Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Debora L. Makino"'
Autor:
Elisabeth Stegmann, Debora L. Makino, Marc Baumgärtner, Elena Conti, Benjamin Schuch, Claire Basquin
Publikováno v:
Nature. 524:54-58
The eukaryotic exosome is a conserved RNA-degrading complex that functions in RNA surveillance, turnover and processing. How the same machinery can either completely degrade or precisely trim RNA substrates has long remained unexplained. Here we repo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ae3c7c94596446b8b3a108591ff2936
https://doi.org/10.1038/nature14865
https://doi.org/10.1038/nature14865
Autor:
Holger Sondermann, Jodi Gureasko, Dafna Bar-Sagi, John Kuriyan, Olga Kuchment, Debora L. Makino
Publikováno v:
Proceedings of the National Academy of Sciences. 107:3430-3435
Membrane-bound Ras is activated by translocation of the Son of Sevenless (SOS) protein to the plasma membrane. SOS is inactive unless Ras is bound to an allosteric site on SOS, and the Dbl homology (DH) and Pleckstrin homology (PH) domains of SOS (th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cccad0ca6283e7e81eed157999d6af67
https://doi.org/10.1073/pnas.0913915107
https://doi.org/10.1073/pnas.0913915107
Autor:
Eric R. Goedken, Mike O'Donnell, Kyle R. Simonetta, Steven N. Seyedin, John Kuriyan, Debora L. Makino, Brian A. Kelch, Aaron J. Cantor, Randall McNally, Steven L. Kazmirski
Publikováno v:
Cell. 137:659-671
SummaryClamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdc8432dc4e910c11b76df9ba221f162
https://doi.org/10.1016/j.cell.2009.03.044
https://doi.org/10.1016/j.cell.2009.03.044
Publikováno v:
Makino, DL; Day, J; Larson, SB; & McPherson, A. (2006). Investigation of RNA structure in satellite panicum mosaic virus. Virology, 351(2), 420-431. doi: 10.1016/j.virol.2006.03.028. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/0bk7h031
Three new crystal forms of satellite panicum mosaic virus (SPMV) were grown and their structures solved from X-ray diffraction data using molecular replacement techniques. The crystals were grown under conditions of pH and ionic strength that were ap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86c2ee477c6bb38d8fdc6a8755294268
Publikováno v:
Makino, DL; Henschen-Edman, AH; & McPherson, A. (2005). Four crystal forms of a Bence-Jones protein. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(1), 79-82. doi: 10.1107/S1744309104028532. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/6h80f902
Four crystal forms have been grown and characterized by X-ray diffraction of a Bence-Jones protein collected from the urine of a multiple myeloma patient more than 40 years ago. Closely related tetragonal and orthorhombic forms belonging to space gro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::174024a4d24ecca222be00958d4f4a6c
https://doi.org/10.1107/s1744309104028532
https://doi.org/10.1107/s1744309104028532
The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase
Autor:
Sebastian Falk, Elena Conti, Claire Basquin, Phil Mitchell, Benjamin Schuch, Monika Feigenbutz, Debora L. Makino
The exosome is a conserved multi-subunit ribonuclease complex that functions in 3′ end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1ee66f1a7769e906f25d96d6526790c
https://europepmc.org/articles/PMC4282559/
https://europepmc.org/articles/PMC4282559/
Autor:
Elena Conti, Debora L. Makino
Publikováno v:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Acta Crystallographica Section D Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography
The crystallographic steps towards the structure determination of a complete eukaryotic exosome complex bound to RNA are presented. Phasing of this 11-protein subunit complex was carried out via molecular replacement.
The RNA exosome is an evolu
The RNA exosome is an evolu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f675ca0de765d1a68c5d4d956df92007
https://hdl.handle.net/11858/00-001M-0000-0014-C2CF-911858/00-001M-0000-0014-C2CD-D
https://hdl.handle.net/11858/00-001M-0000-0014-C2CF-911858/00-001M-0000-0014-C2CD-D
Publikováno v:
Makino, DL; Larson, SB; & McPherson, A. (2013). The crystallographic structure of Panicum Mosaic Virus (PMV). Journal of Structural Biology, 181(1), 37-52. doi: 10.1016/j.jsb.2012.10.012. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4x39z016
The structure of Panicum Mosaic Virus (PMV) was determined by X-ray diffraction analysis to 2.9å resolution. The crystals were of pseudo symmetry F23; the true crystallographic unit cell was of space group P21 with a=411.7å, b=403.9å and c=412.5å
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dd93b9f9df7f458ac93a2c0e8a34e0d
http://www.escholarship.org/uc/item/4x39z016
http://www.escholarship.org/uc/item/4x39z016
Publikováno v:
Nature. 495(7439)
The exosome is the major 3'-5' RNA-degradation complex in eukaryotes. The ubiquitous core of the yeast exosome (Exo-10) is formed by nine catalytically inert subunits (Exo-9) and a single active RNase, Rrp44. In the nucleus, the Exo-10 core recruits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f088d0bd9eba9d45a691a049b344479
https://pubmed.ncbi.nlm.nih.gov/23376952
https://pubmed.ncbi.nlm.nih.gov/23376952
Autor:
Robert C. Nutter, Debora L. Makino, Jun Li, Kun Qu, Michael Kertesz, Yue Wan, Zhengqing Ouyang, Robert Tibshirani, Eran Segal, Howard Y. Chang
SUMMARY RNA structural transitions are important in the function and regulation of RNAs. Here, we reveal a layer of transcriptome organization in the form of RNA folding energies. By probing yeast RNA structures at different temperatures, we obtained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::982038a6fad81fd93ba98aa28d79adc8
https://europepmc.org/articles/PMC3483374/
https://europepmc.org/articles/PMC3483374/