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Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones.

Expert reviews in molecular medicine

Ranford JC, Coates AR, Henderson B.
PMID: 14585136
Expert Rev Mol Med. 2000 Sep 15;2(8):1-17. doi: 10.1017/S1462399400002015.

The chaperonins are a subgroup of oligomeric molecular chaperones; the best-studied examples are chaperonin 60 (GroEL) and chaperonin 10 (GroES), both from the bacterium Escherichia coli. At the end of the 20th century, the paradigm of chaperonins as protein...

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Ranford JC, Coates AR, Henderson B. Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med. 2000;2(8):1-17doi: 10.1017/S1462399400002015.
Ranford, J. C., Coates, A. R., & Henderson, B. (2000). Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert reviews in molecular medicine, 2(8), 1-17. https://doi.org/10.1017/S1462399400002015
Ranford, J C, et al. "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones." Expert reviews in molecular medicine vol. 2,8 (2000): 1-17. doi: https://doi.org/10.1017/S1462399400002015
Ranford JC, Coates AR, Henderson B. Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med. 2000 Sep 15;2(8):1-17. doi: 10.1017/S1462399400002015. PMID: 14585136.
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Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics.

Frontiers in molecular biosciences

Meng Q, Li BX, Xiao X.
PMID: 29732373
Front Mol Biosci. 2018 Apr 20;5:35. doi: 10.3389/fmolb.2018.00035. eCollection 2018.

The 60 kDa heat shock protein (Hsp60) is classically known as a mitochondrial chaperonin protein working together with co-chaperonin 10 kDa heat shock protein (Hsp10). This chaperonin complex is essential for folding proteins newly imported into mitochondria. However, Hsp60,...

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Meng Q, Li BX, Xiao X. Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics. Front Mol Biosci. 2018;5:35doi: 10.3389/fmolb.2018.00035.
Meng, Q., Li, B. X., & Xiao, X. (2018). Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics. Frontiers in molecular biosciences, 535. https://doi.org/10.3389/fmolb.2018.00035
Meng, Qianli, et al. "Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics." Frontiers in molecular biosciences vol. 5 (2018): 35. doi: https://doi.org/10.3389/fmolb.2018.00035
Meng Q, Li BX, Xiao X. Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics. Front Mol Biosci. 2018 Apr 20;5:35. doi: 10.3389/fmolb.2018.00035. eCollection 2018. PMID: 29732373; PMCID: PMC5920047.
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Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi.

Cytotechnology

Han X, Wang Z, Wang W, Bai R, Zhao P, Shang J.
PMID: 24801578
Cytotechnology. 2014 Aug;66(4):567-74. doi: 10.1007/s10616-013-9604-0. Epub 2014 May 07.

The activation of phase-specific cyclin-dependent kinases is associated with ordered cell cycle transitions. Among the mammalian Cdks, Cdk2 is essential for liver cancer cell proliferation. The related cycling protein CDK2 was analyzed by 2D-gel and MALDI-TOF/TOF MS mass assay...

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Han X, Wang Z, Wang W, et al. Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi. Cytotechnology. 2014;66(4):567-74doi: 10.1007/s10616-013-9604-0.
Han, X., Wang, Z., Wang, W., Bai, R., Zhao, P., & Shang, J. (2014). Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi. Cytotechnology, 66(4), 567-74. https://doi.org/10.1007/s10616-013-9604-0
Han, Xiaofang, et al. "Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi." Cytotechnology vol. 66,4 (2014): 567-74. doi: https://doi.org/10.1007/s10616-013-9604-0
Han X, Wang Z, Wang W, Bai R, Zhao P, Shang J. Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi. Cytotechnology. 2014 Aug;66(4):567-74. doi: 10.1007/s10616-013-9604-0. Epub 2014 May 07. PMID: 24801578; PMCID: PMC4082776.
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Systematic Review of Postfertilization Effects and Potential for Embryo Formation and Loss during the Use of Intrauterine Devices.

The Linacre quarterly

Buskmiller C, Harrison D, Ruppersberger LA, Yeung PP.
PMID: 32431449
Linacre Q. 2020 Feb;87(1):60-77. doi: 10.1177/0024363919854289. Epub 2019 Jun 27.

OBJECTIVES: This review sought to evaluate the evidence for embryo formation during intrauterine device (IUD) use, to articulate how often embryo loss occurs in well-designed studies, and to comment on other bodies of literature suggestive of postfertilization mechanisms of...

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Buskmiller C, Harrison D, Ruppersberger LA, et al. Systematic Review of Postfertilization Effects and Potential for Embryo Formation and Loss during the Use of Intrauterine Devices. Linacre Q. 2019;87(1):60-77doi: 10.1177/0024363919854289.
Buskmiller, C., Harrison, D., Ruppersberger, L. A., & Yeung, P. P. (2020). Systematic Review of Postfertilization Effects and Potential for Embryo Formation and Loss during the Use of Intrauterine Devices. The Linacre quarterly, 87(1), 60-77. https://doi.org/10.1177/0024363919854289
Buskmiller, Cara, et al. "Systematic Review of Postfertilization Effects and Potential for Embryo Formation and Loss during the Use of Intrauterine Devices." The Linacre quarterly vol. 87,1 (2020): 60-77. doi: https://doi.org/10.1177/0024363919854289
Buskmiller C, Harrison D, Ruppersberger LA, Yeung PP. Systematic Review of Postfertilization Effects and Potential for Embryo Formation and Loss during the Use of Intrauterine Devices. Linacre Q. 2020 Feb;87(1):60-77. doi: 10.1177/0024363919854289. Epub 2019 Jun 27. PMID: 32431449; PMCID: PMC7016440.
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Showing 1 to 4 of 4 entries