Results 171 to 180 of about 101,653 (280)

A highly abundant circular RNA from the RMST locus plays a role in posterior fossa ependymoma pathogenesis

Brain Pathology, EarlyView.
circRMST (hsa_circ_0099634) is by far the most abundant isoform from the RMST locus. It is highly expressed in cancer cells throughout ependymoma patient samples and is located in the cytoplasm. circRMST knockdown causes cell cycle arrest and induces differentiation, and it is a marker for poor prognosis. The figure is made using BioRender.
Ulvi Ahmadov, Charlotte W. Udengaard, Stine M. Vissing, Silke D. Nielsen, Kim‐Gwendolyn Dietrich, Benedicte Parm Ulhøi, Lasse S. Kristensen   +6 more
wiley   +1 more source

Prophylactic heminephrectomy for an asymptomatic, non-functioning moiety in pediatric duplex systems: is cancer prevention justified? [PDF]

Front Pediatr
Zhanghuang C, Long N, Yan B.
europepmc   +1 more source

Investigating the molecular mechanisms underlying the anti‐CRISPR function of AcrIIA13b protein

The FEBS Journal, EarlyView.
Anti‐CRISPR protein AcrIIA13b inhibits CRISPR–Cas9 function by preventing target DNA engagement. The Cas9–sgRNA ribonucleoprotein (RNP) normally recognizes the protospacer adjacent motif (PAM) duplex to initiate DNA cleavage. AcrIIA13b binding to the PAM‐interacting WED–PI domain blocks this recognition, leaving the target DNA intact.
So Yeon Lee, Hyun Ho Park
wiley   +1 more source

Chemical and photoinduced interstrand crosslinking of oligo DNA duplexes containing 2'-deoxythioguanosines. [PDF]

Commun Chem
Osman JA, Onizuka K, Yamano Y, Nagatsugi F.   +3 more
europepmc   +1 more source

SARS‐CoV‐2 nucleocapsid protein variants have differential RNA chaperone activity

The FEBS Journal, EarlyView.
The SARS‐CoV‐2 nucleocapsid (N) protein facilitates RNA annealing through its RBD–IDR2–CTD region, identifying it as a functional RNA chaperone. The Omicron BA.5 variant shows reduced chaperone activity compared to the Wuhan wild‐type protein. Although phosphorylation has no effect on wild‐type N, phosphomimetic modification of BA.5 N restores its RNA ...
Sabrina Babl, Julia M. Seidel, Fabian Kugler, Elisabeth Silberhorn, Anna Ludwig, Jonas Abel, Sophia Winklbauer, Niklas Schaub, Silvia Materna‐Reichelt, Kamran Honarnejad, Nataša Stojanović Gužvić, Gernot Längst   +11 more
wiley   +1 more source

An antibody uniquely binding short 2'-O-methyl RNA oligonucleotide duplexes: formation and recognition of target duplexes on cell surfaces. [PDF]

Front Immunol
Dunn IS, Lawler MM, Fagundes L, Simoes Junior M, Mangold A, Rinaldi D, Rose LB, Kurnick JT.   +7 more
europepmc   +1 more source

RNF13 is a previously undescribed interactor of iduronate 2‐sulfatase that modifies its glycosylation and maturation

The FEBS Journal, EarlyView.
Iduronate 2‐sulfatase (IDS; purple) is expressed as a precursor protein that goes through multiple steps of maturation, modification, and trafficking to become an active lysosomal enzyme that degrades glycosaminoglycans. Our study shows that the transmembrane ubiquitin ligases RNF13 (orange) and RNF167 (pink) heterodimerize, affecting IDS intracellular
Valérie C. Cabana, Antoine Y. Bouchard, Audrey M. Sénécal, Laurent Cappadocia, Marc P. Lussier   +4 more
wiley   +1 more source

Zinc-finger transcription factor Fzf1 binds to its target DNA in a non-canonical manner. [PDF]

Nucleic Acids Res
Ma C, Du Y, Xiao W, Moore SA.
europepmc   +1 more source

Degradomics for large‐scale mechanistic insights on proteases and proteolysis in human health

The FEBS Journal, EarlyView.
Proteolysis has an important role in human disease but remains relatively unexplored. Degradomics, the uncovering of proteolysis in tissues, cells, and proteins, uses mass spectrometry‐based terminomics to identify protein termini occurring therein (forward degradomics) and to define the actions of proteases (reverse degradomics).
Daniel R. Martin, Sumit Bhutada, Suneel S. Apte   +2 more
wiley   +1 more source

Tho1 and MOS11 promote nucleic acid double-strand unwinding by facilitating DEAD-box helicase oligomerization. [PDF]

Nucleic Acids Res
Becker F, Miosga MB, Mannan M, Bettenworth V, Steinchen W, Sträßer K, Friedhoff P.   +6 more
europepmc   +1 more source