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Christopher Silva (Chris)
Produce Safety and Microbiology Research
Research Chemist

Phone: (510) 559-6135
Fax: (510) 559-6429

(Employee information on this page comes from the REE Directory. Please contact your front office staff to update the REE Directory.)

Projects
Rapid Antemortem Tests for the Early Detection of Transmissible Spongiform Encephalopathies and Other Animal Diseases
In-House Appropriated (D)
  Accession Number: 441758

Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
Utilising natural diversity of kinases to rationally engineer interactions with the angiosperm immune receptor ZAR1 Reprint Icon - (Peer Reviewed Journal)
Diplock, N., Baudin, M., Harden, L.A., Silva, C.J., Erickson-Beltran, M.L., Hassan, J.A., Lewis, J.D. 2023. Utilising natural diversity of kinases to rationally engineer interactions with the angiosperm immune receptor ZAR1. Plant, Cell & Environment. 46(7):2238-2254. https://doi.org/10.1111/pce.14603.
A mass spectrometry-based method of quantifying the contribution of the lysine polymorphism at position 171 in sheep PrP Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Cassmann, E.D., Greenlee, J.J., Erickson-Beltran, M.L., Requena, J.R. 2023. A mass spectrometry-based method of quantifying the contribution of the lysine polymorphism at position 171 in sheep PrP. Journal of American Society for Mass Spectrometry. 34(2):245-254. https://doi.org/10.1021/jasms.2c00277.
General method of quantifying the extent of methionine oxidation in the prion protein Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L. 2023. General method of quantifying the extent of methionine oxidation in the prion protein. Journal of American Society for Mass Spectrometry. 34(2):255-263. https://doi.org/10.1021/jasms.2c00280.
Mass spectrometry-based quantitation of methionine oxidation to assess prion structures - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2022. Mass spectrometry-based quantitation of methionine oxidation to assess prion structures. 10th Iberian Congress on Prions, Vila Real Portugal. May 19-20, 2022. Book Abstract. May 20, 2022. Page 41.
Chronic wasting disease (CWD), an evolving prion disease - (Abstract Only)
Silva, C.J. 2022. Chronic wasting disease (CWD), an evolving prion disease. Meeting Abstract. Speaker 10. Page 1. https://events-prod2.stanford.edu/events/942/94241/.
Chronic wasting disease (CWD) in cervids and the consequences of a mutable protein conformation Reprint Icon - (Peer Reviewed Journal)
Silva, C.J. 2022. Chronic wasting disease (CWD) in cervids and the consequences of a mutable protein conformation. ACS Omega. 7(15):12474–12492. https://doi.org/10.1021/acsomega.2c00155.
Detecting differences in prion protein conformation by quantifying methionine oxidation Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L. 2022. Detecting differences in prion protein conformation by quantifying methionine oxidation. ACS Omega. 7(3):2649-2660. https://doi.org/10.1021/acsomega.1c04989.
The challenges of detecting an evolving prion disease, chronic wasting disease (CWD) Reprint Icon - (Abstract Only)
Silva, C.J. 2022. The challenges of detecting an evolving prion disease, chronic wasting disease (CWD)[Abstract]. American Chemical Society National Meeting. https://doi.org/10.1021/scimeetings.2c00139.
Oxidizing methionine to map a prion's surface and reveal conformational differences Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2022. Oxidizing methionine to map a prion's surface and reveal conformational differences [Abstract]. Abstracts of the American Chemical Society. Spring 2022 Meeting. March 23, 2022. Abstract number: 365591. https://doi.org/10.1021/scimeetings.2c00113.
Use of methionine oxidation to study prion structure - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2021. Use of methionine oxidation to study prion structure[abstract]. Citation (ID) number 308479, November 5, 2021, Proceedings of the 69th ASMS Conference on Mass Spectrometry and Allied Topics, Philadelphia, PA and online, October 31-November 4, 2021. Available: https://www.asms.org/docs/default-source/default-document-library/tues-nov-16-12pm---para. llel-2_guide.pdf?.
Cellular prion protein mediates a-synuclein uptake, localization, and toxicity in vitro and in vivo Reprint Icon - (Peer Reviewed Journal)
Thom, T., Schmitz, M., Fischer, A., Correia, A., Correia, S., Llorens, F., Pique, A., Mobius, W., Domingues, R., Zafar, S., Stoops, E., Silva, C.J., Fischer, A., Outeiro, T.F., Zerr, I. 2021. Cellular prion protein mediates a-synuclein uptake, localization, and toxicity in vitro and in vivo. Movement Disorders. 37(1):39-51. https://doi.org/10.1002/mds.28774.
Using mass spectrometry to detect the presence of and dissect the structure of prions - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson-Beltran, M.L., Requena, J.R. 2021. Using mass spectrometry to detect the presence of and dissect the structure of prions. Meeting Abstract. Abstract ID: 355344. https://acs.digitellinc.com/acs/live/8/page/18/1?eventSearchInput=3555344+&eventSearchTrack%5B%5D=23.
