[图书][B] Single-particle Cryo-EM of biological macromolecules
This edited book is written for students, postdocs and established investigators who want to
enter the field of single-particle cryo-EM. This is a recently developed method to determine …
enter the field of single-particle cryo-EM. This is a recently developed method to determine …
Temperature-resolved cryo-EM uncovers structural bases of temperature-dependent enzyme functions
CY Chen, YC Chang, BL Lin, CH Huang… - Journal of the …, 2019 - ACS Publications
Protein functions are temperature-dependent, but protein structures are usually solved at a
single (often low) temperature because of limitations on the conditions of crystal growth or …
single (often low) temperature because of limitations on the conditions of crystal growth or …
Structural and dynamic basis of DNA capture and translocation by mitochondrial Twinkle helicase
Twinkle is a mitochondrial replicative helicase which can self-load onto and unwind
mitochondrial DNA. Nearly 60 mutations on Twinkle have been linked to human …
mitochondrial DNA. Nearly 60 mutations on Twinkle have been linked to human …
Structural basis of DNA polymerase θ mediated DNA end joining
DNA polymerase θ (Pol θ) plays an essential role in the microhomology-mediated end
joining (MMEJ) pathway for repairing DNA double-strand breaks. However, the mechanisms …
joining (MMEJ) pathway for repairing DNA double-strand breaks. However, the mechanisms …
Flexibility revealed by the 1.85 Å crystal structure of the β sliding-clamp subunit of Escherichia coli DNA polymerase III
AJ Oakley, P Prosselkov, G Wijffels… - … Section D: Biological …, 2003 - journals.iucr.org
The β subunit of the Escherichia coli replicative DNA polymerase III holoenzyme is the
sliding clamp that interacts with the α (polymerase) subunit to maintain the high processivity …
sliding clamp that interacts with the α (polymerase) subunit to maintain the high processivity …
Duplex DNA engagement and RPA oppositely regulate the DNA-unwinding rate of CMG helicase
HB Kose, S Xie, G Cameron, MS Strycharska… - Nature …, 2020 - nature.com
A ring-shaped helicase unwinds DNA during chromosome replication in all organisms.
Replicative helicases generally unwind duplex DNA an order of magnitude slower …
Replicative helicases generally unwind duplex DNA an order of magnitude slower …
A structural view of bacterial DNA replication
AJ Oakley - Protein Science, 2019 - Wiley Online Library
DNA replication mechanisms are conserved across all organisms. The proteins required to
initiate, coordinate, and complete the replication process are best characterized in model …
initiate, coordinate, and complete the replication process are best characterized in model …
The N-terminal domain of human mitochondrial helicase Twinkle has DNA-binding activity crucial for supporting processive DNA synthesis by polymerase γ
Twinkle is the ring-shaped replicative helicase within the human mitochondria with high
homology to bacteriophage T7 gp4 helicase–primase. Unlike many orthologs of Twinkle, the …
homology to bacteriophage T7 gp4 helicase–primase. Unlike many orthologs of Twinkle, the …
An explanation for origin unwinding in eukaryotes
LD Langston, ME O'Donnell - Elife, 2019 - elifesciences.org
Twin CMG complexes are assembled head-to-head around duplex DNA at eukaryotic
origins of replication. Mcm10 activates CMGs to form helicases that encircle single-strand …
origins of replication. Mcm10 activates CMGs to form helicases that encircle single-strand …
Mechanisms for maintaining eukaryotic replisome progression in the presence of DNA damage
TA Guilliam - Frontiers in molecular biosciences, 2021 - frontiersin.org
The eukaryotic replisome coordinates template unwinding and nascent-strand synthesis to
drive DNA replication fork progression and complete efficient genome duplication. During its …
drive DNA replication fork progression and complete efficient genome duplication. During its …