High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome

被引：0

作者：

Yaser Hashem

Amedee des Georges

Jie Fu

Sarah N. Buss

Fabrice Jossinet

Amy Jobe

Qin Zhang

Hstau Y. Liao

Robert A. Grassucci

Chandrajit Bajaj

Eric Westhof

Susan Madison-Antenucci

Joachim Frank

机构：

[1] Howard Hughes Medical Institute (HHMI),Department of Biochemistry and Molecular Biophysics

[2] Columbia University,Department of Biochemistry and Molecular Biophysics

[3] Columbia University,Division of Infectious Diseases, New York State Department of Health

[4] Wadsworth Center,Department of Biological Sciences

[5] Architecture et Réactivité de l’ARN,Department of Computer Science

[6] Université de Strasbourg,undefined

[7] Institut de Biologie Moléculaire et Cellulaire (CNRS),undefined

[8] Columbia University,undefined

[9] Institute for Computational Engineering and Sciences,undefined

[10] University of Texas,undefined

来源：

Nature | 2013年 / 494卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

摘要：

High-resolution cryo-electron microscopy shows that the Trypanosoma brucei kinetoplastid ribosome is characterized by the presence of large expansion segments, ribosomal-protein extensions and additional rRNA insertions, which may have implications for the protein-translation regulation process.

引用

页码：385 / 389

页数：4

共 50 条

[31] The cryo-electron microscopy structure of huntingtin
Qiang Guo
Jingdong Bin Huang
Manuel Cheng
Tatjana Seefelder
Günter Engler
Patrick Pfeifer
Markus Oeckl
Franziska Otto
Melanie Moser
Alexander Maurer
Wolfgang Pautsch
Rubén Baumeister
Stefan Fernández-Busnadiego
Nature, 2018, 555 : 117 - 120
[32] Cryo-Electron Microscopy Reaches Resolution Milestone
Peplow, Mark
ACS CENTRAL SCIENCE, 2020, 6 (08) : 1274 - 1277
[33] The cryo-electron microscopy structure of huntingtin
Guo, Qiang
Huang, Bin
Cheng, Jingdong
Seefelder, Manuel
Engler, Tatjana
Pfeifer, Guenter
Oeckl, Patrick
Otto, Markus
Moser, Franziska
Maurer, Melanie
Pautsch, Alexander
Baumeister, Wolfgang
Fernandez-Busnadiego, Ruben
Kochanek, Stefan
NATURE, 2018, 555 (7694) : 117 - +
[34] THE CRYO-ELECTRON MICROSCOPY STRUCTURE OF HUNTINGTIN
Kochanek, Stefan
Huang, Bin
Seefelder, Manuel
Engler, Tatjana
Cheng, Jingdong
Baumeister, Wolfgang
Guo, Qiang
Fernandezt-Busnadiego, Ruben
JOURNAL OF NEUROLOGY NEUROSURGERY AND PSYCHIATRY, 2018, 89 : A5 - A5
[35] Cryo-electron microscopy reaches atomic resolution
Herzik, Mark A., Jr.
NATURE, 2020, 587 (7832) : 39 - 40
[36] Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
Bartesaghi, Alberto
Matthies, Doreen
Banerjee, Soojay
Merk, Alan
Subramaniam, Sriram
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (32) : 11709 - 11714
[37] Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy
Bharat, Tanmay A. M.
Davey, Norman E.
Ulbrich, Pavel
Riches, James D.
de Marco, Alex
Rumlova, Michaela
Sachse, Carsten
Ruml, Tomas
Briggs, John A. G.
NATURE, 2012, 487 (7407) : 385 - 389
[38] Sample preparation of biological macromolecular assemblies for the determination of high-resolution structures by cryo-electron microscopy
Stark, Holger
Chari, Ashwin
MICROSCOPY, 2016, 65 (01) : 23 - 34
[39] Combining high-resolution cryo-electron microscopy and mutagenesis to develop cowpea mosaic virus for bionanotechnology
Meshcheriakova, Yulia
Durrant, Alex
Hesketh, Emma L.
Ranson, Neil A.
Lomonossoff, George P.
BIOCHEMICAL SOCIETY TRANSACTIONS, 2017, 45 : 1263 - 1269
[40] Technical development and sharing of high-resolution cryo-electron microscopes
Nakamura, Haruki
Kikkawa, Masahide
Murata, Takeshi
BIOPHYSICS AND PHYSICOBIOLOGY, 2021, 18 : 265 - 266

← 1 2 3 4 5 →