Time of detection of prions in the brain by nanoscale liquid chromatography coupled to tandem mass spectrometry is comparable to animal bioassay Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson-Beltran, M.L., Requena, J.R. 2021. Time of detection of prions in the brain by nanoscale liquid chromatography coupled to tandem mass spectrometry is comparable to animal bioassay. Journal of Agricultural and Food Chemistry. 69(7):2279-2286. https://doi.org/10.1021/acs.jafc.0c06241.
Quantifying the role of lysine in prion replication by Nano-LC mass spectrometry and bioassay Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.C. 2020. Quantifying the role of lysine in prion replication by Nano-LC mass spectrometry and bioassay. Frontiers in Bioengineering and Biotechnology. 8. Article 562953. https://doi.org/10.3389/fbioe.2020.562953.
Using targeted mass spectrometry, covalent modification, Western blot, and bioassay to quantitate the relative role of specific lysines in prion replication - (Abstract Only)
C.J. Silva, M.L. Erickson-Beltran, I.C. Dynin. 2020. ANYL 10: Using targeted mass spectrometry, covalent modification, Western blot, and bioassay to quantitate the relative role of specific lysines in prion replication. American Chemical Society Abstracts. ACS Fall 2020 Virtual Meeting & Exposition: 10-ANYL.
Using mass spectrometry to quantify prion polymorphisms and phenotypes in heterozygous sheep and deer - (Abstract Only)
C.J. Silva, M.L. Erickson-Beltran, C. Duque-Velásquez, J.M. Aiken, D. Mckenzie, I. Martín-Burriel, J. Badiola, J.R. Requena, B. Marín, R. Bolea. 2020. AGFD 138: Using mass spectrometry to quantify prion polymorphisms and phenotypes in heterozygous sheep and deer. Abstracts of Papers of the American Chemical Society. ACS Fall 2020 Virtual Meeting & Exposition: 138-AGFD.
A general mass spectrometry-based method of quantitating prion polymorphisms from heterozygous chronic wasting disease-infected cervids Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Duque Velásquez, C., Aiken, J.M., McKenzie, D. 2019. A general mass spectrometry-based method of quantitating prion polymorphisms from heterozygous chronic wasting disease-infected cervids. Analytical Chemistry. 92(1):1276-1284. https://doi.org/10.1021/acs.analchem.9b04449.
Quantitating prion polymorphisms from heterozygous CWD-infected white-tailed deer - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Duque Velásquez, C., Aiken, J.M., Mckenzie, D. 2019.Quantitating prion polymorphisms from heterozygous CWD-infected white-tailed deer [abstract]. 8th Iberian Congress on Prions. 8:33-33. ISBN: 978-972-579-050-2. October, 2019.
Draft genome sequences of Shiga toxin-producing Escherichia coli O157:H7 strains recovered from a major production region for leafy greens in California Reprint Icon - (Peer Reviewed Journal)
Quiñones, B., Yambao, J.C., Silva, C.J., Lee, B.G. 2019. Draft genome sequences of Shiga toxin-producing Escherichia coli O157:H7 strains recovered from a major production region for leafy greens in California. Microbiology Resource Announcements. 8(27):e00644-19. https://doi.org/10.1128/MRA.00644-19.
A general mass spectrometry-based method of quantitating the oxidation of the methionine side chains in classical and atypical scrapie PrPSc - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Martin-Burriel, I., Badiola, J.J., Requena, J.R., Bolea, R. 2019. 238: A general mass spectrometry-based method of quantitating the oxidation of the methionine side chains in classical and atypical scrapie PrPSc [abstract]. Prion. 13(Supplement):131-132.
A general mass spectrometry-based method of quantitating the relative amounts of PrP polymorphisms in CWD PrPSc - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Duque Velasquez, C., Aiken, J.M., Mckenzie, D. 2019. 237: A general mass spectrometry-based method of quantitating the relative amounts of PrP polymorphisms in CWD PrPSc [abstract]. Prion. 13(supplement):131-131.
Quantitating Shiga toxin production in environmental STEC isolated from a major produce production region in California - (Abstract Only)
Silva, C.J., Lee, B.G., Yambao, J.C., Erickson-Beltran, M.L., Quinones, B. 2019. Quantitating Shiga toxin production in environmental STEC isolated from a major produce production region in California [abstract]. ASM Microbe 2019, June 20-24, 2019, San Francisco, CA. Poster AES-1194.
Distinguishing among protein conformations (prion strains) by detecting covalent differences using quantitative mass spectrometry - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2019. Distinguishing among protein conformations (prion strains) by detecting covalent differences using quantitative mass spectrometry [abstract]. ASM Microbe 2019, June 20-24, 2019, San Francisco, CA. Poster MBP-19.
Quantitating and verifying Shiga toxin expression from Californian environmental STEC by mass spectrometry - (Abstract Only)
Silva, C.J., Lee, B.G., Yambao, J.C., Erickson-Beltran, M.L., Quinones, B. 2019. Quantitating and verifying Shiga toxin expression from Californian environmental STEC by mass spectrometry. Meeting Abstract. Poster. ARS-FSIS 2019 meeting.
