Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Marco J, Lobba"'
Autor:
Marco J. Lobba, Christof Fellmann, Alan M. Marmelstein, Johnathan C. Maza, Elijah N. Kissman, Stephanie A. Robinson, Brett T. Staahl, Cole Urnes, Rachel J. Lew, Casey S. Mogilevsky, Jennifer A. Doudna, Matthew B. Francis
Publikováno v:
ACS Central Science, Vol 6, Iss 9, Pp 1564-1571 (2020)
Externí odkaz:
https://doaj.org/article/717bb74132f54986ad0e5c0d11e24c37
Autor:
Emily C. Hartman, Christopher M. Jakobson, Andrew H. Favor, Marco J. Lobba, Ester Álvarez-Benedicto, Matthew B. Francis, Danielle Tullman-Ercek
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Self-assembling proteins have important applications in industrial technologies, but it is difficult to predict how mutations affect assembly. Here the authors present SyMAPS, coupling comprehensive codon mutagenesis with high-throughput sequencing,
Externí odkaz:
https://doaj.org/article/32650acf858e4272b1227a70f3e4f8ee
Autor:
Gavin J Knott, Brady F Cress, Jun-Jie Liu, Brittney W Thornton, Rachel J Lew, Basem Al-Shayeb, Daniel J Rosenberg, Michal Hammel, Benjamin A Adler, Marco J Lobba, Michael Xu, Adam P Arkin, Christof Fellmann, Jennifer A Doudna
Publikováno v:
eLife, Vol 8 (2019)
CRISPR-Cas systems provide bacteria and archaea with programmable immunity against mobile genetic elements. Evolutionary pressure by CRISPR-Cas has driven bacteriophage to evolve small protein inhibitors, anti-CRISPRs (Acrs), that block Cas enzyme fu
Externí odkaz:
https://doaj.org/article/164dc30ebd294804bf4e661f484ab735
Autor:
Marco J. Lobba, Jennifer A. Doudna, Jamie M Gleason, Daniel D. Brauer, Casey S. Mogilevsky, Matthew B. Francis, Johnathan C. Maza, Alan M. Marmelstein
Publikováno v:
J Am Chem Soc
Site-selective protein–protein coupling has long been a goal of chemical biology research. In recent years, that goal has been realized to varying degrees through a number of techniques, including the use of tyrosinase-based coupling strategies. Ea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38958dba634715c0cce2c3e4bb0a0779
https://doi.org/10.1021/jacs.1c03079
https://doi.org/10.1021/jacs.1c03079
Autor:
Matthew B. Francis, Alan M. Marmelstein, Brett T. Staahl, Johnathan C. Maza, Stephanie A. Robinson, Elijah N Kissman, Marco J. Lobba, Casey S. Mogilevsky, Rachel J. Lew, Jennifer A. Doudna, Christof Fellmann, Cole Urnes
Publikováno v:
ACS Central Science, Vol 6, Iss 9, Pp 1564-1571 (2020)
ACS Central Science
ACS Central Science
The synthesis of protein–protein and protein–peptide conjugates is an important capability for producing vaccines, immunotherapeutics, and targeted delivery agents. Herein we show that the enzyme tyrosinase is capable of oxidizing exposed tyrosin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4600a77b0411205dee1e9f3902acd10d
https://doaj.org/article/717bb74132f54986ad0e5c0d11e24c37
https://doaj.org/article/717bb74132f54986ad0e5c0d11e24c37
Autor:
Johnathan C. Maza, Marco J. Lobba, Daniel D. Brauer, Matthew B. Francis, Casey S. Mogilevsky, Alan M. Marmelstein
Publikováno v:
Journal of the American Chemical Society. 142:5078-5086
Oxidative coupling (OC) through o-quinone intermediates has been established as an efficient and site-selective way to modify protein N-termini and the unnatural amino acid p-aminophenylalanine (paF). Recently, we reported that the tyrosinase-mediate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84dfb8a4a882313a57757eebe0334015
https://doi.org/10.1021/jacs.9b12002
https://doi.org/10.1021/jacs.9b12002
Autor:
Marco J. Lobba, Gavin J. Knott, Brittney W. Thornton, Jun-Jie Liu, Basem Al-Shayeb, Kyle E. Watters, Jennifer A. Doudna
Publikováno v:
Nature structural & molecular biology, vol 26, iss 4
Knott, Gavin J; Thornton, Brittney W; Lobba, Marco J; Liu, Jun-Jie; Al-Shayeb, Basem; Watters, Kyle E; et al.(2019). Broad-spectrum enzymatic inhibition of CRISPR-Cas12a.. Nature structural & molecular biology, 26(4), 315-321. doi: 10.1038/s41594-019-0208-z. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/72n7n3pp
Nature structural & molecular biology
Knott, Gavin J; Thornton, Brittney W; Lobba, Marco J; Liu, Jun-Jie; Al-Shayeb, Basem; Watters, Kyle E; et al.(2019). Broad-spectrum enzymatic inhibition of CRISPR-Cas12a.. Nature structural & molecular biology, 26(4), 315-321. doi: 10.1038/s41594-019-0208-z. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/72n7n3pp
Nature structural & molecular biology
Cas12a is a bacterial RNA-guided nuclease used widely for genome editing and, more recently, as a molecular diagnostic. In bacteria, Cas12a enzymes can be inhibited by bacteriophage-derived proteins, anti-CRISPRs (Acrs), to thwart clustered regularly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33b1124d75a71b561581bf7c713cb76a
https://doi.org/10.1038/s41594-019-0208-z
https://doi.org/10.1038/s41594-019-0208-z
Autor:
Shrutee, Jakhanwal, Brady F, Cress, Pascal, Maguin, Marco J, Lobba, Luciano A, Marraffini, Jennifer A, Doudna
Publikováno v:
Nucleic Acids Research
CRISPR-Cas9 is an RNA-guided DNA endonuclease involved in bacterial adaptive immunity and widely repurposed for genome editing in human cells, animals and plants. In bacteria, RNA molecules that guide Cas9′s activity derive from foreign DNA fragmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e5d615ab94772cdc768bf43e3cab239e
https://pubmed.ncbi.nlm.nih.gov/33693715
https://pubmed.ncbi.nlm.nih.gov/33693715
Autor:
Luciano A. Marraffini, Marco J. Lobba, Jennifer A. Doudna, Brady F. Cress, Shrutee Jakhanwal, Pascal Maguin
Publikováno v:
Nucleic Acids Research.
CRISPR-Cas9 is an RNA-guided DNA endonuclease involved in bacterial adaptive immunity and widely repurposed for genome editing in human cells, animals and plants. In bacteria, RNA molecules that guide Cas9's activity derive from foreign DNA fragments
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f78d490d2f5cd1e085b5aafb090fb2d0
https://doi.org/10.1093/nar/gkab123
https://doi.org/10.1093/nar/gkab123
Autor:
Stephanie A. Robinson, Emily C. Hartman, Marco J. Lobba, Andrew H. Favor, Matthew B. Francis, Danielle Tullman-Ercek
Publikováno v:
Biochemistry. 58:1527-1538
Protein evolution occurs via restricted evolutionary paths that are influenced by both previous and subsequent mutations. This effect, termed epistasis, is critical in population genetics, drug resistance, and immune escape; however, the effect of ep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e94c20e9e44bd618d74a18ead1af8fc1
https://doi.org/10.1021/acs.biochem.8b00948
https://doi.org/10.1021/acs.biochem.8b00948