Andrew K. Goring

ORCID: 0000-0003-4220-6472
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About
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Research Areas
  • Diphtheria, Corynebacterium, and Tetanus
  • Clostridium difficile and Clostridium perfringens research
  • Mass Spectrometry Techniques and Applications
  • Hemoglobin structure and function
  • Bacterial Genetics and Biotechnology
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Endoplasmic Reticulum Stress and Disease
  • Neonatal Health and Biochemistry
  • Toxin Mechanisms and Immunotoxins
  • Advanced Proteomics Techniques and Applications
  • Fungal and yeast genetics research
  • Bacterial Identification and Susceptibility Testing
  • Erythrocyte Function and Pathophysiology
  • Peptidase Inhibition and Analysis
  • Bioinformatics and Genomic Networks
  • Microbial infections and disease research
  • Alzheimer's disease research and treatments
  • Signaling Pathways in Disease
  • Wnt/β-catenin signaling in development and cancer
  • Gut microbiota and health
  • 14-3-3 protein interactions
  • Microbial Community Ecology and Physiology
  • Genomics and Phylogenetic Studies
  • Cancer-related gene regulation

University of California, Berkeley
2024

University of California, Los Angeles
2020-2024

Santa Barbara City College
2018

University of California, Santa Barbara
2018

Tau filaments formed with heparin are structurally different from Alzheimer's disease extracted human brains. Heparin creates heterogeneous in which tau proteins locally stretched and have minimal large-domain structuration.

10.1039/c8cc01355a article EN Chemical Communications 2018-01-01

Native mass spectrometry (MS) of proteins and protein assemblies reveals size binding stoichiometry, but elucidating structures to understand their function is more challenging. top-down MS (nTDMS), i.e., fragmentation the gas-phase protein, conventionally used derive sequence information, locate post-translational modifications (PTMs), pinpoint ligand sites. nTDMS also endeavors dissociate covalent bonds in a conformation-sensitive manner, such that information about higher-order structure...

10.1021/jacs.2c06726 article EN Journal of the American Chemical Society 2022-11-28

Amyloid aggregation of the intrinsically disordered protein (IDP) tau is involved in several diseases, called tauopathies. Some tauopathies can be inherited due to mutations gene encoding tau, which might favor formation amyloid fibrils. This work aims at deciphering mechanisms through disease-associated single-point promote formation. We combined biochemical and biophysical characterization, notably, small-angle X-ray scattering (SAXS), study six different FTDP-17 derived mutations. found...

10.1021/jacsau.3c00550 article EN cc-by JACS Au 2023-12-19

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...

10.1073/pnas.2211939120 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2023-01-24

Abstract Amyloid aggregation of the intrinsically disordered protein (IDP) tau is involved in several diseases, called tauopathies. Mutations gene encoding are responsible for a class inherited tauopathies frontotemporal dementia and parkinsonism linked to chromosome 17Q (FTDP-17). These mutations thought trigger FTDP-17 by favoring formation amyloid fibrils. This work aims at deciphering mechanisms through which diseases-associated single point promote formation. We combined biochemical...

10.1101/2023.05.12.540512 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-05-14

Parkinson's disease, a neurodegenerative disease that affects 15 million people worldwide, is characterized by deposition of α-synuclein into Lewy Bodies in brain neurons. Although this prevalent therapy or cure has yet to be found. Several small compounds have been reported disrupt fibril formation. Among these molecular tweezer known as CLR01 targets lysine and arginine residues. This study aims characterize how interacts with various proteoforms the structure subsequently altered. Native...

10.1021/jasms.3c00281 article EN Journal of the American Society for Mass Spectrometry 2023-11-07

Clostridium thermocellum is a potential microbial platform to convert abundant plant biomass biofuels and other renewable chemicals. It efficiently degrades lignocellulosic using surface displayed cellulosome, megadalton sized multienzyme containing complex. The enzymatic composition architecture of the cellulosome controlled by several transmembrane biomass-sensing RsgI-type anti-σ factors. Recent studies suggest that these factors transduce signals from cell via conserved RsgI...

10.1002/prot.26690 article EN publisher-specific-oa Proteins Structure Function and Bioinformatics 2024-04-10

ABSTRACT Toxin-producing Corynebacterium diphtheriae strains are the etiological agent of severe upper respiratory disease, diphtheria. A global phylogenetic analysis revealed that biotype gravis is particularly lethal as it produces diphtheria toxin and a range other virulence factors, when encounters low levels iron at sites infection. To gain insight into how colonizes its host we have identified iron-dependent changes in exoproteome surfaceome C. strain 1737 using combination whole-cell...

10.1101/2024.05.19.594877 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-05-19

Wall teichoic acid (WTA) polymers are covalently affixed to the Gram-positive bacterial cell wall and have important functions in elongation, morphology, biofilm formation, β-lactam antibiotic resistance. The first committed step WTA biosynthesis is catalyzed by TagA glycosyltransferase (also called TarA), a peripheral membrane protein that produces conserved linkage unit, which joins peptidoglycan. contains GT26 core domain followed C-terminal polypeptide tail for catalysis binding. Here,...

10.1016/j.jbc.2021.101464 article EN cc-by-nc-nd Journal of Biological Chemistry 2021-12-02

To successfully mount infections, nearly all bacterial pathogens must acquire iron, a key metal cofactor that primarily resides within human hemoglobin. Corynebacterium diphtheriae causes the life-threatening respiratory disease diphtheria and captures hemoglobin for iron scavenging using surface-displayed receptor HbpA. Here, we show X-ray crystallography, NMR, in situ binding measurements C. selectively iron-loaded by partially ensconcing heme molecules of its α subunits. Quantitative...

10.1073/pnas.2411833122 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2024-12-31

Abstract Corynebacterium diphtheriae is responsible for the severe upper respiratory tract disease, diphtheria, which can be fatal in healthy individuals without proper treatment. Its interaction with infected host crucial to its virulence, secreting diphtheria toxin and a variety of machinery acquire nutrients further import into cell. Additionally, it shares conserved iron mechanism related pathogenic actinobacteria such as Mycobacterium tuberculosis , contains sortase-mediated anchored...

10.1101/2020.09.06.285155 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-09-07
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