Catherine Fenselau

ORCID: 0000-0003-4979-0229
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Research Areas
  • Mass Spectrometry Techniques and Applications
  • Analytical Chemistry and Chromatography
  • Advanced Proteomics Techniques and Applications
  • Bacterial Identification and Susceptibility Testing
  • Ion-surface interactions and analysis
  • Metabolomics and Mass Spectrometry Studies
  • Analytical chemistry methods development
  • Genomics and Phylogenetic Studies
  • Bacillus and Francisella bacterial research
  • Trace Elements in Health
  • Enzyme Structure and Function
  • Bacteriophages and microbial interactions
  • Glutathione Transferases and Polymorphisms
  • Pharmacogenetics and Drug Metabolism
  • Antibiotic Resistance in Bacteria
  • Microfluidic and Capillary Electrophoresis Applications
  • Immune cells in cancer
  • Glycosylation and Glycoproteins Research
  • Ubiquitin and proteasome pathways
  • Protein Structure and Dynamics
  • Drug Transport and Resistance Mechanisms
  • RNA and protein synthesis mechanisms
  • Neonatal Health and Biochemistry
  • Amino Acid Enzymes and Metabolism
  • Advanced biosensing and bioanalysis techniques

University of Maryland, College Park
2014-2024

Johns Hopkins University Applied Physics Laboratory
2000-2011

Georgetown University
2009-2011

Georgetown University Medical Center
2009-2011

University of Connecticut
2009

University of Maryland, Baltimore
1987-2008

University of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center
2006

U-M Rogel Cancer Center
2005

UConn Health
2005

University of Maryland, Baltimore County
1993-2004

A new method for proteolytic stable isotope labeling is introduced to provide quantitative and concurrent comparisons between individual proteins from two entire proteome pools or their subfractions. Two 18O atoms are incorporated universally into the carboxyl termini of all tryptic peptides during cleavage in first pool. Proteins second pool cleaved analogously with resulting containing 16O (i.e., no labeling). The peptide mixtures pooled fractionation separation, masses ratios each pair...

10.1021/ac001404c article EN Analytical Chemistry 2001-05-02

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIdentification of bacteria using mass spectrometryJohn P. Anhalt and Catherine. FenselauCite this: Anal. Chem. 1975, 47, 2, 219–225Publication Date (Print):February 1, 1975Publication History Published online1 May 2002Published inissue 1 February 1975https://doi.org/10.1021/ac60352a007Request reuse permissionsArticle Views2133Altmetric-Citations369LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum full text article downloads since...

10.1021/ac60352a007 article EN Analytical Chemistry 1975-02-01

This study characterizes various features of the proteins that are detected in MALDI mass spectra when whole bacteria cells analyzed, an effort to understand why some successfully and many others not. Forty peaks observed range 4000−20 000 Da Escherichia coli K-12 11775 tentatively assigned a protein database, these characterized by cell location, copy number, pI, hydropathicity. Those originate cytosol generally share traits high abundance within cell, strong bacisity, medium hydrophilicity.

10.1021/ac0008791 article EN Analytical Chemistry 2001-01-18

A method for rapid identification of microorganisms is presented, which exploits the wealth information contained in prokaryotic genome and protein sequence databases. The based on determining masses a set ions by MALDI TOF mass spectrometry intact or treated cells. Subsequent correlation each ion to protein, along with organismic source performed searching an Internet-accessible database. Convoluting lists all ranking organisms corresponding matched results microorganism. has been...

10.1021/ac990165u article EN Analytical Chemistry 1999-05-27

The MN strain of human immunodeficiency virus type 1 was grown in H9 cells, concentrated by centrifugation, and disrupted, proteins were purified reversed-phase high-pressure liquid chromatography. Complete amino acid sequences determined for the mature Gag proteins, showing natural proteolytic cleavage sites order (p17-p24-p2-p7-p1-p6) precursors. At least two sequence variants p24 eight p17 detected. most abundant represented at 50% +/- 5% 20% their totals, respectively. These data suggest...

10.1128/jvi.66.4.1856-1865.1992 article EN Journal of Virology 1992-04-01

We present a building-block approach toward functionalized CB[7] derivatives by the condensation of methylene-bridged glycoluril hexamer 1 and bis(cyclic ethers) 2 12. The Me2CB[7] CyCB[7] are highly soluble in water (264 mM 181 mM, respectively). As result high intrinsic solubility Me2CB[7], it is able to solubilize insoluble benzimidazole drug albendazole. reaction with derivative 12, which bears primary alkyl chloride group, gives 18 16% isolated yield. Compound reacts NaN3 yield...