Quantitating Shiga toxins produced by environmental E. coli - (Other)
Silva, C.J., Lee, B.G., Yambao, J.C., Erickson-Beltran, M.L., Quinones B. 2019. Quantitating Shiga toxins produced by environmental E. coli. Cover, Journal of Agricultural and Food Chemistry. 67(5). February 6, 2019.
Using nanospray liquid chromatography and mass spectrometry to quantitate Shiga toxin production in environmental Escherichia coli recovered from a major produce production region in California Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Lee, B.G., Yambao, J.C., Erickson-Beltran, M.L., Quiñones, B. 2019. Using nanospray liquid chromatography and mass spectrometry to quantitate Shiga toxin production in environmental Escherichia coli recovered from a major produce production region in California. Journal of Agricultural and Food Chemistry. 67(5):1554-1562. https://doi.org/10.1021/acs.jafc.8b05324.
Exploring the conformational differences between PrPSc from classical and atypical scrapie using mass spectrometry Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Martin-Burriel, I., Badiola, J., Requena, J.R., Bolea, R. 2018. Exploring the conformational differences between PrPSc from classical and atypical scrapie using mass spectrometry. Meeting Abstract. 38(1):65-80. https://doi.org/10.1051/vetres:2006046.
Chronic Wasting Disease: The American experience - (Abstract Only)
Silva, C.J. 2018. Chronic Wasting Disease: The American experience. Meeting Abstract. [abstract]. University of Santiago de Compostela, Spain.
Food forensics: using mass spectrometry to detect foodborne protein contaminants as exemplified by Shiga toxin variants and prion strains Reprint Icon - (Peer Reviewed Journal)
Silva, C.J. 2018. Food forensics: using mass spectrometry to detect foodborne protein contaminants as exemplified by Shiga toxin variants and prion strains. Journal of Agricultural and Food Chemistry. 66(32):8435-8450. https://doi.org/10.1021/acs.jafc.8b01517.
Using mass spectrometry to determine the relative susceptibility of PrP polymorphisms to atypical scrapie - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Martín-Burriel, I., Badiola, J., Requena, J.R., Bolea, R. 2018. Using mass spectrometry to determine the relative susceptibility of PrP polymorphisms to atypical scrapie. Meeting Abstract. Poster 110. Prion2018, Santiago de Compostela, Spain.
Does methionine oxidation influence the progression of classical or atypical scrapie - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Martín-Burriel, I., Badiola, J., Requena, J.R., Bolea, R. 2018. Does methionine oxidation influence the progression of classical or atypical scrapie. 66thASMS Conference on Mass Spectrometry and Allied Topics. Poster No. ThP 586. June 7, 2018. San Diego California.
Chronic wasting disease: Bambi vs. the prion - (Abstract Only)
Silva, C.J. 2018. Chronic wasting disease: Bambi vs. the prion. Northern California Branch American Society for Microbiology Spring Meeting, March 2-3, 2018. Session 2. Presentation 2.
An improved method for the sensitive detection of Shiga toxin 2 in human serum Reprint Icon - (Peer Reviewed Journal)
He, X., Ardissino, G., Patfield, S.A., Cheng, L.W., Silva, C.J., Brigotti, M. 2018. An improved method for the sensitive detection of Shiga toxin 2 in human serum. Toxins. 10(2):59. https://doi.org/10.3390/toxins10020059.
Determining the relative susceptibility of four prion protein genotypes to atypical scrapie Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Martín-Burriel, I., Badiola, J., Requena, J.R., Bolea, R. 2017. Determining the relative susceptibility of four prion protein genotypes to atypical scrapie. Analytical Chemistry. 90(2):1255-1262. https://doi.org/10.1021/acs.analchem.7b03985.
Recombinant PrPSc shares structural features with brain-derived PrPSc suggesting that they have a similar architecture: Insights from limited proteolysis Reprint Icon - (Peer Reviewed Journal)
Sevillano, A.M., Fernández-Borges, N., Younas, N., Wang, F., Elezgarai, S.R., Bravo, S., Vázquez-Fernández, E., Rosa, I., Eraña, H., Gil, D., Veiga, S., Vidal, E., Erickson-Beltran, M.L., Guitián, E., Silva, C.J., Nonno, R., Ma, J., Castilla, J., Requena, J.R. 2018. Recombinant PrPSc shares structural features with brain-derived PrPSc suggesting that they have a similar architecture: Insights from limited proteolysis. PLoS Pathogens. 14(1):e1006797. https://doi.org/10.1371/journal.ppat.1006797.
Detecting and distinguishing among covalent and non-covalent differences in proteins: Shiga toxins and prions - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2017. Detecting and distinguishing among covalent and non-covalent differences in proteins: Shiga toxins and prions. Meeting Abstract. 254: 224-AGFD.
The architecture of PrPSc: Threading secondary structure elements into the 4-rung ß-solenoid scaffold - (Abstract Only)
Sevillano, A.M., Chakraborty, S., Vazquez-Fernandez, E., Silva, C.J., Requena, J.R. 2017. The architecture of PrPSc: Threading secondary structure elements into the 4-rung ß-solenoid scaffold. Meeting Abstract. Prion 2017: Poster 221..
