LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 8 of total 8

Search options

  1. Article ; Online: Manipulating neural activity in physiologically classified neurons: triumphs and challenges.

    Gore, Felicity / Schwartz, Edmund C / Salzman, C Daniel

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences

    2015  Volume 370, Issue 1677, Page(s) 20140216

    Abstract: Understanding brain function requires knowing both how neural activity encodes information and how this activity generates appropriate responses. Electrophysiological, imaging and immediate early gene immunostaining studies have been instrumental in ... ...

    Abstract Understanding brain function requires knowing both how neural activity encodes information and how this activity generates appropriate responses. Electrophysiological, imaging and immediate early gene immunostaining studies have been instrumental in identifying and characterizing neurons that respond to different sensory stimuli, events and motor actions. Here we highlight approaches that have manipulated the activity of physiologically classified neurons to determine their role in the generation of behavioural responses. Previous experiments have often exploited the functional architecture observed in many cortical areas, where clusters of neurons share response properties. However, many brain structures do not exhibit such functional architecture. Instead, neurons with different response properties are anatomically intermingled. Emerging genetic approaches have enabled the identification and manipulation of neurons that respond to specific stimuli despite the lack of discernable anatomical organization. These approaches have advanced understanding of the circuits mediating sensory perception, learning and memory, and the generation of behavioural responses by providing causal evidence linking neural response properties to appropriate behavioural output. However, significant challenges remain for understanding cognitive processes that are probably mediated by neurons with more complex physiological response properties. Currently available strategies may prove inadequate for determining how activity in these neurons is causally related to cognitive behaviour.
    MeSH term(s) Animals ; Behavior/physiology ; Brain/cytology ; Brain/physiology ; Conditioning (Psychology)/physiology ; Electrophysiological Phenomena ; Fear/physiology ; Fear/psychology ; Genetic Techniques ; Humans ; Learning/physiology ; Memory/physiology ; Neurons/classification ; Neurons/physiology ; Substance-Related Disorders/physiopathology ; Substance-Related Disorders/psychology
    Language English
    Publishing date 2015-05-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 208382-6
    ISSN 1471-2970 ; 0080-4622 ; 0264-3839 ; 0962-8436
    ISSN (online) 1471-2970
    ISSN 0080-4622 ; 0264-3839 ; 0962-8436
    DOI 10.1098/rstb.2014.0216
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Einzelsignatur: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Small-molecule-mediated rescue of protein function by an inducible proteolytic shunt.

    Pratt, Matthew R / Schwartz, Edmund C / Muir, Tom W

    Proceedings of the National Academy of Sciences of the United States of America

    2007  Volume 104, Issue 27, Page(s) 11209–11214

    Abstract: Controlling protein function through posttranslational manipulations has emerged as an attractive complementary technology to existing genetic systems. Often these methods involve developing pharmacological agents to probe protein function without the ... ...

    Abstract Controlling protein function through posttranslational manipulations has emerged as an attractive complementary technology to existing genetic systems. Often these methods involve developing pharmacological agents to probe protein function without the need to generate a unique compound for each protein family. One common strategy uses small molecules that act as chemical inducers of dimerization by mediating the interaction of two proteins. Herein we report the use of a chemical inducer of dimerization for the development of a posttranslational technology for the manipulation of protein function. This system, split ubiquitin for the rescue of function (SURF), places the complementation of genetically split ubiquitin under the control of rapamycin-induced dimerization of FK506-binding protein and FKBP12-rapamycin-binding protein. Before complementation a "degron" dooms a protein of interest for destruction by the proteasome. Addition of rapamycin results in a proteolytic shunt away from degradation by inducing ubiquitin complementation and cleavage of the protein of interest from the degron. Importantly, the native protein is rescued. We characterized this system with firefly luciferase and went on to apply it to members of three important classes of proteins: proteases (caspase-3), kinases (v-Src), and transcription factors (Smad3). This general strategy should allow for inducible rescue of a variety of proteins in such a way that their native structure and function are maintained.
    MeSH term(s) Formazans/metabolism ; Genetic Complementation Test ; HeLa Cells ; Humans ; Hydrolysis ; Peptide Hydrolases/metabolism ; Protein Processing, Post-Translational/physiology ; Smad3 Protein/physiology ; Tetrazolium Salts/metabolism ; Transforming Growth Factor beta1/biosynthesis ; Transforming Growth Factor beta1/genetics ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitin/physiology
    Chemical Substances Formazans ; Smad3 Protein ; Tetrazolium Salts ; Transforming Growth Factor beta1 ; Ubiquitin ; MTT formazan (23305-68-2) ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2007-07-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0700816104
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: Post-translational enzyme activation in an animal via optimized conditional protein splicing.

