Courtney Zlatic

The Monomeric α-Crystallin Domain of the Small Heat-shock Proteins αB-crystallin and Hsp27 Binds Amyloid Fibril Ends.

Emily E Selig, Roberta J Lynn, Courtney O Zlatic, Yee-Foong Mok, Heath Ecroyd, Paul R Gooley, Michael DW Griffin

Journal article  |  2022  |  J Mol Biol

Small heat-shock proteins (sHSPs) are ubiquitously expressed molecular chaperones present in all kingdoms of life that inhibit pro..

N- and C-terminal regions of ?B-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation

Emily E Selig, Courtney O Zlatic, Dezerae Cox, Yee-Foong Mok, Paul R Gooley, Heath Ecroyd, Michael DW Griffin

Journal article  |  2020  |  JOURNAL OF BIOLOGICAL CHEMISTRY

Small heat-shock proteins (sHSPs) are ubiquitously expressed molecular chaperones that inhibit amyloid fibril formation; however, ..

The structure of the extracellular domains of human interleukin 11? receptor reveals mechanisms of cytokine engagement

Riley D Metcalfe, Kaheina Aizel, Courtney O Zlatic, Paul M Nguyen, Craig J Morton, Daisy Sio-Seng Lio, Heung-Chin Cheng, Renwick CJ Dobson, Michael W Parker, Paul R Gooley, Tracy L Putoczki, Michael DW Griffin

Journal article  |  2020  |  JOURNAL OF BIOLOGICAL CHEMISTRY

Interleukin (IL) 11 activates multiple intracellular signaling pathways by forming a complex with its cell surface α-receptor, IL-..

THE STRUCTURE OF THE INTERLEUKIN 11 SIGNALLING COMPLEX

Riley D Metcalfe, Kahenia Aizel, Courtney O Zlatic, Paul M Nguyen, Paul R Gooley, Tracy L Putoczki, Michael DW Griffin

Conference Proceedings  |  2019  |  PROTEIN SCIENCE

Polymorphism in disease-related apolipoprotein C-II amyloid fibrils: a structural model for rod-like fibrils

Courtney O Zlatic, Yu Mao, Nevena Todorova, Yee-Foong Mok, Geoffrey J Howlett, Irene Yarovsky, Paul R Gooley, Michael DW Griffin

Journal article  |  2018  |  FEBS JOURNAL

Human apolipoprotein (apo) C-II is one of several plasma apolipoproteins that form amyloid deposits in vivo and is an independent ..

Intra- and Intersubunit Ion-Pair Interactions Determine the Ability of Apolipoprotein C-II Mutants To Form Hybrid Amyloid Fibrils.

Nevena Todorova, Courtney O Zlatic, Yu Mao, Irene Yarovsky, Geoffrey J Howlett, Paul R Gooley, Michael DW Griffin

Journal article  |  2017  |  Biochemistry

The apolipoprotein family is structurally defined by amphipathic α-helical regions that interact with lipid surfaces. In the absen..

Intra- and Intersubunit Ion-Pair Interactions Determine the Ability of Apolipoprotein C-II Mutants To Form Hybrid Amyloid Fibrils

Nevena Todorova, Courtney O Zlatic, Yu Mao, Irene Yarovsky, Geoffrey J Howlett, Paul R Gooley, Michael DW Griffin

Journal article  |  2017  |  BIOCHEMISTRY

Solution Conditions Affect the Ability of the K30D Mutation To Prevent Amyloid Fibril Formation by Apolipoprotein C-II: Insights from Experiments and Theoretical Simulations

Yu Mao, Nevena Todorova, Courtney O Zlatic, Paul R Gooley, Michael DW Griffin, Geoffrey J Howlett, Irene Yarovsky

Journal article  |  2016  |  BIOCHEMISTRY

Apolipoproteins form amphipathic helical structures that bind lipid surfaces. Paradoxically, lipid-free apolipoproteins display a ..

Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II

Yu Mao, Courtney O Zlatic, Michael DW Griffin, Geoffrey J Howlett, Nevena Todorova, Irene Yarovsky, Paul R Gooley

Journal article  |  2015  |  BIOCHEMISTRY

Plasma apolipoproteins form amphipathic α helices in lipid environments but in the lipid-free state show a high propensity to form..

Fluphenazine center dot HCl and Epigallocatechin Gal late Modulate the Rate of Formation and Structural Properties of Apolipoprotein C-II Amyloid Fibrils

Courtney O Zlatic, Yu Mao, Timothy M Ryan, Yee-Foong Mok, Blaine R Roberts, Geoffrey J Howlett, Michael DW Griffin

Journal article  |  2015  |  BIOCHEMISTRY

Protein misfolding and aggregation, leading to amyloid fibril formation, are characteristic of many devastating and debilitating a..