Overcoming the challenges of safely quantifying and distinguishing among Shiga toxins in complex media and human serum - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Patfield, S.A., He, X., Wu, V.C. 2017. Overcoming the challenges of safely quantifying and distinguishing among Shiga toxins in complex media and human serum. Meeting Abstract. Poster. ARS-FSIS 2017 meeting.
Using mass spectrometry and small molecule reagents to detect distinctive structural features of different prion conformations (strains) - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.A. 2017. Using mass spectrometry and small molecule reagents to detect distinctive structural features of different prion conformations (strains). Abstracts of the Papers of the American Chemical Society. 253:438-ANYL.
Quantifying the relative amounts of PrP polymorphisms present in prions isolated from heterozygous prion-infected animals - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Hui, C., Badiola, J., Requena, J.R., Bolea, R. 2017. Quantifying the relative amounts of PrP polymorphisms present in prions isolated from heterozygous prion-infected animals. Abstracts of the Papers of the American Chemical Society. 253:208-BIOL.
Detecting and distinguishing among type 1 and type 2 Shiga toxins in human serum - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Patfield, S.A., He, X. 2017. Detecting and distinguishing among type 1 and type 2 Shiga toxins in human serum. Abstracts of the Papers of the American Chemical Society. 253:234-AGFD.
Quantitating PrP polymorphisms present in prions from heterozygous scrapie-infected sheep - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Hui, C., Badiola, J.J., Nicholson, E.M., Requena, J.R., Bolea, R. 2016. Quantitating PrP polymorphisms present in prions from heterozygous scrapie-infected sheep. Analytical Chemistry. 89(1):854-861. doi:10.1021/acs.analchem.6b03822.
Shiga toxins: a review of structure, mechanism, and detection - (Book / Chapter)
Silva, C.J., Brandon, D.L., Skinner, C.B., He, X. 2017. Shiga Toxins: a Review of Structure, Mechanism, and Detection. Cham, Switzerland: Springer International Publishing. 118 p.
Detecting and discriminating among Shiga toxins - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Patfield, S.A., He, X., Wu, V.C. 2016. Detecting and discriminating among Shiga toxins. doi: 10.1021/acs.jafc.6b00379.
Using small molecule reagents to help distinguish among prion structural models - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.A. 2016. Using small molecule reagents to help distinguish among prion structural models. Prion 10(Supplement 1). p. S37-S38.
Identification of new molecular alterations in Fatal Familial Insomnia. - (Abstract Only)
Ferrer, I., Llorens, F., Frau-Mendez, M.A., Frnandez-Vega, I., Thune, K., Del Rio, J.A., Schmitz, M., Ansoleaga, B., Gotzmann, N., Cramm, M., Silva, C.J., Zerr, I., Zarranz, J. 2016. Identification of new molecular alterations in Fatal Familial Insomnia. Prion 10 (Supplement 1): S83.
Identification of new molecular alterations in Fatal Familial Insomnia - (Peer Reviewed Journal)
Llorens, F., Thune, K., Schmitz, M., Cramm, M., Tahir, W., Gotzmann, N., Zerr, I., Silva, C.J., Frau-Mendez, M.A., Ansoleaga, B., Berjawi, S., Carmona, M., Ferrar, I., Fernandez, I., Zarranz, J. 2016. Identification of new molecular alterations in Fatal Familial Insomnia. Human Molecular Genetics. Vol: 25; Page: 2417-2436.
Safe, rapid, and sensitive method of quantitating and distinguishing among Shiga toxins in complex media and human serum - (Abstract Only)
Wu, V.C., Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Patfield, S.A., He, X. 2016. Safe, rapid, and sensitive method of quantitating and distinguishing among Shiga toxins in complex media and human serum. ARS Food Safety and Inspection Service Research Workshop. ARS-FSIS.
Covalent surface modification of prions: a mass spectrometry-based means of detecting distinctive structural features of prion strains Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.C. 2016. Covalent surface modification of prions: a mass spectrometry-based means of detecting distinctive structural features of prion strains. Biochemistry. 55:894-902.
Mass spectrometry-based method of detecting and distinguishing type 1 and type 2 Shiga-like toxins in human serum Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Patfield, S.A., He, X. 2015. Mass spectrometry-based method of detecting and distinguishing type 1 and type 2 Shiga-like toxins in human serum. Toxins. 7:5236-5253.
The chemistry of prions: small molecules, protein conformers and mass spectrometry Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2015. The chemistry of prions: small molecules, protein conformers and mass spectrometry. Meeting Abstract. Prion (Supplement 1) 9: S70.
Using proteinase K to study the structure of prions. Reprint Icon - (Abstract Only)
Silva, C.J., Vazquez-Fernandez, E., Requena, J.R. 2015. Using proteinase K to study the structure of prions.. Meeting Abstract. Prion (Supplement 1) 9: S69-S70.
The view from above: The potential of aerial surveillance in identifying CWD infected herds. Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L. 2015. The view from above: The potential of aerial surveillance in identifying CWD infected herds.. Meeting Abstract. Prion (Supplement 1) 9: S73..
