Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Elizabeth V. Landorf"'
Autor:
Kemin Tan, Changsoo Chang, Sarah Zerbs, Frank R. Collart, Elizabeth V. Landorf, Andrzej Joachimiak, Marianne E. Cuff, Jamey C. Mack, Jerzy Osipiuk
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:1709-1726
Lignin comprises 15.25% of plant biomass and represents a major environmental carbon source for utilization by soil microorganisms. Access to this energy resource requires the action of fungal and bacterial enzymes to break down the lignin polymer in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bdbd1d85cd867dd294f76e5c0d3c81f8
https://doi.org/10.1002/prot.24305
https://doi.org/10.1002/prot.24305
Autor:
Andrew E. Plymale, Margaret F. Romine, Lindsey N. Anderson, Elizabeth V. Landorf, Frank R. Collart, Allan E. Konopka, Aaron T. Wright, Mary S. Lipton, Phillip K. Koech
Publikováno v:
ACS chemical biology. 11(2)
The rapid completion of microbial genomes is inducing a conundrum in functional gene discovery. Novel methods are needed to shorten the gap between characterizing a microbial genome and experimentally validating bioinformatically predicted functions.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c92fc90d9d8b37562ac56055f60fb5d2
https://pubmed.ncbi.nlm.nih.gov/26669591
https://pubmed.ncbi.nlm.nih.gov/26669591
Autor:
Elizabeth V. Landorf, Shimon Weiss, Younggyu Kim, You Korlann, Natalie R. Gassman, Frank R. Collart, Sam On Ho
Publikováno v:
Bioconjugate Chemistry. 19:786-791
Methods for chemical modifications of proteins have been crucial for the advancement of proteomics. In particular, site-specific covalent labeling of proteins with fluorophores and other moieties has permitted the development of a multitude of assays
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07908b6cbee6438274be96fc6b57d7bc
https://doi.org/10.1021/bc7002499
https://doi.org/10.1021/bc7002499
Autor:
Wenjin Guo, Andrew T. Bauman, Sean Rapson, Elizabeth Stewart, Eugene Kolker, Natali Kolker, Robin Stacy, Roger Higdon, Peter J. Myler, Gerald van Belle, Jared C. Roach, Elizabeth V. Landorf, Brenton Loiue, Wesley C. Van Voorhis, Vincent Lu, Alberto J. Napuli, Jason M. Hogan, Frank R. Collart
High-throughput (HTP) proteomics studies generate large amounts of data. Interpretation of these data requires effective approaches to distinguish noise from biological signal, particularly as instrument and computational capacity increase and studie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4f5eda8edcdd89e6607601665e7dd0c
https://europepmc.org/articles/PMC3110723/
https://europepmc.org/articles/PMC3110723/
Publikováno v:
eLS
Purified proteins are a starting point for many experimental, therapeutic and commercial applications. Developments in biotechnology have generated a collection of resources to enable production of proteins from a variety of sources. Keywords: protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29aa4eb34f8bdc245b3d61bc25b6043d
https://doi.org/10.1002/9780470015902.a0000983.pub2
https://doi.org/10.1002/9780470015902.a0000983.pub2
Autor:
Eugene Kolker, Frank R. Collart, Gerald van Belle, Alexander F. Yakunin, Natali Kolker, Elizabeth V. Landorf, Roger Higdon, Jason M. Hogan
Publikováno v:
Proteomics. 7(20)
Mixtures of known proteins have been very useful in the assessment and validation of methods for high-throughput (HTP) MS (MS/MS) proteomics experiments. However, these test mixtures have generally consisted of few proteins at near equal concentratio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f4e097689043eed86301bce610bbe9
https://pubmed.ncbi.nlm.nih.gov/17890649
https://pubmed.ncbi.nlm.nih.gov/17890649
Autor:
Priscilla A. Moore, Chiann Tso Lin, Vladimir Kery, Elizabeth V. Landorf, Kristin D. Victry, Frank R. Collart, Deanna L. Auberry, Teresa Peppler
Publikováno v:
Protein expression and purification. 47(1)
Protein crystallography, mapping protein interactions, and other functional genomic approaches require purifying many different proteins, each of sufficient yield and homogeneity, for subsequent high-throughput applications. To fill this requirement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d53f3b9e4a7c193846dd05c82243608c
https://pubmed.ncbi.nlm.nih.gov/16406573
https://pubmed.ncbi.nlm.nih.gov/16406573
Autor:
Younggyu Kim, Shimon Weiss, Sam O. Ho, Natalie R. Gassman, You Korlann, Elizabeth V. Landorf, Frank R. Collart
Publikováno v:
Bioconjugate Chemistry; Mar2008, Vol. 19 Issue 3, p786-791, 6p