A5018033735- Hemoglobin structure and function
- Streptococcal Infections and Treatments
- Neonatal Health and Biochemistry
- Iron Metabolism and Disorders
- Protein Structure and Dynamics
- Clostridium difficile and Clostridium perfringens research
- Enzyme Structure and Function
- Antimicrobial Resistance in Staphylococcus
- Advanced NMR Techniques and Applications
- Tuberculosis Research and Epidemiology
- RNA and protein synthesis mechanisms
- Mycobacterium research and diagnosis
- Hemoglobinopathies and Related Disorders
- Alzheimer's disease research and treatments
- Erythrocyte Function and Pathophysiology
- Biochemical and Structural Characterization
- Heme Oxygenase-1 and Carbon Monoxide
- CAR-T cell therapy research
- Click Chemistry and Applications
- Electron Spin Resonance Studies
- Monoclonal and Polyclonal Antibodies Research
- Botulinum Toxin and Related Neurological Disorders
- Bacterial Genetics and Biotechnology
University of California, Los Angeles
2015-2023
UCLA Health
2018
Genomics (United Kingdom)
2018
Howard Hughes Medical Institute
2015
Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting out-of-register β sheets, which may constitute one the toxic species in aggregation related diseases. Here we sought to determine presence such motif islet amyloid polypeptide (IAPP), whose properties are associated with type 2 diabetes. We determined four new crystal structures within IAPP, all forming steric zippers. Most interestingly, fibril core IAPP forms an zipper....
Staphylococcus aureus is a leading cause of life-threatening infections in the United States. It actively acquires essential nutrient iron from human hemoglobin (Hb) using iron-regulated surface-determinant (Isd) system. This process initiated when closely related bacterial IsdB and IsdH receptors bind to Hb extract its hemin through conserved tri-domain unit that contains two NEAr Transporter (NEAT) domains are connected by helical linker domain. Previously, we demonstrated within...
Streptococcus pyogenes (group A Streptococcus) is a clinically important microbial pathogen that requires iron in order to proliferate. During infections, S. uses the surface displayed Shr receptor capture human hemoglobin (Hb) and acquires its iron-laden heme molecules. Through poorly understood mechanism, engages Hb via two structurally unique N-terminal Hb-interacting domains (HID1 HID2) which facilitate transfer proximal NEAr Transporter (NEAT) domains. Based on results of X-ray...
Iron is a versatile metal cofactor that used in wide range of essential cellular processes. During infections, many bacterial pathogens acquire iron from human hemoglobin (Hb), which contains the majority body's total content form heme (iron protoporphyrin IX). Clinically important Gram-positive scavenge using an array secreted and cell-wall-associated receptors contain NEAr-iron Transporter (NEAT) domains. Experimentally defining Hb binding properties NEAT domains has been challenging,...
Abstract We present the Indinavir Ligand Induced Transient Engagement switch (IDV LITE Switch), a fully synthetic Chemically Dimerization (CID) system wherein two humanized antibody fragments are heterodimerized by antiviral drug indinavir. The IDV Switch represents first CID made from protein components and dimerized clinically approved small molecule lacking mammalian target, making it an ideal bioorthogonal molecular for application in small-molecule controlled therapeutics.
Staphylococcus aureus is a bacterial pathogen that actively procures iron from its host in order to successfully establish an infection. Heme (Iron–protoporphyrin IX) bound hemoglobin (Hb) the most abundant source of human body and preferentially captured by S. aureus. It uses two highly conserved iron-regulated surface determinant (Isd) proteins bind Hb extract oxidized form heme (hemin), IsdH IsdB. Both receptors rapidly hemin using tri-domain unit consisting NEAT (near transporter)...
Our research seeks to learn how Gram‐positive pathogens acquire iron from the human host, a key process required for bacterial pathogenesis and potential drug target. In particular, focus of our work is mechanism heme extraction hemoglobin (Hb), main source in body. an effort decipher this process, we are using combination biochemical biophysical methods including X‐ray crystallography, isothermal titration calorimetry (ITC), nuclear magnetic resonance (NMR), analytical ultra‐centrifugation...