PrP0\0 mice show behavioral abnormalities that suggest PrPC has a role in maintaining the cytoskeleton. Reprint Icon - (Abstract Only)
Schmitz, M., Silva, C.J. 2015. PrP0\0 mice show behavioral abnormalities that suggest PrPC has a role in maintaining the cytoskeleton.. Meeting Abstract. Prion (Supplement 1) 9: S73-S74..
Proteinase K and the structure of PrPse: the good, the bad, and the ugly Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Vázquez-Fernández, E., Onikso, B., Requena, J.R. 2015. Proteinase K and the structure of PrPse: the good, the bad, and the ugly. Virus Research. doi: 10.1016/j.virusres.2015.03.008.
Detecting prions and discriminating among prion strains by discerning the differences in absence. - (Abstract Only)
Silva, C.J. 2015. Detecting prions and discriminating among prion strains by discerning the differences in absence.. Meeting Abstract. Volume 2015. Page: Lecture #23.
Behavioral abnormalities in prion protein knockout mice and the potential relevance of PrPc for the cytoskeleton Reprint Icon - (Peer Reviewed Journal)
Schmitz, M., Zafar, S., Silva, C.J., Zerr, I. 2014. Behavioral abnormalities in prion protein knockout mice and the potential relevance of PrPc for the cytoskeleton. Prion. 8(6) 381-386.
Safe and effective means of detecting and quantitating Shiga-like toxins in attomole amounts Reprint Icon - (Peer Reviewed Journal)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Dynin, I., Hui, C., Patfield, S.A., Carter, J.M., He, X. 2014. Safe and effective means of detecting and quantitating Shiga-like toxins in attomole amounts. Analytical Chemistry. 86(10):4698-4706.
Overview of the Western Regional Research Center, Albany, California. - (Other)
Silva, C.J. 2014. Overview of the Western Regional Research Center, Albany, California. Meeting Proceedings. #10.
Oxidized methionine is not a prion-specific covalent modification Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I., Hui, C., Carter, J.M. 2014. Oxidized methionine is not a prion-specific covalent modification. Meeting Abstract. Abstracts of the Papers of the American Chemical Society. 248: 230-BIOL.
Small molecules and antibodies: a means of distinguishing between PrPC and PrPSc Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.A. 2014. Small molecules and antibodies: a means of distinguishing between PrPC and PrPSc [abstract]. Meeting Abstract. Current Topics in Biological Chemistry. Paper No. 12.
The physiological role of the normal cellular prion protein (PrPC). Reprint Icon - (Abstract Only)
Schmitz, M., Greis, C., Ottis, P., Silva, C.J., Schulz-Schaeffer, W.J., Wrede, A., Koppe, K., Requean, J.R. 2014. The physiological role of the normal cellular prion protein (PrPC) [abstract]. Meeting Abstract. Current Topics in Biological Chemistry. Paper No. 113.
Using mass spectrometry to detect and discriminate among Shiga-like toxins in the attomole range. Reprint Icon - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Skinner, C.B., Dynin, I.A., Hui, C., Patfield, S.A., He, X. 2014. Using mass spectrometry to detect and discriminate among Shiga-like toxins in the attomole range [abstract]. Meeting Abstract. Innovations in Mass Spectrometry. Paper No. 355.
Loss of prion protein leads to age-dependent behavioral abnormalities and changes in cytoskeletal protein expression - (Peer Reviewed Journal)
Schmitz, M., Greis, C., Ottis, P., Silva, C.J., Schulz-Schaeffer, W., Wrede, A., Koppe, K., Onisko, B., Requena, J.R., Govindarajan, N., Korth, C., Fisher, A., Zerr, I. 2014. Loss of prion protein leads to age-dependent behavioral abnormalities and changes in cytoskeletal protein expression. Molecular Neurobiology. DOI: 10.1007/s12035-014-8655-3; 50(3):923-936.
Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure Reprint Icon - (Peer Reviewed Journal)
Silva, C.J. 2014. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. 8(1):42-50. DOI: http://dx.doi.org/10.4161/pri.27891.
Distinguishing between PrPC and PrPSc using small molecule reagents - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I., Carter, J.M. 2013. Distinguishing between PrPC and PrPSc using small molecule reagents. Meeting Abstract. Prion 2013 Banff, Alberta, Canada May 26-29, 2013. jdc..
Methods to differentiate protein conformers - (Patent Application)
Onisko, B.C., Silva, C.J., Requena, J.R., Carter, J.M. 2013. Methods to differentiate protein conformers. Patent Application. US Patent 8,445,642.
Oxidation of methionine in PrP is dependent upon the oxidant and the amino acid two positions removed(Abstract) Reprint Icon - (Proceedings)
Silva, C.J., Dynin, I.A., Erickson-Beltran, M.L., Hui, C., Carter, J.M. 2013. Oxidation of methionine in PrP is dependent upon the oxidant and the amino acid two positions removed(Abstract). Meeting Abstract. Prion 7:81. Available: https://landesbioscience.com/journals/prion/05-Prion7-2ARB-Posters%20PS.pdf.
