Alexandria K. D’Souza

ORCID: 0000-0003-2429-3218
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About
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Research Areas
  • Advanced Proteomics Techniques and Applications
  • Glycosylation and Glycoproteins Research
  • Mass Spectrometry Techniques and Applications
  • Peptidase Inhibition and Analysis
  • Single-cell and spatial transcriptomics
  • Galectins and Cancer Biology
  • Trace Elements in Health
  • Advanced Biosensing Techniques and Applications
  • Cell Image Analysis Techniques
  • Genetic Associations and Epidemiology
  • Carbohydrate Chemistry and Synthesis
  • Wound Healing and Treatments
  • Digestive system and related health
  • Reproductive tract infections research
  • Bacillus and Francisella bacterial research
  • RNA modifications and cancer
  • Yersinia bacterium, plague, ectoparasites research
  • Genomics and Phylogenetic Studies
  • Amino Acid Enzymes and Metabolism
  • Pressure Ulcer Prevention and Management
  • Drug Transport and Resistance Mechanisms
  • Antimicrobial Peptides and Activities
  • Viral Infections and Outbreaks Research
  • Metabolomics and Mass Spectrometry Studies
  • Machine Learning in Bioinformatics

Harvard University
2020-2023

Harvard University Press
2022

University of Chicago
2020

Buck Institute for Research on Aging
2013-2019

Posttranslational modifications, such as Nε-lysine acetylation, regulate protein function. acetylation can occur either nonenzymatically or enzymatically. The nonenzymatic mechanism uses acetyl phosphate (AcP) coenzyme A (AcCoA) donor to modify an residue of a protein. enzymatic acetyltransferases (KATs) specifically transfer group from AcCoA residues on proteins. To date, only one KAT (YfiQ, also known Pka and PatZ) has been identified in Escherichia coli Here, we demonstrate the existence...

10.1128/mbio.01905-18 article EN cc-by mBio 2018-10-22

Post-translational modification of lysine residues by NƐ-acylation is an important regulator protein function. Many large-scale acylation studies have assessed relative changes sites after antibody enrichment using mass spectrometry-based proteomics. Although fold-changes are important, this does not reveal site occupancy, or stoichiometry, individual sites, which critical to understand functional consequences. Recently, methods for determining acetylation stoichiometry been proposed based...

10.1007/s13361-016-1476-z article EN Journal of the American Society for Mass Spectrometry 2016-09-02

Single-cell analysis has clearly established itself in biology and biomedical fields as an invaluable tool that allows one to comprehensively understand the relationship between cells, including their types, states, transitions, trajectories, spatial position. Scientific methods such fluorescence labeling, nanoscale super-resolution microscopy, advances single cell RNAseq proteomics technologies, provide more detailed information about biological processes which were not evident with of bulk...

10.1039/d3mo00124e article EN Molecular Omics 2023-08-16

The receptor tyrosine kinase ErbB2 is a breast cancer biomarker whose posttranslational modifications (PTMs) are key indicator of its activation. Quantifying the expression and PTMs biomarkers such as by selected reaction monitoring (SRM) mass spectrometry has several limitations, including minimal coverage extensive assay development time. Therefore, we assessed utility two high resolution, full scan approaches, MS1 Filtering SWATH MS2, for targeted proteomics. Endogenous immunoprecipitated...

10.1155/2013/791985 article EN cc-by International Journal of Proteomics 2013-04-04

O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct of the kinases write phosphate modification. Casein kinase 2 alpha (CK2α), catalytic subunit ubiquitously expressed and constitutively active CK2, modified O-GlcNAc, but effect this phosphoproteome in cells unknown. Here, we apply complementary targeted editors, nanobody-OGT -splitOGA, to selectively erase from a tagged CK2α measure...

10.1021/acschembio.1c00987 article EN ACS Chemical Biology 2022-04-25

Neisseria gonorrhoeae, the causative agent of gonorrhea, has a number factors known to contribute pathogenesis; however, full understanding these processes and their regulation proven be elusive. Post-translational modifications (PTMs) bacterial proteins are now recognized as one mechanism protein regulation. In present study, Western blot analyses, with an anti-acetyl-lysine antibody, indicated that large gonococcal post-translationally modified. Previous work shown Nε-lysine acetylation...

10.1371/journal.pone.0179621 article EN cc-by PLoS ONE 2017-06-27

Francisella tularensis is the causative agent of tularemia and a potential bioterrorism agent. In present study, we isolated, identified, quantified proteins in membranes virulent type A strain, Schu S4, attenuated B LVS (live vaccine strain). Spectral counting mass spectrometric data showed enrichment for membrane both strains. Mice vaccinated with whole encapsulated poly (lactic-co-glycolic acid) (PLGA) nanoparticles containing adjuvant polyinosinic-polycytidylic acid [poly(I·C)]...

10.1128/mbio.01592-17 article EN cc-by mBio 2017-10-11

Single-cell analysis has clearly established itself in biology and biomedical fields as an invaluable tool that allows one to comprehensively understand the relationship between cells, including their types, states, transitions, trajectories, spatial position. Scientific methods such fluorescence labeling, nanoscale super-resolution microscopy, advances single cell RNAseq proteomics technologies, provide more detailed information about biological processes which were not evident with of bulk...

10.26434/chemrxiv-2022-js9wz preprint EN cc-by 2022-06-13

Abstract Post-translational modifications, such as Nε-lysine acetylation, regulate protein function. acetylation can occur either non-enzymatically or enzymatically. The non-enzymatic mechanism uses acetyl phosphate (AcP) coenzyme A (AcCoA) donors to modify an residue of a protein. enzymatic acetyltransferases (KATs) specifically transfer group from AcCoA residues on proteins. To date, only one KAT (YfiQ, also known Pka and PatZ) has been identified in E. coli . Here, we demonstrate the...

10.1101/408930 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2018-09-05

Abstract A missense mutation (A391T) in the manganese transporter SLC39A8 is strongly associated with schizophrenia genomic studies, though molecular connection to brain remains hypothetical. Human carriers of A391T have reduced serum manganese, altered plasma glycosylation, and MRI changes consistent metal transport. Here, using a knock-in mouse model homozygous for A391T, we show that schizophrenia-associated variant protein glycosylation brain. N-linked was most significantly impaired,...

10.1101/2020.12.22.424076 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-12-23

Single-cell analysis has clearly established itself in biology and biomedical fields as an invaluable tool that allows one to comprehensively understand the relationship between cells, including their types, states, transitions, trajectories, spatial position. Scientific methods such fluorescence labeling, nanoscale super-resolution microscopy, advances single cell RNAseq proteomics technologies, provide more detailed information about biological processes which were not evident with of bulk...

10.26434/chemrxiv-2022-js9wz-v2 preprint EN cc-by 2022-06-14

Label-free quantification using data-independent acquisition (DIA) is a robust method for deep and accurate proteome 1,2 . However, when lacking pre-existing spectral library, as often the case with studies of novel post-translational modifications (PTMs), samples are typically analyzed several times: one or more data dependent acquisitions (DDA) used to generate library followed by DIA quantification. This type multi-injection analysis results in significant cost regard sample consumption...

10.1101/141382 preprint EN cc-by-nc bioRxiv (Cold Spring Harbor Laboratory) 2017-05-24
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