Results 61 to 70 of about 99,841 (293)

Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor [PDF]

, 2010
We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM.
Ban, Nenad, Boehringer, Daniel, Estrozi, Leandro F., Schaffitzel, Christiane, Shan, Shu-ou   +4 more
core   +1 more source

Engineered extracellular vesicles enriched with the miR‐214/199a cluster enhance the efficacy of chemotherapy in ovarian cancer

Molecular Oncology, EarlyView.
Loss of the miR‐214/199a cluster is associated with recurrence in ovarian cancer. Engineered small extracellular vesicles (m214‐sEVs) elevate miR‐214‐3p/miR‐199a‐5p in tumor cells, suppress β‐catenin, TLR4, and YKT6 signaling, reprogram tumor‐derived sEV cargo, reduce chemoresistance and migration, and enhance carboplatin efficacy and survival in ...
Weida Wang, Ayesha Alvero, Yi Qin, Mingjin Wang, Alexandra Fox, Yanfeng Li, Michael Millman, Amy Kemper, Gil Mor, Xian Shuang Liu, Michael Chopp, Zheng Gang Zhang, Yi Zhang   +12 more
wiley   +1 more source

A cryo-electron microscopic approach to elucidate protein structures from human brain microsomes

Life Science Alliance, 2023
Using cryo-EM to simultaneously identify and solve structures of five enzymes from a raw human brain microsomal lysate, highlighting the potential for facilitating structural-omics at the atomic level.
Marios L Tringides, Zhemin Zhang, Christopher E Morgan, Chih-Chia Su, Edward W Yu   +4 more
doaj   +1 more source

Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement. [PDF]

, 2019
Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The Saccharomyces cerevisiae RSC (Remodeling the Structure of Chromatin) complex, a member of the SWI/SNF chromatin ...
Afonine, Afonine, Allen, Angus-Hill, Ashkenazy, Ashkenazy, Asturias, Badis, Buchan, Buchan, Cairns, Cairns, Campsteijn, Chaban, Chambers, Chatterjee, Clapier, Clapier, Côté, Da, Dechassa, Duan, Dutta, Dürr, El-Gebali, Emsley, Erkina, Filippakopoulos, Goddard, Han, Jones, Jones, Kadoch, Kasten, Klein-Brill, Krietenstein, Kuryan, Leschziner, Leschziner, Li, Liu, Lopéz-Blanco, Mashtalir, Morin, Nagai, Nakane, Ng, Patel, Pettersen, Puig, Saha, Sammak, Schorb, Schubert, Sen, Shim, Sievers, Skiniotis, Smith, Suloway, Söding, Tan, Tsunaka, Ungar, Valencia, Wagner, Wang, Wilson, Xia, Yan, Yang, Ye, Yen, Zhang, Zhang, Zhang, Zheng, Zivanov, Zivanov, Zukin   +79 more
core   +3 more sources

A light‐triggered Time‐Resolved X‐ray Solution Scattering (TR‐XSS) workflow with application to protein conformational dynamics

FEBS Open Bio, EarlyView.
Time‐resolved X‐ray solution scattering captures how proteins change shape in real time under near‐native conditions. This article presents a practical workflow for light‐triggered TR‐XSS experiments, from data collection to structural refinement. Using a calcium‐transporting membrane protein as an example, the approach can be broadly applied to study ...
Fatemeh Sabzian‐Molaei, Fredrik Orädd, Konstantinos Magkakis, Magnus Andersson   +3 more
wiley   +1 more source

Substrates bind to residues lining the ring of asymmetrically engaged bacterial proteasome activator Bpa

Nature Communications
Mycobacteria harbor a proteasome that was acquired by Actinobacteria through horizontal gene transfer and that supports the persistence of the human pathogen Mycobacterium tuberculosis within host macrophages. The core particle of the proteasome (20S CP)
Tatjana von Rosen, Rafal Zdanowicz, Yasser El Hadeg, Pavel Afanasyev, Daniel Boehringer, Alexander Leitner, Rudi Glockshuber, Eilika Weber-Ban   +7 more
doaj   +1 more source

The Triplex-Centric Assembly and Maturation of the Herpesvirus Procapsid

Viruses
Herpesviruses are prevalent infectious agents in humans, with complex structures and life cycles. The viability and detail of a model of capsid assembly and maturation can now be examined against the recently available mature herpesvirus capsids ...
J. Bernard Heymann
doaj   +1 more source

Cryo-EM advances in RNA structure determination

Signal Transduction and Targeted Therapy, 2022
Cryo-electron microscopy (cryo-EM) has emerged as an unprecedented tool to resolve protein structures at atomic resolution. Structural insights of biological samples not accessible by conventional X-ray crystallography and NMR can be explored with cryo ...
Haiyun Ma, Xinyu Jia, Kaiming Zhang, Zhaoming Su   +3 more
doaj   +1 more source

Interpreting the cryo-EM map [PDF]

IUCrJ, 2019
Beckers et al. [IUCrJ (2019), 6, 18-33] propose a general approach to visualization of cryo-EM maps. Their method overcomes some of the challenges inherent in the conventional approach for depicting maps using a single isosurface threshold.
openaire   +3 more sources

Cryo-EM: Spinning the Micelles Away [PDF]

Structure, 2015
Structural characterization of integral membrane proteins (MPs) demands that the samples be pure, monodisperse, and stable. Detergents are required to extract MPs from the lipid bilayer in which they reside and to stabilize them for downstream biophysical analyses.
Singh, Satinder K., Sigworth, Fred J.
openaire   +2 more sources