A comparison of the structure of the PK-sensitive and PK-resistant forms of PrPSc(Abstract) - (Abstract Only)
Silva, C.J., Sajnani, G., Ramos, A., Pastrana, M.A., Onisko, B.C., Erickson-Beltran, M.L., Antaki, E.M., Dynin, I.A., Vazquez-Fernandez, E., Sigurdson, C.J., Carter, J.M., Requena, J.R. 2013. A comparison of the structure of the PK-sensitive and PK-resistant forms of PrPSc(Abstract). Meeting Abstract. PS 26.
Distinguishing between PrPC and PrPSc using small molecule reagents(Abstract) - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.A., Carter, J.M. 2013. Distinguishing between PrPC and PrPSc using small molecule reagents(Abstract). Meeting Abstract. PS 25.
Oxidation of methionine 216 in sheep and elk prion protein is highly dependent upon the amino acid at position 218 but is not important for prion propagation - (Peer Reviewed Journal)
Silva, C.J., Dynin, I.A., Erickson-Beltran, M.L., Requena, J.R., Balachandran, A., Onisko, B.C., Hui, C., Carter, J.M. 2013. Using mass spectrometry to detect prions and oxidized prions in scrapie-infected sheep and CWD-infected elk. Biochemistry. 52:2139-2147. doi:10.1021/bi3016795.
Structural organization of mammalian prions as probed by limited proteolysis - (Peer Reviewed Journal)
Vasquez-Fernandez, E., Alonso, J., Pastrana, M.A., Ramos, A., Stitz, L., Vidal, E., Dynin, I.A., Petsch, B., Silva, C.J., Requena, J.R. 2012. Structural organization of mammalian prions as probed by limited proteolysis. PLoS One. 7(11):e50111. doi:10.1371/journal.pone.0050111.
Oxidation of methionine in PrP is dependent upon the oxidant and the amino acid two positions removed - (Abstract Only)
Detecting and discriminating among pathogenic protein conformers(prions), using mass spectrometry-based and antibody-based approaches(Abstract) - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson-Beltran, M.L., Hui, C., Carter, J.M. 2012. Detecting and discriminating among pathogenic protein conformers(prions), using mass spectrometry-based and antibody-based approaches(Abstract). Meeting Abstract. Poster 216.
Using synthetic small molecule reagents and antibodies to distinguish among PrP conformers: new uses for old antibodies - (Abstract Only)
Silva, C.J., Erickson-Beltran, M.L., Dynin, I.A., Carter, J.M. 2012. Using synthetic small molecule reagents and antibodies to distinguish among PrP conformers: new uses for old antibodies. Meeting Abstract. Prion 6(supplement),90.
Probing the structure of GPI-less PrPSc by limited proteolysis(Abstract) - (Abstract Only)
Vazquez-Fernandez, E., Pastrana, M., Ramos, A., Alonso, J., Stitz, L., Vindal, E., Dynin, I.A., Silva, C.J. 2012. Probing the structure of GPI-less PrPSc by limited proteolysis(Abstract). Meeting Abstract. Prion 6(supplement),26-27.
Molecular approaches to detecting and discriminating among prions, a class of pathogenic molecules(Abstract) - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson-Beltran, M.L., Hui, C., Carter, J.M. 2012. Molecular approaches to detecting and discriminating among prions, a class of pathogenic molecules(Abstract). Meeting Abstract. Poster, 615.
Human and rat brain lipofuscin proteome - (Peer Reviewed Journal)
Otts, P., Koppe, K., Onisko, B.C., Dynin, I.A., Arzberger, T., Kretzschmar, H., Requena, J.R., Silva, C.J., Huston, J.P., Korth, C. 2012. Human and rat brain lipofuscin proteome. Proteomics. 12(15-16):2445-2454. doi:10.1002/pmic.201100668.
PK-sensitive PrPSc is infectious and shares basic structural features with PK-resistant PrPSc - (Peer Reviewed Journal)
Sajnani, G., Silva, C.J., Ramos, A., Pastrana, M.A., Onisko, B.C., Erickson-Beltran, M.L., Antaki, E.M., Sigurdson, C.J., Carter, J.M., Requena, J.R. 2012. PK-sensitive PrPSc is infectious and shares basic structural features with PK-resistant PrPSc. PLoS Pathogens. 8(3):e1002547. doi:10.1371/journal.ppat.1002547.
Using small molecule reagents to selectively modify epitopes based on their conformation - (Peer Reviewed Journal)
Silva, C.J. 2012. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. 6:(2)165-175.
Using Mass Spectrometry to Diagnose Prion diseases: Can we do that? - (Abstract Only)
Diagnosing Prion Diseases: Mass Spectrometry-Based Approaches - (Abstract Only)
Silva, C.J., Erickson, M.L., Dynin, I.A., Onisko, B.C., Carter, J.M. 2011. Diagnosing Prion Diseases: Mass Spectrometry-Based Approaches. Meeting Abstract. Prion, Volume 5 (Supplement), April/May/June 2011. page 85.
Probing structural differences between PrPC and PrPSc by surface nitration and acetylation: evidence of conformational change in the C-terminus - (Peer Reviewed Journal)
Gong, B., Ramos, A., Vazquez-Fernandez, E., Silva, C.J., Alonso, J., Requena, J.R. 2011. Probing structural differences between PrPC and PrPSc by surface nitration and acetylation: evidence of conformational change in the C-terminus. Biochemistry. 50:4963-4972.
