppel-Like Transcription Factors ; Oligopeptides ; Repressor Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; carfilzomib (72X6E3J5AR) ; Chloroquine (886U3H6UFF) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; NSD2 protein, human (EC 2.1.1.43)
    Language English
    Publishing date 2015-06-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2560162-3
    ISSN 1949-2553 ; 1949-2553
    ISSN (online) 1949-2553
    ISSN 1949-2553
    DOI 10.18632/oncotarget.4530
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Noncanonical SQSTM1/p62-Nrf2 pathway activation mediates proteasome inhibitor resistance in multiple myeloma cells via redox, metabolic and translational reprogramming.

    Riz, Irene / Hawley, Teresa S / Marsal, Jeffrey W / Hawley, Robert G

    Oncotarget

    2016  Volume 7, Issue 41, Page(s) 66360–66385

    Abstract: Multiple Myeloma (MM) is a B-cell malignancy characterized by the accumulation of clonal plasma cells in the bone marrow, with drug resistance being a major cause of therapeutic failure. We established a carfilzomib-resistant derivative of the LP-1 MM ... ...

    Abstract Multiple Myeloma (MM) is a B-cell malignancy characterized by the accumulation of clonal plasma cells in the bone marrow, with drug resistance being a major cause of therapeutic failure. We established a carfilzomib-resistant derivative of the LP-1 MM cell line (LP-1/Cfz) and found that the transcription factor NF-E2 p45-related factor 2 (Nrf2; gene symbol NFE2L2) contributes to carfilzomib resistance. The mechanism of Nrf2 activation involved enhanced translation of Nrf2 as well as its positive regulator, the autophagy receptor sequestosome 1 (SQSTM1)/p62. The eukaryotic translation initiation factor gene EIF4E3 was among the Nrf2 target genes upregulated in LP-1/Cfz cells, suggesting existence of a positive feedback loop. In line with this, we found that siRNA knockdown of eIF4E3 decreased Nrf2 protein levels. On the other hand, elevated SQSTM1/p62 levels were due at least in part to activation of the PERK-eIF2α pathway. LP-1/Cfz cells had decreased levels of reactive oxygen species as well as elevated levels of fatty acid oxidation and prosurvival autophagy. Genetic and pharmacologic inhibition of the Nrf2-EIF4E3 axis or the PERK-eIF2α pathway, disruption of redox homeostasis or inhibition of fatty acid oxidation or autophagy conferred sensitivity to carfilzomib. Our findings were supported by clinical data where increased EIF4E3 expression was predictive of Nrf2 target gene upregulation in a subgroup of patients with chemoresistant minimal residual disease and relapsed/refractory MM. Thus, our data offer a preclinical rationale for including inhibitors of the SQSTM1/p62-Nrf2 pathway to the treatment regimens for certain advanced stage MM patients.
    Language English
    Publishing date 2016-10-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2560162-3
    ISSN 1949-2553 ; 1949-2553
    ISSN (online) 1949-2553
    ISSN 1949-2553
    DOI 10.18632/oncotarget.11960
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book: Flow cytometry protocols

    Hawley, Teresa S / Hawley, Robert G

    (Springer protocols ; Methods in molecular biology, ; 699)

    2011  

    Series title Springer protocols
    Methods in molecular biology, ; 699
    MeSH term(s) Flow Cytometry/methods
    Language English
    Size xii, 485 p. :, ill. ;, 24 cm.
    Edition 3rd ed. /
    Publisher Humana Press
    Publishing place New York
    Document type Book
    ISBN 9781617379499 ; 1617379492 ; 9781617379505 ; 1617379506
    Database Catalogue of the US National Library of Medicine (NLM)

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