Zobrazeno 1 - 10
of 38
pro vyhledávání: '"J, Kaliszewski"'
Autor:
D. Paul Mallory, Abegel Freedman, Megan J. Kaliszewski, Gladys Rocío Montenegro-Galindo, Coleen Pugh, Adam W. Smith
Publikováno v:
Biomacromolecules.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d50e2755282313fd4d377dab9e58652d
https://doi.org/10.1021/acs.biomac.2c01538
https://doi.org/10.1021/acs.biomac.2c01538
Autor:
Michael D. Holsey, Grant T. Gilmore, Adam W. Smith, Jonathan A. Javitch, Avik Kumar Pati, Kaleeckal G. Harikumar, Zhou Zhou, Jozsef Meszaros, Laurence J. Miller, Khuloud Jaqaman, Peter Geggier, Signe Mathiasen, Wesley B. Asher, Megan J. Kaliszewski, Mitchell D. McCauley, Scott C. Blanchard, Daniel S. Terry, Alekhya Govindaraju
Publikováno v:
Nature Methods. 18:397-405
Class C G protein-coupled receptors (GPCRs) are known to form stable homodimers or heterodimers critical for function, but the oligomeric status of class A and B receptors, which constitute >90% of all GPCRs, remains hotly debated. Single-molecule fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b1d5af5024e5772f7bfbd0e90f26b66
https://doi.org/10.1038/s41592-021-01081-y
https://doi.org/10.1038/s41592-021-01081-y
Autor:
Yongjian Huang, Shashank Bharill, Deepti Karandur, Sean M Peterson, Morgan Marita, Xiaojun Shi, Megan J Kaliszewski, Adam W Smith, Ehud Y Isacoff, John Kuriyan
Publikováno v:
eLife, Vol 5 (2016)
The epidermal growth factor receptor (EGFR) is activated by dimerization, but activation also generates higher-order multimers, whose nature and function are poorly understood. We have characterized ligand-induced dimerization and multimerization of
Externí odkaz:
https://doaj.org/article/20dcaaea62014192b2103042c99e3e7a
Autor:
Wesley B, Asher, Peter, Geggier, Michael D, Holsey, Grant T, Gilmore, Avik K, Pati, Jozsef, Meszaros, Daniel S, Terry, Signe, Mathiasen, Megan J, Kaliszewski, Mitchell D, McCauley, Alekhya, Govindaraju, Zhou, Zhou, Kaleeckal G, Harikumar, Khuloud, Jaqaman, Laurence J, Miller, Adam W, Smith, Scott C, Blanchard, Jonathan A, Javitch
Publikováno v:
Nature methods. 18(4)
Class C G protein-coupled receptors (GPCRs) are known to form stable homodimers or heterodimers critical for function, but the oligomeric status of class A and B receptors, which constitute90% of all GPCRs, remains hotly debated. Single-molecule fluo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7f333d5b4d4c15d36b008483cec173d
https://pubmed.ncbi.nlm.nih.gov/33686302
https://pubmed.ncbi.nlm.nih.gov/33686302
Publikováno v:
Advances in Biomembranes and Lipid Self-Assembly ISBN: 9780081028568
Electrostatic interactions drive molecular assembly and organization in the plasma membrane. Specific protein-lipid interactions, however, are difficult to resolve. Here we report on a unique approach to investigate these interactions with time-resol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd628144231dc42a295a5ee004754522
https://doi.org/10.1016/bs.abl.2019.01.005
https://doi.org/10.1016/bs.abl.2019.01.005
Autor:
Kevin C. Skinner, Morgan Marita, Yuxiao Wang, Pranathi Dasari, Xuewu Zhang, Xiaojun Shi, Adam W. Smith, William D. Comar, Megan J. Kaliszewski
Publikováno v:
Biophysical Journal. 109(9):1937-1945
Plexins are single-pass transmembrane receptors that bind the axon guidance molecules semaphorins. Single-pass transmembrane proteins are an important class of receptors that display a wide variety of activation mechanisms, often involving ligand-dep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0a67579f5f6e15d9ea70795d56ec40e
Publikováno v:
Langmuir. 31:1784-1791
Binding of biomacromolecules to anionic lipids in the plasma membrane is a common motif in many cell signaling pathways. Previous work has shown that macromolecules with cationic sequences can form nanodomains with sequestered anionic lipids, which a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad3129c152246d9597b1646a2b8b44e5
https://doi.org/10.1021/la504241w
https://doi.org/10.1021/la504241w
Autor:
Hui Jin, Kevin C. Skinner, Megan J. Kaliszewski, Adam W. Smith, Morgan H. Torcasio, William D. Comar, Krzysztof Palczewski, Anthony S. Esway, Beata Jastrzebska
Publikováno v:
Biochemistry. 56(1)
G protein-coupled receptors (GPCRs) detect a wide variety of physical and chemical signals and transmit that information across the cellular plasma membrane. Dimerization is a proposed modulator of GPCR signaling, but the structure and stability of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c22225f2b0b9ef7e7ebbe65b3f428d6
https://pubmed.ncbi.nlm.nih.gov/28045251
https://pubmed.ncbi.nlm.nih.gov/28045251
Autor:
Shashank Bharill, Xiaojun Shi, Adam W. Smith, Ehud Y. Isacoff, Megan J. Kaliszewski, Seana M Peterson, Deepti Karandur, Yongjian Huang, John Kuriyan, Morgan Marita
Publikováno v:
Huang, Y; Bharill, S; Karandur, D; Peterson, SM; Marita, M; Shi, X; et al.(2016). Molecular basis for multimerization in the activation of the epidermal growth factor receptor. eLife, 5(MARCH2016). doi: 10.7554/eLife.14107. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/4hb8p75r
eLife, Vol 5 (2016)
eLife, vol 5, iss MARCH2016
eLife
eLife, Vol 5 (2016)
eLife, vol 5, iss MARCH2016
eLife
The epidermal growth factor receptor (EGFR) is activated by dimerization, but activation also generates higher-order multimers, whose nature and function are poorly understood. We have characterized ligand-induced dimerization and multimerization of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f65d07cda9be588344ebba6880aa45ef
http://www.escholarship.org/uc/item/4hb8p75r
http://www.escholarship.org/uc/item/4hb8p75r
Autor:
Deepti Karandur, Adam W. Smith, Morgan Marita, Yongjian Huang, Ehud Y. Isacoff, Xiaojun Shi, Megan J. Kaliszewski, Sean M. Peterson, Shashank Bharill, John Kuriyan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2703a088fb6cbd62fdb132029718d95
https://doi.org/10.7554/elife.14107.023
https://doi.org/10.7554/elife.14107.023