Utility of mass spectrometry in the diagnosis of prion diseases - (Peer Reviewed Journal)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson-Beltran, M.L., Requena, J.J., Carter, J.M. 2011. Utility of mass spectrometry in the diagnosis of prion diseases. Analytical Chemistry. 83(5):1609-1615. doi:10.1021/ac102527w.
Mass spectrometry and prions: The need to simplify and remove oil from the system - (Review Article)
Silva, C.J. 2010. Mass spectrometry and prions: The need to simplify and remove oil from the system. International News on Fats, Oils and Related Materials.21(8):517-520.
Detecting and quantifying prions: Mass spectrometry-based approaches - (Abstract Only)
Assessing the Role of Oxidized Methionine at Position 213 in the Formation of Prions in Hamsters - (Peer Reviewed Journal)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson, M.L., Vensel, W.H., Requena, J., Antaki, E.M., Carter, J.M. 2010. Assessing the Role of Oxidized Methionine at Position 213 in the Formation of Prions in Hamsters. Journal of Biochemistry. (49):1854-1861.
Mass Spectrometry of Prions: Approaches to Conformational Distinction - (Abstract Only)
Silva, C.J., Onisko, B., Dynin, I.A., Erickson, M.L., Carter, J.M. 2009. Mass Spectrometry of Prions: Approaches to Conformational Distinction. [Abstract]. AOAC 123rd Annual Meeting & Exposition. S-902. p68-69
Disinfectants and Prions - (Abstract Only)
Silva, C.J. 2009. Disinfectants and Prions. [Abstract]. AOAC Annual Meeting & Exposition S-401. p63
Induction of Purple Sulfur Bacterial Growth in Dairy Wastewater Lagoons by Circulation - (Peer Reviewed Journal)
Mcgarvey, J.A., Miller, W.G., Lathrop, J.R., Silva, C.J., Bullard, G. 2009. Induction of Purple Sulfur Bacterial Growth in Dairy Wastewater Lagoons by Circulation. Letters in Applied Microbiology. 49:427-433.
Prion Infectivity Assays. - (Government Publication)
Mass Spectrometric Approaches to Detecting and Quantifying Prions - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson, M.L. 2009. Mass Spectrometric Approaches to Detecting and Quantifying Prions. [Abstract]. PrP Canada p28.
Quantifying prions in experimentally infected animals - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson, M.L., Carter, J.M. 2009. Quantifying prions in experimentally infected animals. [Abstract]. PrP Canada Navigating the Risks. Path 58. p81.
Prion diseases: A little prevention can prevent a catastrophe - (Abstract Only)
Silva, C.J. 2009. Prion diseases: A little prevention can prevent a catastrophe. [Abstract]. AOAC AM-1 p1.
Prions: The Chemistry of Infectious Proteins - (Abstract Only)
Silva, C.J. 2008. Prions: The Chemistry of Infectious Proteins [Abstract]. American Oil Chemists' Society. S-401. p.63.
Mass spectrometric approaches to detecting prions and protein conformers - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson, M.L. 2009. Mass spectrometric approaches to detecting prions and protein conformers. [Abstract] AOAC S-401. p63
Prion Diseases - (Book / Chapter)
Silva, C.J. 2009.Prion Diseases:Sequelae and Long Term Consequences of Infectious Diseases. District of Columbia:ASM Press. 442p.
Mass Spectrometric Approaches to Detecting and Quantifying Prions - (Abstract Only)
Silva, C.J., Onisko, B.C., Dynin, I.A., Erickson, M.L., Carter, J.M. 2008. Mass Spectrometric Approaches to Detecting and Quantifying Prions. [Abstract]. Third International CWD Symposium. Advancing the Science and Developing the Tools. Vol 3. p23.
Bovine Spongiform Encephalopathy - (Review Article)
Harman, J.L., Silva, C.J. 2009. Bovine Spongiform Encephalopathy. Journal of the American Veterinary Medical Association. (2009)234(1):59-72
Sensitive, Preclinical Detection of Prions in Brain by nanospray liquid chromatography/tandem mass spectrometry - (Peer Reviewed Journal)
Onisko, B.C., Silva, C.J., Dynin, I.A., Erickson, M.L., Vensel, W.H., Hnasko, R.M., Requena, J.R., Carter, J.M. 2007. Sensitive, Preclinical Detection of Prions in Brain by nanospray liquid chromatography/tandem mass spectrometry. Rapid Communications in Mass Spectrometry. 21(24):4023-4026.
Pathobiology and diagnosis of animal transmissible spongiform encephalopathies: current knowledge, research gaps, and opportunities - (Government Publication)
Kehrli, Jr., M.E., O'Rourke, K.I., Hamir, A.N., Richt, J.A., Nicholson, E.M., Silva, C.J., Edelman, D., Gay, C.G. 2007. Pathobiology and diagnosis of animal transmissible spongiform encephalopathies: current knowledge, research gaps, and opportunities [government white paper]. Beltsville, MD: Interagency Working Group on Prion Science, Subcommittee on Pathobiology and Diagnostics. USDA, Agriculture Research Service. 33 p.
