Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jonathan B. Leano"'
Autor:
Jonathan B Leano, Samir Batarni, Jacob Eriksen, Narinobu Juge, John E Pak, Tomomi Kimura-Someya, Yaneth Robles-Colmenares, Yoshinori Moriyama, Robert M Stroud, Robert H Edwards
Publikováno v:
PLoS Biology, Vol 17, Iss 5, p e3000260 (2019)
Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins u
Externí odkaz:
https://doaj.org/article/65102fbea5e242989c390f1b3737e279
Autor:
Jonathan B Leano, Kevin C Slep
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0219823 (2019)
Tubulin-binding TOG domains are found arrayed in a number of proteins that regulate microtubule dynamics. While much is known about the structure and function of TOG domains from the XMAP215 microtubule polymerase family, less in known about the TOG
Externí odkaz:
https://doaj.org/article/34e0550ce1ee4511a9d3467561d08a44
Autor:
Jarrett D. Egertson, Cassandra Stawicki, Taryn E. Gillies, James H. Joly, Noah Steiner, Kevin Cardenas, Jonathan B. Leano, Kevin Chen, Sophie Watts, Hunter B. Boyce, Dan DiPasquo, Alana Killeen, Vadim Lobanov, Greg Kapp, Sujal Patel, Parag Mallick
Publikováno v:
Cancer Research. 82:LB225-LB225
Protein Identification by Short-epitope Mapping (PrISM) is a novel proteomics method with the goal of comprehensive proteome quantification at single-molecule sensitivity. In this work, we present computational modeling demonstrating the feasibility
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8192fc0699725988348163484613469
https://doi.org/10.1158/1538-7445.am2022-lb225
https://doi.org/10.1158/1538-7445.am2022-lb225
Autor:
John E. Pak, Robert M. Stroud, Yaneth Robles-Colmenares, Samir Batarni, Jacob Eriksen, Robert H. Edwards, Jonathan B. Leano, Yoshinori Moriyama, Narinobu Juge, Tomomi Kimura-Someya
Publikováno v:
PLoS Biology
PLoS Biology, Vol 17, Iss 5, p e3000260 (2019)
PLoS biology, vol 17, iss 5
PLoS Biology, Vol 17, Iss 5, p e3000260 (2019)
PLoS biology, vol 17, iss 5
Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55db0d2a5d3f79f6b4600980886e3182
http://europepmc.org/articles/PMC6532931
http://europepmc.org/articles/PMC6532931
Autor:
Kevin C. Slep, Jonathan B. Leano
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0219823 (2019)
PLoS ONE
PLoS ONE
Tubulin-binding TOG domains are found arrayed in a number of proteins that regulate microtubule dynamics. While much is known about the structure and function of TOG domains from the XMAP215 microtubule polymerase family, less in known about the TOG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::669c244e95333d2f66a151168c84ead1
https://doi.org/10.1101/479766
https://doi.org/10.1101/479766
Publikováno v:
Biophysical Journal. 116:56a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9dc1375bab77e42445964efc57e1f9cd
https://doi.org/10.1016/j.bpj.2018.11.349
https://doi.org/10.1016/j.bpj.2018.11.349
CLASP is a key regulator of microtubule (MT) dynamics and bipolar mitotic spindle structure with CLASP mutants displaying a distinctive monopolar spindle phenotype. It has been postulated that cryptic TOG domains underlie CLASP’s ability regulate M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40679ada028f4911aba7bbe2929b6ef4
https://europepmc.org/articles/PMC3731388/
https://europepmc.org/articles/PMC3731388/