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1

The molecular chaperones interaction networks in protein folding and degradation. Springer, 2014.

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2

Houry, Walid A., ed. The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1130-1.

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3

Protein and peptide folding, misfolding, and non-folding. John Wiley & Sons, 2012.

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4

Molecular chaperones of the endoplasmic reticulum. Nova Science Publishers, 2010.

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5

Foldase enzymes catalyzing protein folding. Nova Science Publishers, 2008.

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6

Olden, Darren Michael. The roles of molecular chaperones, with particular reference to GroEL, during protein folding in escherichia coli. University of Birmingham, 1997.

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7

Macario, Alberto J. L. The chaperonopathies: Diseases with defective molecular chaperones : an introduction and guide to diseases in which chaperones play an etiologic-pathogenic role. Springer, 2013.

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8

Jackson, Sophie. Molecular Chaperones. Springer, 2015.

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9

Jackson, Sophie. Molecular Chaperones. Springer, 2012.

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10

Jackson, Sophie. Molecular Chaperones. Springer, 2012.

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11

H, Lorimer G., and Baldwin Thomas O, eds. Molecular chaperones. Academic Press, 1998.

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12

L, Blatch Gregory, ed. Networking of chaperones by co-chaperones. Landes Bioscience/Eurekah.com, 2007.

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13

Houry, Walid A. The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Springer, 2016.

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14

Mary-Jane, Gething, ed. Guidebook to the molecular chaperones and protein-folding catalysts. Oxford University Press, 1997.

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15

Structure and Action of Molecular Chaperones: Machines That Assist Protein Folding in the Cell. World Scientific Publishing Co Pte Ltd, 2016.

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16

Bakau, Bernd. Molecular Chaperones and Folding Catalysts: Regulation, Cellular Functions and Mechanisms. CRC, 1999.

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17

Schweitzer-Stenner, Reinhard, and Vladimir Uversky. Protein and Peptide Folding, Misfolding, and Non-Folding. Wiley & Sons, Incorporated, John, 2012.

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18

Schweitzer-Stenner, Reinhard, and Vladimir Uversky. Protein and Peptide Folding, Misfolding, and Non-Folding. Wiley & Sons, Incorporated, John, 2012.

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19

Schweitzer-Stenner, Reinhard, and Vladimir Uversky. Protein and Peptide Folding, Misfolding, and Non-Folding. Wiley & Sons, Incorporated, John, 2012.

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20

(Editor), John N. Abelson, Melvin I. Simon (Editor), George H. Lorimer (Editor), and Thomas O. Baldwin (Editor), eds. Methods in Enzymology, Volume 290: Molecular Chaparones (Methods in Enzymology). Academic Press, 1998.

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21

(Editor), Johannes Buchner, and Thomas Kiefhaber (Editor), eds. Protein Folding Handbook 5-volume set. Wiley-VCH, 2005.

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22

Gething, Mary-Jane. Guidebook to Molecular Chaperones and Protein-Folding Catalysts (Guidebook Series (Oxford, England).). A Sambrook and Tooze Publication at Oxford University Press, 1998.

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23

Prof, Bukau Bernd, ed. Molecular chaperones and folding catalysts: Regulation, cellular function, and mechanisms. Harwood Academic Publishers, 1999.

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24

Folding For The Synapse. Springer, 2010.

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25

Molecular design and modeling: Concepts and applications. Academic Press, 1991.

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26

Csermely, Peter, and László Vígh. Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Springer, 2010.

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27

(Editor), Peter Csermely, and László Vígh (Editor), eds. Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks (Advances in Experimental Medicine and Biology). Springer, 2006.

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28

1944-, Langone John J., ed. Molecular design and modeling: Concepts and applications. Part A, Proteins, peptides, and enzymes. Academic Press, 1991.

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29

J, Langone John, ed. Molecular design and modeling: Concepts and applications. Academic Press, 1991.

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30

Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Abstract:
Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (U
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