Yetunde A. Ayinuola

发表

Group A Streptococcus-Induced Activation of Human Plasminogen Is Required for Keratinocyte Wound Retraction and Rapid Clot Dissolution

F. Castellino, V. Ploplis, Shaun W. Lee, 2021, Frontiers in Cardiovascular Medicine.

Binding of the kringle‐2 domain of human plasminogen to streptococcal PAM‐type M‐protein causes dissociation of PAM dimers

F. Castellino, V. Ploplis, Shaun W. Lee, 2021, MicrobiologyOpen.

The M Protein of Streptococcus pyogenes Strain AP53 Retains Cell Surface Functional Plasminogen Binding after Inactivation of the Sortase A Gene

V. Fischetti, F. Castellino, V. Ploplis, 2020, Journal of bacteriology.

Structure and Function Characterization of the a1a2 Motifs of Streptococcus pyogenes M Protein in Human Plasminogen Binding.

J. Whisstock, R. Law, P. Conroy, 2019, Journal of molecular biology.

Evolution of Streptococcus pyogenes has maximized the efficiency of the Sortase A cleavage motif for cell wall transpeptidation

V. Fischetti, F. Castellino, V. Ploplis, 2022, The Journal of biological chemistry.

Evolution of Gram+ Streptococcus pyogenes has maximized efficiency of the Sortase A cleavage site

V. Fischetti, F. Castellino, V. Ploplis, 2021, bioRxiv.

Proteomic identification of an alpha class glutathione S-transferase in freshwater snails (Bulinus globosus)

I. O. Adewale, Yetunde A. Ayinuola, 2019, Animal Biology.

hPg. PAM is covalently bound to the cell wall (CW) through cell membrane (CM)-resident 24 sortase A (SrtA)-catalyzed cleavage of the PAM-proximal C-terminal LPST

V. Fischetti, F. Castellino, V. Ploplis, 2021 .

Inactivation of the lysine binding sites of human plasminogen (hPg) reveals novel structural requirements for the tight hPg conformation, M-protein binding, and rapid activation

F. Castellino, Yetunde A. Ayinuola, 2023, Frontiers in Molecular Biosciences.

Streptococcus co-opts a conformational lock in human plasminogen to facilitate streptokinase cleavage and bacterial virulence

F. Castellino, V. Ploplis, Shaun W. Lee, 2020, The Journal of biological chemistry.

A high-resolution single-particle cryo-EM hydrated structure of Streptococcus pyogenes enolase offers insights into its function as a plasminogen receptor

F. Castellino, Yetunde A. Ayinuola, Bradley M. Readnour, 2022, bioRxiv.

Solution structure of VEK50 in the bound form with plasminogen kringle 2

J. Whisstock, R. Law, F. Castellino, 2019 .

Relationships Between Plasminogen-Binding M-Protein and Surface Enolase for Human Plasminogen Acquisition and Activation in Streptococcus pyogenes

V. Fischetti, F. Castellino, V. Ploplis, 2022, Frontiers in Microbiology.

Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes.

J. Whisstock, R. Law, F. Castellino, 2019, Journal of structural biology.

Binding of the kringle‐2 domain of human plasminogen to streptococcal PAM‐type M‐protein causes dissociation of PAM dimers

F. Castellino, V. Ploplis, Shaun W. Lee, 2021, MicrobiologyOpen.