Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Aida Razi"'
Autor:
Jasmin Federizon, Conrard Giresse Tetsassi Feugmo, Wei-Chiao Huang, Xuedan He, Kazutoyo Miura, Aida Razi, Joaquin Ortega, Mikko Karttunen, Jonathan F. Lovell
Publikováno v:
Pharmaceutics, Vol 13, Iss 1, p 98 (2021)
Cobalt porphyrin phospholipid (CoPoP) can incorporate within bilayers to enable non-covalent surface-display of antigens on liposomes by mixing with proteins bearing a polyhistidine tag (his-tag); however, the mechanisms for how this occurs are poorl
Externí odkaz:
https://doaj.org/article/c294f218516a4589b97c589e2b7c5a29
Autor:
Nikhil Jain, Joaquin Ortega, Aida Razi, Alba Guarné, Xiaodan Ni, Kaustuv Basu, Amal Seffouh, Robert A. Britton, Dushyant Jahagirdar
Publikováno v:
Nucleic Acids Research
Bacteria harbor a number GTPases that function in the assembly of the ribosome and are essential for growth. RbgA is one of these GTPases and is required for the assembly of the 50S subunit in most bacteria. Homologs of this protein are also implicat
Highly-Soluble Cyanine J-aggregates Entrapped by Liposomes for In Vivo Optical Imaging around 930 nm
Autor:
Jumin Geng, Depeng Wang, Yang Zhou, Jonathan F. Lovell, Joaquin Ortega, Haoyuan Huang, Hak Soo Choi, Aida Razi, Ye Zhan, Homan Kang, Dyego Miranda, Jun Xia, Hailey I Kilian, Wesley R. Stiles
Publikováno v:
Theranostics
Near infrared (NIR) dyes are useful for in vivo optical imaging. Liposomes have been used extensively for delivery of diverse cargos, including hydrophilic cargos which are passively loaded in the aqueous core. However, most currently available NIR d
Autor:
Xuedan He, Conrard Giresse Tetsassi Feugmo, Jonathan F. Lovell, Mikko Karttunen, Joaquin Ortega, Kazutoyo Miura, Aida Razi, Jasmin Federizon, Wei-Chiao Huang
Publikováno v:
Pharmaceutics, Vol 13, Iss 98, p 98 (2021)
Pharmaceutics
Chemistry Publications
Volume 13
Issue 1
Pharmaceutics
Chemistry Publications
Volume 13
Issue 1
Cobalt porphyrin phospholipid (CoPoP) can incorporate within bilayers to enable non-covalent surface-display of antigens on liposomes by mixing with proteins bearing a polyhistidine tag (his-tag)
however, the mechanisms for how this occurs are p
however, the mechanisms for how this occurs are p
Autor:
Joaquin Ortega, Aida Razi
Publikováno v:
eLS
The ribosome is the macromolecular assembly dedicated to translating the genetic information into proteins. Ribosomes are made of several RNA molecules and between 50 and 80 proteins. The role played by these proteins has been the focus of investigat
Autor:
Aida Razi, Joaquin Ortega, Kaustuv Basu, Amal Seffouh, Alba Guarné, Xiaodan Ni, Robert A. Britton, Dushyant Jahagirdar, Nikhil Jain
Publikováno v:
Microscopy and Microanalysis. 26:118-119
Publikováno v:
Nucleic Acids Research
Cryo-electron microscopy (cryo-EM) had played a central role in the study of ribosome structure and the process of translation in bacteria since the development of this technique in the mid 1980s. Until recently cryo-EM structures were limited to ∼
Autor:
Yao Shen, Tamiza Nanji, Emma J. Gehrke, Melanie Gloyd, Alba Guarné, Angela Huynh, Marie A. Elliot, Aida Razi, Xiafei Zhang, Joaquin Ortega, Christopher D. Firby
Publikováno v:
Biochimica et biophysica acta. General subjects. 1863(11)
Background Nucleoid associated proteins (NAPs) are essential for chromosome condensation in bacterial cells. Despite being a diverse group, NAPs share two common traits: they are small, oligomeric proteins and their oligomeric state is critical for D
Autor:
Javier Vargas, Nikhil Jain, Alba Guarné, James R. Williamson, Kaustuv Basu, Dushyant Jahagirdar, Robert A. Britton, Joseph H. Davis, Brett Thurlow, Aida Razi, Yumeng Hao, Sarah A. Woodson, Joaquin Ortega, Josué Gómez-Blanco
SUMMARYTo reveal the role of the essential protein Era in the assembly of the 30S ribosomal subunit, we analyzed assembly intermediates that accumulated in Era-depletedEscherichia colicells using quantitative mass spectrometry, cryo-electron microsco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83ba7fc32eb2236ed23e827d30d8c29d
https://doi.org/10.1101/525360
https://doi.org/10.1101/525360
Autor:
Nikhil Jain, Xiaodan Ni, Joseph H. Davis, Robert A. Britton, Joaquin Ortega, John L. Rubinstein, Andrew G. McArthur, Aida Razi, James R. Williamson, Samir Benlekbir
Publikováno v:
Nucleic Acids Research
YphC and YsxC are GTPases in Bacillus subtilis that facilitate the assembly of the 50S ribosomal subunit, however their roles in this process are still uncharacterized. To explore their function, we used strains in which the only copy of the yphC or