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Wladimir Labeikovsky
Researcher at Howard Hughes Medical Institute
Publications - 11
Citations - 1476
Wladimir Labeikovsky is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Creatine kinase & Protein structure. The author has an hindex of 8, co-authored 10 publications receiving 1412 citations. Previous affiliations of Wladimir Labeikovsky include National Science Foundation & Rockefeller University.
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Journal ArticleDOI
Intrinsic dynamics of an enzyme underlies catalysis
Elan Z. Eisenmesser,Oscar Millet,Wladimir Labeikovsky,Dmitry M. Korzhnev,Magnus Wolf-Watz,Magnus Wolf-Watz,Daryl A. Bosco,Daryl A. Bosco,Jack J. Skalicky,Jack J. Skalicky,Lewis E. Kay,Dorothee Kern +11 more
TL;DR: It is shown that the intrinsic plasticity of the protein is a key characteristic of catalysis, and the pre-existence of collective dynamics in enzymes before catalysis is a common feature of biocatalysts and that proteins have evolved under synergy pressure between structure and dynamics.
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Transient Non-native Hydrogen Bonds Promote Activation of a Signaling Protein
Alexandra K. Gardino,Janice Villali,Aleksandr Kivenson,Ming Lei,Ce Feng Liu,Phillip Steindel,Elan Z. Eisenmesser,Wladimir Labeikovsky,Magnus Wolf-Watz,Michael W. Clarkson,Dorothee Kern +10 more
TL;DR: The data show that the loss of native stabilizing contacts during activation is compensated by non-native transient atomic interactions during the transition, which unravel atomistic details of native-state protein energy landscapes by expanding the knowledge about ground states to transition landscapes.
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Structure and dynamics of Pin1 during catalysis by NMR
TL;DR: The backbone dynamics of the peptidylprolyl isomerase (Pin1) catalytic domain in the free state and during catalysis are characterized and suggest a model for the reaction trajectory of Pin1 catalysis.
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Solution characterization of the extracellular region of CD147 and its interaction with its enzyme ligand cyclophilin A.
Jennifer Schlegel,Jasmina S. Redzic,Christopher C. Porter,Vyacheslav Yurchenko,Michael Bukrinsky,Wladimir Labeikovsky,Geoffrey S. Armstrong,Fengli Zhang,Nancy G. Isern,James DeGregori,Robert S. Hodges,Elan Z. Eisenmesser +11 more
TL;DR: The solution behavior of the two most prevalent CD147 extracellular isoforms are characterized through biochemical methods that include gel-filtration and native gel analysis as well as directly through multiple NMR methods, which suggest that CD147 homophilic interactions in vivo are mediated through other partners.
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Changes in the mitochondrial proteome from mouse hearts deficient in creatine kinase
TL;DR: It is discovered that the loss of MM- and ScMit-CK isoforms did not cause large scale changes in heart mitochondrial proteins, and two mitochondrial protein differences have been found in the parent mouse strains of the DbKO-Ck mice.