    Schwartz, Edmund C / Saez, Lino / Young, Michael W / Muir, Tom W

    Nature chemical biology

    2007  Volume 3, Issue 1, Page(s) 50–54

    Abstract: Control over the timing, location and level of protein activity in vivo is crucial to understanding biological function. Living systems are able to respond to external and internal stimuli rapidly and in a graded fashion by maintaining a pool of proteins ...

    Abstract Control over the timing, location and level of protein activity in vivo is crucial to understanding biological function. Living systems are able to respond to external and internal stimuli rapidly and in a graded fashion by maintaining a pool of proteins whose activities are altered through post-translational modifications. Here we show that the process of protein trans-splicing can be used to modulate enzymatic activity both in cultured cells and in Drosophila melanogaster. We used an optimized conditional protein splicing system to rapidly trigger the in vivo ligation of two inactive fragments of firefly luciferase in a tunable manner. This technique provides a means of controlling enzymatic function with greater speed and precision than with standard genetic techniques and is a useful tool for probing biological processes.
    MeSH term(s) Animals ; Animals, Genetically Modified ; Cells, Cultured ; Culture Media, Conditioned ; Drosophila/enzymology ; Drosophila/genetics ; Enzyme Activation/genetics ; Exteins/genetics ; Inteins/genetics ; Luciferases/genetics ; Luciferases/metabolism ; Protein Splicing/genetics ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Up-Regulation
    Chemical Substances Culture Media, Conditioned ; Recombinant Fusion Proteins ; Luciferases (EC 1.13.12.-)
    Language English
    Publishing date 2007-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/nchembio832
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6251: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 90: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: "The splice is right": how protein splicing is opening new doors in protein science.

    Schwartz, Edmund C / Muir, Tom W / Tyszkiewicz, Amy B

    Chemical communications (Cambridge, England)

    2003  , Issue 17, Page(s) 2087–2090

    MeSH term(s) Biotechnology/methods ; Protein Engineering/methods ; Protein Splicing ; Recombinant Fusion Proteins/chemical synthesis ; Recombinant Fusion Proteins/isolation & purification
    Chemical Substances Recombinant Fusion Proteins
    Language English
    Publishing date 2003-09-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b304989m
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Small-molecule-mediated rescue of protein function by an inducible proteolytic shunt

    Pratt, Matthew R / Schwartz, Edmund C / Muir, Tom W

    Proceedings of the National Academy of Sciences of the United States of America. 2007 July 3, v. 104, no. 27

    2007  

    Abstract: Controlling protein function through posttranslational manipulations has emerged as an attractive complementary technology to existing genetic systems. Often these methods involve developing pharmacological agents to probe protein function without the ... ...

    Abstract Controlling protein function through posttranslational manipulations has emerged as an attractive complementary technology to existing genetic systems. Often these methods involve developing pharmacological agents to probe protein function without the need to generate a unique compound for each protein family. One common strategy uses small molecules that act as chemical inducers of dimerization by mediating the interaction of two proteins. Herein we report the use of a chemical inducer of dimerization for the development of a posttranslational technology for the manipulation of protein function. This system, split ubiquitin for the rescue of function (SURF), places the complementation of genetically split ubiquitin under the control of rapamycin-induced dimerization of FK506-binding protein and FKBP12-rapamycin-binding protein. Before complementation a "degron" dooms a protein of interest for destruction by the proteasome. Addition of rapamycin results in a proteolytic shunt away from degradation by inducing ubiquitin complementation and cleavage of the protein of interest from the degron. Importantly, the native protein is rescued. We characterized this system with firefly luciferase and went on to apply it to members of three important classes of proteins: proteases (caspase-3), kinases (v-Src), and transcription factors (Smad3). This general strategy should allow for inducible rescue of a variety of proteins in such a way that their native structure and function are maintained.
    Language English
    Dates of publication 2007-0703
    Size p. 11209-11214.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 63/44: Show issues
    87/25270: Show issues
    Qa 4' 169/3: Show issues
    Z 8.7: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article ; Online: Neural Representations of Unconditioned Stimuli in Basolateral Amygdala Mediate Innate and Learned Responses.

