Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones

Authors: Erik B. Nordquist, Charles A. English, Eugenia M. Clerico, Woody Sherman, Lila M. Gierasch, Jianhan Chen

Source: PLoS Computational Biology, Vol 17, Iss 11 (2021)

Subject Terms: Biology (General), QH301-705.5

File Description: electronic resource

Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604352/?tool=EBI; https://doaj.org/toc/1553-734X; https://doaj.org/toc/1553-7358

Access URL: https://doaj.org/article/ad3b0c700af84c299fcbf138aa4bb030

The data must be accessible to all

Authors: Lila M. Gierasch, Nicholas O. Davidson, Kerry-Anne Rye, Alma L. Burlingame

Source: Journal of Lipid Research, Vol 61, Iss 4, Pp 465- (2020)

Subject Terms: Biochemistry, QD415-436

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S0022227520434959; https://doaj.org/toc/0022-2275

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Opening ASBMB publications freely to all

Authors: Lila M. Gierasch, Nicholas O. Davidson, Kerry-Anne Rye, Alma L. Burlingame

Source: Journal of Lipid Research, Vol 61, Iss 7, Pp 969-970 (2020)

Subject Terms: Biochemistry, QD415-436

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S0022227520435746; https://doaj.org/toc/0022-2275

Access URL: https://doaj.org/article/57775e5fa3d74dfa9875d8ac19f1db17

For the sake of science

Authors: Lila M. Gierasch, Nicholas O. Davidson, Kerry-Anne Rye, Alma L. Burlingame

Source: Journal of Lipid Research, Vol 60, Iss 4, Pp 719-720 (2019)

Subject Terms: Biochemistry, QD415-436

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S0022227520325827; https://doaj.org/toc/0022-2275

Access URL: https://doaj.org/article/609afc84676148418e43cb4414f42001

Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli

Authors: Younhee Cho, Xin Zhang, Kristine Faye R. Pobre, Yu Liu, David L. Powers, Jeffery W. Kelly, Lila M. Gierasch, Evan T. Powers

Source: Cell Reports, Vol 11, Iss 2, Pp 321-333 (2015)

Subject Terms: Biology (General), QH301-705.5

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S2211124715002715; https://doaj.org/toc/2211-1247

Access URL: https://doaj.org/article/91b493a5c85e427482a2079d643a323c

FoldEco: A Model for Proteostasis in E. coli

Authors: Evan T. Powers, David L. Powers, Lila M. Gierasch

Source: Cell Reports, Vol 1, Iss 3, Pp 265-276 (2012)

Subject Terms: Biology (General), QH301-705.5

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S221112471200068X; https://doaj.org/toc/2211-1247

Access URL: https://doaj.org/article/13cc089476ab47478bc2785c13568b47

An interdomain sector mediating allostery in Hsp70 molecular chaperones

Authors: Robert G Smock, Olivier Rivoire, William P Russ, Joanna F Swain, Stanislas Leibler, Rama Ranganathan, Lila M Gierasch

Source: Molecular Systems Biology, Vol 6, Iss 1, Pp 1-10 (2010)

Subject Terms: allostery, chaperone, co‐evolution, SCA, sector, Biology (General), QH301-705.5, Medicine (General), R5-920

File Description: electronic resource

Relation: https://doaj.org/toc/1744-4292

Access URL: https://doaj.org/article/b2ba0e6b5cfe4e2a91bd8ce9f67a48bb

Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions.

Authors: Kannan Gunasekaran, Arnold T. Hagler, Lila M. Gierasch

Source: Proteins; Feb2004, Vol. 54 Issue 2, p179-194, 16p

Subject Terms: CARRIER proteins, LIPIDS, TRETINOIN, AMINO acids

Inaugural editorial.

Authors: Lila M. Gierasch

Source: Biopolymers; Apr2004, Vol. 76 Issue 1, p1-2, 2p

ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.

Authors: Ignacio J General, Ying Liu, Mandy E Blackburn, Wenzhi Mao, Lila M Gierasch, Ivet Bahar

Source: PLoS Computational Biology, Vol 10, Iss 5, p e1003624 (2014)

Subject Terms: Biology (General), QH301-705.5

File Description: electronic resource

Relation: http://europepmc.org/articles/PMC4022485?pdf=render; https://doaj.org/toc/1553-734X; https://doaj.org/toc/1553-7358

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Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.

Authors: Ying Liu, Lila M Gierasch, Ivet Bahar

Source: PLoS Computational Biology, Vol 6, Iss 9 (2010)

Subject Terms: Biology (General), QH301-705.5

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Relation: http://europepmc.org/articles/PMC2940730?pdf=render; https://doaj.org/toc/1553-734X; https://doaj.org/toc/1553-7358

Access URL: https://doaj.org/article/36664d7621be4d72a558875902a7430f