10.1021/ja3058502 article EN Journal of the American Chemical Society 2012-07-16

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIsotopic distributions in mass spectra of large moleculesJames. Yergey, David. Heller, Gordon. Hansen, Robert J. Cotter, and Catherine. FenselauCite this: Anal. Chem. 1983, 55, 2, 353–356Publication Date (Print):February 1, 1983Publication History Published online1 May 2002Published inissue 1 February 1983https://pubs.acs.org/doi/10.1021/ac00253a037https://doi.org/10.1021/ac00253a037research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/ac00253a037 article EN Analytical Chemistry 1983-02-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCollision energy dependence of proton-bound dimer dissociation: entropy effects, proton affinities, and intramolecular hydrogen-bonding in protonated peptidesXueheng Cheng, Zhuchun Wu, Catherine FenselauCite this: J. Am. Chem. Soc. 1993, 115, 11, 4844–4848Publication Date (Print):June 1, 1993Publication History Published online1 May 2002Published inissue 1 June...

10.1021/ja00064a052 article EN Journal of the American Chemical Society 1993-06-01

Myeloid-derived suppressor cells (MDSC) are present in most cancer patients where they inhibit natural anti-tumor immunity and an obstacle to anti-cancer immunotherapies. They mediate immune suppression through their production of proteins soluble mediators that prevent the activation tumor-reactive T lymphyocytes, polarize macrophages toward a tumor-promoting phenotype, facilitate angiogenesis. The accumulation suppressive potency MDSC is regulated by inflammation within tumor...

10.1021/pr400879c article EN Journal of Proteome Research 2013-12-02

Myeloid-derived suppressor cells (MDSC) are immature myeloid that accumulate in the circulation and tumor microenvironment of most cancer patients. There, MDSC suppress both adaptive innate immunity, hindering immunotherapies. The inflammatory milieu often present cancers facilitates suppressive activity, causing aggressive progression metastasis. from tumor-bearing mice release exosomes, which carry biologically active proteins mediate some immunosuppressive functions characteristic MDSC....

10.1021/acs.jproteome.7b00646 article EN Journal of Proteome Research 2017-11-15

Proteolytic labeling in H218O has been recently revived as a versatile method for proteomics research. To understand the molecular basis of process, we have dissected process into two separate events: cleavage peptide amide bonds and exchange terminal carboxyl oxygens. It was demonstrated that both oxygens can be catalytically labeled, independent step. Reaction kinetics tryptic 16O-to-18O YGGFMR, YGGFMK, digest apomyoglobin were studied by matrix-assisted laser desorption/ionization Fourier...

10.1021/pr025572s article EN Journal of Proteome Research 2002-12-11

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAssessment of metals in reconstituted metallothioneins by electrospray mass spectrometryXiaolan. Yu, Marek. Wojciechowski, and Catherine. FenselauCite this: Anal. Chem. 1993, 65, 10, 1355–1359Publication Date (Print):May 15, 1993Publication History Published online1 May 2002Published inissue 15 1993https://pubs.acs.org/doi/10.1021/ac00058a010https://doi.org/10.1021/ac00058a010research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/ac00058a010 article EN Analytical Chemistry 1993-05-15

A novel class of lipopeptides was isolated from Bacillus thuringiensis kurstaki HD-1. Four compounds (1−4) were separated by high-performance liquid chromatography and their primary structures determined using a combination chemical reactions mass spectrometry. The four found to have the same amino acid sequence, Thr-Gly-Ala-Ser-His-Gln-Gln, but different fatty acids. acyl chain is linked N-terminal residue via an amide bond. Each lipopeptide has lactone linkage between carboxyl terminal...

10.1021/np000169q article EN Journal of Natural Products 2000-09-15

Recently, proteolytic 18O labeling has been demonstrated as a promising strategy for comparative proteomic studies (Yao, X.; Freas, A.; Ramirez, J.; Demirev, P. Fenselau, C. Anal. Chem. 2001, 73, 2836−42). In this approach, protein mixtures are digested in parallel H216O and H218O the ratios of isotopically distinct peptide products measured by mass spectrometry. initial report from laboratory, trypsin was shown to catalyze incorporation two atoms into carboxyl terminus each new formed...

10.1021/pr0100016 article EN Journal of Proteome Research 2002-01-07

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProfiling of bacteria by fast atom bombardment mass spectrometryD. N. Heller, R. J. Cotter, Catherine. Fenselau, and O. M. UyCite this: Anal. Chem. 1987, 59, 23, 2806–2809Publication Date (Print):December 1, 1987Publication History Published online1 May 2002Published inissue 1 December 1987https://pubs.acs.org/doi/10.1021/ac00150a018https://doi.org/10.1021/ac00150a018research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/ac00150a018 article EN Analytical Chemistry 1987-12-01
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