H. Yao

发表

Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus

Xiaoqun Duan, Linbin Jiang, H. Yao, 2009, Biochemical and Biophysical Research Communications.

Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial Iron Homeostasis, Requires a Structural Anion Binding Site.

M. Rivera, Yan Wang, K. Battaile, 2018, Biochemistry.

Inhibiting the BfrB:Bfd interaction in Pseudomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron deficiency in the bacterial cytosol.

M. Rivera, Josephine R. Chandler, H. Yao, 2017, Metallomics : integrated biometal science.

Identification of angiogenesis-inhibiting peptides from Chan Su.

F. Gao, H. Yao, Y. Qian, 2019, Protein expression and purification.

Protein–protein Interactions Regulate the Release of Iron Stored in Bacterioferritin

M. Rivera, Yan Wang, H. Yao, 2016 .

Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center .

M. Rivera, C. J. Fischer, S. Weeratunga, 2010, Biochemistry.

Small Molecule Inhibitors of the BfrB–Bfd Interaction Decrease Pseudomonas aeruginosa Fitness and Potentiate Fluoroquinolone Activity

M. Rivera, B. Peterson, K. Battaile, 2019, Journal of the American Chemical Society.

Heme-iron utilization by Leptospira interrogans requires a heme oxygenase and a plastidic-type ferredoxin-NADP(+) reductase.

E. Ceccarelli, M. Rivera, H. Yao, 2014, Biochimica et biophysica acta.

Pseudomonas aeruginosa Bacterioferritin Is Assembled from FtnA and BfrB Subunits with the Relative Proportions Dependent on the Environmental Oxygen Availability

M. Rivera, Josephine R. Chandler, H. Yao, 2022, Biomolecules.

Inhibiting Iron Mobilization from Bacterioferritin in Pseudomonas aeruginosa Impairs Biofilm Formation Irrespective of Environmental Iron Availability

M. Rivera, Josephine R. Chandler, H. Yao, 2020, ACS infectious diseases.

Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein.

W. Im, Yifei Qi, M. Rivera, 2016, Biochemistry.

Substrate induced structural and dynamics changes in human phosphomevalonate kinase and implications for mechanism

Supa Hannongbua, Daniel S Sem, D. Sem, 2009, Proteins.

Structural characterization of the transmembrane domain from subunit e of yeast F1Fo-ATP synthase: a helical GXXXG motif located just under the micelle surface.

R. Stuart, D. Sem, H. Yao, 2008, Biochemistry.

Structural evidence for a functionally relevant second camphor binding site in P450cam: Model for substrate entry into a P450 active site

A. Costache, D. Sem, H. Yao, 2007, Proteins.

NMR dynamics investigation of ligand induced changes of main and side chain arginine N‐H's in human phosphomevalonate kinase

Daniel S Sem, D. Sem, H. Miziorko, 2009, Journal of the American Chemical Society.

Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa

M. Rivera, K. Battaile, H. Yao, 2014, Biochemistry.

Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: identification of a rare cCMP cofactor preference

D. Sem, H. Yao, Daniel S. Sem, 2005, FEBS letters.

Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity

M. Rivera, K. Battaile, H. Yao, 2023, International journal of molecular sciences.

Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein–Protein Interaction in Solution and Determination of Binding Energy Hot Spots

M. Rivera, Yan Wang, K. Battaile, 2015, Biochemistry.

Concerted motions networking pores and distant ferroxidase centers enable bacterioferritin function and iron traffic.

W. Im, M. Rivera, H. Rui, 2015, Biochemistry.

The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin.

I. Vakser, A. M. Ruvinsky, M. Rivera, 2012, Journal of the American Chemical Society.

Two distinct ferritin-like molecules in Pseudomonas aeruginosa: the product of the bfrA gene is a bacterial ferritin (FtnA) and not a bacterioferritin (Bfr).

M. Rivera, S. Weeratunga, K. Battaile, 2011, Biochemistry.

Chemical Proteomic Tool for Ligand Mapping of CYP Antitargets: An NMR-Compatible 3D QSAR Descriptor in the Heme-Based Coordinate System

Huili Yao, Aurora D. Costache, Daniel S. Sem, 2004, J. Chem. Inf. Model..

Small Molecule Inhibitors of the Bacterioferritin (BfrB)–Ferredoxin (Bfd) Complex Kill Biofilm-Embedded Pseudomonas aeruginosa Cells

M. Rivera, K. Battaile, H. Yao, 2020, ACS infectious diseases.

Two distinct ferritin-like molecules in P . aeruginosa : The product of the bfrA gene is a bacterial ferritin ( FtnA ) not a bacterioferritin ( Bfr ) †

M. Rivera, S. Weeratunga, K. Battaile, 2011 .

Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center .

M. Rivera, C. J. Fischer, S. Weeratunga, 2010, Biochemistry.

Pseudomonas aeruginosa gene PA4880 encodes a Dps-like protein with a Dps fold, bacterioferritin-type ferroxidase centers, and endonuclease activity

K. Battaile, H. Yao, Lijun Liu, 2024, Frontiers in molecular biosciences.