Mass Spectrometric Detection of Attomole Amounts of the Prion Protein by nanoLC-MS-MS - (Peer Reviewed Journal)
Onisko, B.C., Dynin, I.A., Requena, J.R., Silva, C.J., Erickson, M.L., Carter, J.M. 2007. Mass Spectrometric Detection of Attomole Amounts of the Prion Protein by nanoLC-MS-MS. Journal of American Society for Mass Spectrometry. Volume(18); 1070-1079
State of BSE in the United States - (Trade Journal)
Silva, C.J. 2007. State of BSE in the United States. The National Provisioner. April 2007: Page 15. http://www.provisioneronline.com/content.php?s=NP/2007/04&p=15
MASS SPECTROMETRIC DETECTION OF ATTOMOLE AMOUNTS OF THE PRION PROTEIN, PRP 27-30, BY NANOLC-MS-MS - (Abstract Only)
Onisko, B.C., Requena, J., Silva, C.J., Dynin, I.A., Carter, J.M. 2006. Mass spectrometric detection of attomole amounts of the prion protein, prp 27-30, by nanolc-ms-ms. [Abstract]. 232nd ACS National Meeting and Exposition. Poster AGFD 200
PRIONS: PATHOLOGICAL PROTEINS AT THE INTERFACE OF OIL AND WATER - (Abstract Only)
Silva, C.J. 2006. Prions: pathological proteins at the interface of oil and water [Abstract]. 97th AOCS Annual Meeting & Expo, April 30-May3, 2006, St. Louis, MO. Abstract # FM3-1; page 43. Available: http://www.aocs.org/archives/am2006/session.asp?session=FM+3%3A+Animal%2DHuman+Linked+Health+and+Nutrition+Issues
PRIONS: PATHOLOGICAL PROTEINS AT THE INTERFACE OF OIL AND WATER. - (Review Article)
Silva, C.J. 2006. Prions: pathological proteins at the interface of oil and water. Inform. 17(2), pp. 76-77+79.
HETEROLOGOUS PRODUCTION OF DAPTOMYCIN IN STREPTOMYCES LIVIDANS - (Peer Reviewed Journal)
Penn, J., Li, X., Whiting, A., Latif, M., Silva, C.J., Brian, P., Davies, J., Miao, V., Wrigley, S.K., Baltz, R.H. 2005. Heterologous production of daptomycin in streptomyces lividans [Epub ahead of print]. Journal of Industrial Microbiology and Biotechnology. Nov 1:1-8.
BACTERIAL POPULATION STRUCTURE OF DAIRY WASTEWATERS - (Abstract Only)
Mcgarvey, J.A., Miller, W.G., Sanchez, S., Silva, C.J. 2005. Bacterial population structure of dairy wastewaters [abstract]. International Union of Microbiological Societies, July 23-28, 2005, San Francisco, CA. Poster No. B1102.
BACTERIAL AND CHEMICAL COMPOSITION OF DAIRY WASTEWATER - (Abstract Only)
Mcgarvey, J.A., Miller, W.G., Sanchez, S., Silva, C.J. 2005. Bacterial and chemical composition of dairy wastewater [abstract]. American Society for Microbiology General Meeting, 6/5-6/9/05, Atlanta, GA. P. 008.
COMPARISON OF BACTERIAL POPULATIONS AND CHEMICAL COMPOSITION OF DAIRY WASTEWATER HELD IN CIRCULATED AND STAGNANT LAGOONS - (Peer Reviewed Journal)
Mcgarvey, J.A., Miller, W.G., Sanchez, S., Silva, C.J., Whitehand, L.C. 2005 Comparison of bacterial populations and chemical composition of dairy wastewater held in circulated and stagnant lagoons [abstract]. Journal of Applied Microbiology. 99(10):867-877.
DAPTOMYCIN BIOSYNTHESIS IN STREPTOMYCES ROSEOSPORUS: CLONING AND ANALYSIS OF THE GENE CLUSTER AND REVISION OF PEPTIDE STEREOCHEMISTRY - (Peer Reviewed Journal)
Miao, V., Coeffet-LeGal, M-F, Brian, P., Brost, R., Penn, J., Whiting, A., Martin, S. Ford, R., Parr, I., Bouchard, M., Silva, C.J., Wrigley, S.K., Baltz, R.H. 2005. Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry. Microbiology. 151(5):1507-1523.
SCRAPIE: THE VERY MODEL OF AN INFECTIOUS(PROTEIN)ISOFORM - (Abstract Only)
Silva, C.J. 2005. Scrapie: The Very Model of an Infectious (Protein) Isoform [abstract]. 96th AOCS Annual Meeting & Expo. Salt Lake City, UT, May 2, 2005.
PRIONS: THE TWISTED TALE OF INFECTIOUS PROTEIN ISOFORMS - (Other)
Silva, C.J. 2004. Prions: The Twisted Tale of Infectious Protein Isoforms. The Vortex. American Chemical Society, California Section. 65(6):4.
CHOLESTEROL: A MARKER FOR THE PRESENCE OF ANIMAL MATERIAL IN FEED - (Abstract Only)