    Gore, Felicity / Schwartz, Edmund C / Brangers, Baylor C / Aladi, Stanley / Stujenske, Joseph M / Likhtik, Ekaterina / Russo, Marco J / Gordon, Joshua A / Salzman, C Daniel / Axel, Richard

    Cell

    2015  Volume 162, Issue 1, Page(s) 134–145

    Abstract: Stimuli that possess inherently rewarding or aversive qualities elicit emotional responses and also induce learning by imparting valence upon neutral sensory cues. Evidence has accumulated implicating the amygdala as a critical structure in mediating ... ...

    Abstract Stimuli that possess inherently rewarding or aversive qualities elicit emotional responses and also induce learning by imparting valence upon neutral sensory cues. Evidence has accumulated implicating the amygdala as a critical structure in mediating these processes. We have developed a genetic strategy to identify the representations of rewarding and aversive unconditioned stimuli (USs) in the basolateral amygdala (BLA) and have examined their role in innate and learned responses. Activation of an ensemble of US-responsive cells in the BLA elicits innate physiological and behavioral responses of different valence. Activation of this US ensemble can also reinforce appetitive and aversive learning when paired with differing neutral stimuli. Moreover, we establish that the activation of US-responsive cells in the BLA is necessary for the expression of a conditioned response. Neural representations of conditioned and unconditioned stimuli therefore ultimately connect to US-responsive cells in the BLA to elicit both innate and learned responses.
    MeSH term(s) Animals ; Appetitive Behavior ; Basolateral Nuclear Complex/physiology ; Behavior, Animal ; Conditioning, Classical ; Learning ; Male ; Mice ; Mice, Inbred C57BL ; Reward
    Language English
    Publishing date 2015-07-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2015.06.027
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 58: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: “The splice is right”: how protein splicing is opening new doors in protein science

    Schwartz, Edmund C / Muir, Tom W / Tyszkiewicz, Amy B

    Chemical communications. 2003 Aug. 8, , no. 17

    2003  

    Abstract: In the decade since the discovery of protein splicing, this natural process has been exploited to develop novel techniques that have expanded the scope of protein science. These techniques are being adapted for in-vivo use, facilitating the study of ... ...

    Abstract In the decade since the discovery of protein splicing, this natural process has been exploited to develop novel techniques that have expanded the scope of protein science. These techniques are being adapted for in-vivo use, facilitating the study of proteins in their natural environment.
    Keywords chemical compounds ; chemical reactions ; proteins
    Language English
    Dates of publication 2003-0808
    Size p. 2087-2090.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b304989m
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article: A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding.

    Schwartz, Edmund C / Shekhtman, Alexander / Dutta, Kaushik / Pratt, Matthew R / Cowburn, David / Darst, Seth / Muir, Tom W

    Chemistry & biology

    2008  Volume 15, Issue 10, Page(s) 1091–1103

    Abstract: The sigma factors are the key regulators of bacterial transcription initiation. Through direct read-out of promoter DNA sequence, they recruit the core RNA polymerase to sites of initiation, thereby dictating the RNA polymerase promoter-specificity. The ... ...

    Abstract The sigma factors are the key regulators of bacterial transcription initiation. Through direct read-out of promoter DNA sequence, they recruit the core RNA polymerase to sites of initiation, thereby dictating the RNA polymerase promoter-specificity. The group 1 sigma factors, which direct the vast majority of transcription initiation during log phase growth and are essential for viability, are autoregulated by an N-terminal sequence known as sigma1.1. We report the solution structure of Thermotoga maritima sigmaA sigma1.1. We additionally demonstrate by using chemical crosslinking strategies that sigma1.1 is in close proximity to the promoter recognition domains of sigmaA. We therefore propose that sigma1.1 autoinhibits promoter DNA binding of free sigmaA by stabilizing a compact organization of the sigma factor domains that is unable to bind DNA.
    MeSH term(s) Amino Acid Sequence ; DNA/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Structure, Tertiary ; Sequence Alignment ; Sigma Factor/chemistry ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Thermotoga maritima/chemistry ; Thermotoga maritima/genetics ; Thermotoga maritima/metabolism
    Chemical Substances Sigma Factor ; DNA (9007-49-2)
    Language English
    Publishing date 2008-10-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 917827-2
    ISSN 1879-1301 ; 1074-5521
    ISSN (online) 1879-1301
    ISSN 1074-5521
    DOI 10.1016/j.chembiol.2008.09.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4429: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top