Elizabeth A. Craig

Elizabeth A. Craig is a Steenbock Professor of Microbial Science and faculty member in the Biochemistry Department at the University of Wisconsin-Madison. She was elected to the National Academy of Sciences in 1998. Research in her laboratory concentrates on the folding and remodeling of proteins in the cell via molecular chaperones. Provided by Wikipedia
Showing 1 - 10 results of 10 for search 'Elizabeth A Craig', query time: 0.07s Refine Results
  1. 1
    Interaction of client—the scaffold on which FeS clusters are build—with J-domain protein Hsc20 and its evolving Hsp70 partners

    Interaction of client—the scaffold on which FeS clusters are build—with J-domain protein Hsc20 and its evolving Hsp70 partners by Jaroslaw Marszalek, Elizabeth A. Craig

    Published 2022-10-01
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  2. 2
    Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23

    Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23 by See-Yeun Ting, Nicholas L Yan, Brenda A Schilke, Elizabeth A Craig

    Published 2017-04-01
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  3. 3
    Pathway of Hsp70 interactions at the ribosome

    Pathway of Hsp70 interactions at the ribosome by Kanghyun Lee, Thomas Ziegelhoffer, Wojciech Delewski, Scott E. Berger, Grzegorz Sabat, Elizabeth A. Craig

    Published 2021-09-01
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  4. 4
    Correction: [], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity.

    Correction: [], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. by Justin K. Hines, Xiaomo Li, Zhiqiang Du, Takashi Higurashi, Liming Li, Elizabeth A. Craig

    Published 2011-02-01
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  5. 5
    [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.

    [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity. by Justin K Hines, Xiaomo Li, Zhiqiang Du, Takashi Higurashi, Liming Li, Elizabeth A Craig

    Published 2011-02-01
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  6. 6
    Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.

    Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. by Brenda A Schilke, Szymon J Ciesielski, Thomas Ziegelhoffer, Erina Kamiya, Marco Tonelli, Woonghee Lee, Gabriel Cornilescu, Justin K Hines, John L Markley, Elizabeth A Craig

    Published 2017-10-01
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  7. 7
    Two-step mechanism of J-domain action in driving Hsp70 function.

    Two-step mechanism of J-domain action in driving Hsp70 function. by Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A Uzarska, Szymon J Ciesielski, Jacek Czub, Elizabeth A Craig, Jaroslaw Marszalek

    Published 2020-06-01
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  8. 8
    Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.

    Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70. by Om Kumar Shrestha, Ruchika Sharma, Bartlomiej Tomiczek, Woonghee Lee, Marco Tonelli, Gabriel Cornilescu, Milena Stolarska, Lukasz Nierzwicki, Jacek Czub, John L Markley, Jaroslaw Marszalek, Szymon J Ciesielski, Elizabeth A Craig

    Published 2019-01-01
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  9. 9
    Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function

    Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function by Samantha J. Ganser, Bridget A. McNish, Gillian L. Schwanitz, John L. Delaney, Bridget A. Corpus, Brenda A. Schilke, Anup K. Biswal, Chandan Sahi, Elizabeth A. Craig, Justin K. Hines

    Published 2024-04-01
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  10. 10
    The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation

    The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation by Ryo Yonashiro, Erich B Tahara, Mario H Bengtson, Maria Khokhrina, Holger Lorenz, Kai-Chun Chen, Yu Kigoshi-Tansho, Jeffrey N Savas, John R Yates III, Steve A Kay, Elizabeth A Craig, Axel Mogk, Bernd Bukau, Claudio AP Joazeiro

    Published 2016-03-01
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