Author

A. Laganowsky

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 5 Biophysics· 1 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 4 Assay:proteomics· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Research Focus:development & morphogenesis· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

J. Lyu· 3 shared D. H. Russell· 2 shared L. Wang· 2 shared M. Zhou· 2 shared T. Zhang· 2 shared A. Aggarwal· 1 shared A. Pillai· 1 shared A. Tripathi· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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3 shared papersBiochemistry

J. Lyu

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Symmetry facilitated the evolution of specificity and high-order stoichiometry in vertebrate hemoglobin

C. R. Cortez-Romero, J. Lyu, A. Pillai, A. Laganowsky, J. W. Thornton

This study investigates how vertebrate hemoglobin evolved from a homodimeric ancestor to a heterotetramer through simple genetic changes that exploited symmetry in its structure.

bioRxiv · Jul 24, 2024Evolutionary Biology

Native mass spectrometry of membrane protein-lipid interactions in different detergent environments

S. Kumar, L. Stover, L. Wang, H. Bahramimoghaddam, M. Zhou, D. H. Russll, A. Laganowsky

This study uses native mass spectrometry to investigate how different detergents and charge-reducing molecules affect protein-lipid interactions in membrane proteins.

bioRxiv · Jun 27, 2024Biochemistry

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions

J. Lyu, T. Zhang, M. Marty, D. Clemmer, D. H. Russell, A. Laganowsky

The paper uses native mass spectrometry and mutant cycles to study the thermodynamics of MsbA-LPS interactions, revealing entropy-driven binding and conformational changes.

bioRxiv · Jul 3, 2023Biochemistry

Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time

T. Walker, H. M. Sun, T. Gunnels, V. Wysocki, A. Laganowsky, H. Rye, D. H. Russell

This paper uses variable-temperature electrospray ionization native mass spectrometry to study the thermodynamics of ATP binding to the GroEL complex, revealing enthalpy-entropy compensation and cooperativity.

bioRxiv · Sep 13, 2022Biophysics

Structural basis for lipid and copper regulation of the ABC transporter MsbA

J. Lyu, C. Liu, T. Zhang, S. Schrecke, N. Elam, G. Hocberg, D. Russell, M. Zhao, A. Laganowsky

This study uses native mass spectrometry and structural analysis to show how copper and lipids regulate the ABC transporter MsbA, revealing a conserved KLA binding site that modulates ATPase activity.

bioRxiv · Aug 4, 2022Biochemistry

A Sec14-like Phosphatidylinositol Transfer Protein Paralog Defines a Novel Class of Heme-binding Proteins With An Unusual Heme Coordination Mechanism

D. Khan, D. Lee, G. Gulten, A. Aggarwal, J. Wofford, K. V. Inna, A. Tripathi, J. W. Patrick, D. M. Eckert, A. Laganowsky, J. C. Sacchettini, P. Lindahl, V. Bankaitis

The paper identifies Sfh5 as a novel heme-binding protein with an unusual coordination mechanism, distinct from its Sec14-like PITP family members.

bioRxiv · Mar 19, 2020Biochemistry

Structure and mechanism of a primate ferroportin

Z. Ren, S. Gao, J. Shen, L. Wang, Z. Xu, Y. Yu, P. Bachina, H. Zhang, A. Laganowsky, N. Yan, M. Zhou, Y. Pan

This study presents the structure of primate ferroportin and elucidates its mechanism of iron transport and regulation by hepcidin.

bioRxiv · Mar 4, 2020Biochemistry