Zobrazeno 1 - 10
of 158
pro vyhledávání: '"F. Presti"'
Autor:
Mohammad Ahmad, Jeung-Hoi Ha, Lauren A. Mayse, Maria F. Presti, Aaron J. Wolfe, Kelsey J. Moody, Stewart N. Loh, Liviu Movileanu
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Sensitive and accurate approaches for protein detection have many potential applications. Here the authors show how engineered protein nanopore sensors, consisting of a monobody fused to a single-polypeptide nanopore, can be used for highly specific
Externí odkaz:
https://doaj.org/article/1f2b1191daee43b2bc50ec7144ff89b9
Autor:
Harsimranjit Sekhon, Jeung-Hoi Ha, Maria F. Presti, Spencer B. Procopio, Paige O. Mirsky, Anna M. John, Stewart N. Loh
Publikováno v:
bioRxiv
A grand challenge in biosensor design is to develop a single molecule, fluorescent protein-based platform that can be easily adapted to recognize targets of choice. Conceptually, this can be achieved by fusing a small, antibody-like binding domain to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01df9e3919de7435abd48ac624f757f0
https://doi.org/10.1101/2023.03.28.534597
https://doi.org/10.1101/2023.03.28.534597
Protein detection and biomarker profiling have implications in basic research and molecular diagnostics. Substantial progress has been made in protein analytics using nanopores and the resistive-pulse technique. Yet, a long-standing challenge is impl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::422f7f24d4c464c49ee1713c0f7635ec
Autor:
Mohammad Ahmad, Jeung-Hoi Ha, Lauren A. Mayse, Maria F. Presti, Aaron J. Wolfe, Kelsey J. Moody, Stewart N. Loh, Liviu Movileanu
Protein detection and biomarker profiling have wide-ranging implications in many areas of basic research and molecular diagnostics. Substantial progress has been made in protein analytics using nanopores and the resistive-pulse technique. Yet, a long
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceff005eb143445fccd2e931d4fdc428
https://doi.org/10.1101/2022.10.12.511930
https://doi.org/10.1101/2022.10.12.511930
Protein-based fluorescent biosensors are powerful tools for analyte recognition in vitro and in cells. Numerous proteinaceous binding scaffolds have been developed that recognize ligands with affinity and specificity comparable to those of convention
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3aff41b370e0d6628c677abb920c66db
https://doi.org/10.1101/2022.08.26.505460
https://doi.org/10.1101/2022.08.26.505460
Autor:
Thuy P Dao, Yiran Yang, Maria F Presti, Michael S Cosgrove, Jesse B Hopkins, Weikang Ma, Stewart N Loh, Carlos A Castañeda
Publikováno v:
EMBO reports. 23(8)
Ubiquitin-binding shuttle UBQLN2 mediates crosstalk between proteasomal degradation and autophagy, likely via interactions with K48- and K63-linked polyubiquitin chains, respectively. UBQLN2 comprises self-associating regions that drive its homotypic
Autor:
Pei-Ju Liu, Laura K. Gunther, Michael E. Garone, Chunling Zhang, Diana Perez, Jing Bi-Karchin, Christopher D. Pellenz, Sharon E. Chase, Maria F. Presti, Eric L. Plante, Claire E. Martin, Svjetlana Lovric, Christopher M. Yengo, Friedhelm Hildebrandt, Mira Krendel
Publikováno v:
Journal of the American Society of Nephrology : JASN. 33(11)
Myo1e is a nonmuscle motor protein enriched in podocytes. Mutations inlt;igt;MYO1Elt;/igt; are associated with steroid-resistant nephrotic syndrome (SRNS). Most of thelt;igt;MYO1Elt;/igt; variants identified by genomic sequencing have not been functi
Autor:
Thuy P. Dao, Yiran Yang, Maria F. Presti, Michael S. Cosgrove, Jesse B. Hopkins, Weikang Ma, Stewart N. Loh, Carlos A. Castañeda
SummaryUbiquitin-binding shuttle UBQLN2 mediates crosstalk between proteasomal degradation and autophagy, likely via interactions with K48- and K63-linked polyubiquitin chains, respectively. UBQLN2 is recruited to stress granules in cells and undergo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33f1ee5c3c6127cd4015078d25675758
https://doi.org/10.1101/2021.11.12.467822
https://doi.org/10.1101/2021.11.12.467822
Autor:
Pei-Ju Liu, Laura K. Gunther, Diana Perez, Jing Bi-Karchin, Christopher D. Pellenz, Sharon E. Chase, Maria F. Presti, Eric L. Plante, Claire E. Martin, Svjetlana Lovric, Christopher M. Yengo, Friedhelm Hildebrandt, Mira Krendel
Myo1e is a non-muscle motor protein enriched in the podocyte foot processes. Mutations in MYO1E are associated with steroid-resistant nephrotic syndrome (SRNS). Here, we set out to differentiate between the pathogenic and neutral MYO1E variants ident
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::974d3c0c1e9dd3790d8de4df8269ae35
https://doi.org/10.1101/2021.11.11.468158
https://doi.org/10.1101/2021.11.11.468158
Publikováno v:
J Phys Chem B
Designing proteins that can switch between active (ON) and inactive (OFF) conformations in response to signals such as ligand binding and incident light has been a tantalizing endeavor in protein engineering for over a decade. While such designs have