Results 51 to 60 of about 1,712,707 (295)

PCNA and XPF cooperate to distort DNA substrates [PDF]

open access: yes, 2009
XPF is a structure-specific endonuclease that preferentially cleaves 3' DNA flaps during a variety of repair processes. The crystal structure of a crenarchaeal XPF protein bound to a DNA duplex yielded insights into how XPF might recognise branched DNA ...
J. Carlos Penedo   +12 more
core   +1 more source

Single Cell Analysis of Human RAD18-Dependent DNA Post-Replication Repair by Alkaline Bromodeoxyuridine Comet Assay [PDF]

open access: yes, 2013
Damage to DNA can block replication progression resulting in gaps in the newly synthesized DNA. Cells utilize a number of post-replication repair (PRR) mechanisms such as the RAD18 controlled translesion synthesis or template switching to overcome the ...
Himabindu Gali   +14 more
core   +2 more sources

Analysis of the DNA damage response in living cells [PDF]

open access: yes, 2007
DNA lesions arising from environmental and endogenous sources induce various cellular responses including cell cycle arrest, DNA repair and apoptosis. Although detailed insights into the biochemical mechanisms and composition of DNA repair pathways have ...
Mortusewicz, Oliver
core   +1 more source

The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase. [PDF]

open access: yesPLoS ONE, 2016
DNA ligases are essential both to in vivo replication, repair and recombination processes, and in vitro molecular biology protocols. Prior characterization of DNA ligases through gel shift assays has shown the presence of a nick site to be essential for ...
Robert J Bauer   +2 more
doaj   +1 more source

Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy

open access: yesCell Division, 2007
Recent investigation of Cullin 4 (CUL4) has ushered this class of multiprotein ubiquitin E3 ligases to center stage as critical regulators of diverse processes including cell cycle regulation, developmental patterning, DNA replication, DNA damage and ...
Zhang Hui, Higa Leigh
doaj   +1 more source

Structural basis for nick recognition by a minimal pluripotent DNA ligase

open access: yes, 2007
Chlorella virus DNA ligase, the smallest eukaryotic ligase known, has pluripotent biological activity and an intrinsic nick-sensing function, despite having none of the accessory domains found in cellular ligases.
Nair, P.A.   +5 more
core   +1 more source

Allogeneic hematopoietic stem cell transplantation in two brothers with DNA ligase IV deficiency: a case report and review of the literature

open access: yesBMC Pediatrics, 2019
Background DNA ligase IV deficiency is a rare autosomal recessive disorder caused by hypomorphic mutations in the DNA ligase IV (LIG4) gene. DNA ligase IV is an essential protein for the development of a healthy immune system as well as for the ...
Sarah Schober   +10 more
doaj   +1 more source

Saccharomyces cerevisiae DNA ligase IV supports imprecise end joining independently of its catalytic activity. [PDF]

open access: yesPLoS Genetics, 2013
DNA ligase IV (Dnl4 in budding yeast) is a specialized ligase used in non-homologous end joining (NHEJ) of DNA double-strand breaks (DSBs). Although point and truncation mutations arise in the human ligase IV syndrome, the roles of Dnl4 in DSB repair ...
Kishore K Chiruvella   +4 more
doaj   +1 more source

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

open access: yesFEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

open access: yesFEBS Letters, EarlyView.
Proximity‐dependent labeling at the LAMTOR complex revealed the Rho GEF PLEKHG3 as a lysosome‐proximal protein directing the study toward the influence of lysosome positioning on actin dynamics and cell motility. We show that PLEKHG3 colocalizes with lysosomes at focal adhesion sites and observe that forced peripheral dispersion of lysosomes hinders ...
Rainer Ettelt   +8 more
wiley   +1 more source

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