Results 191 to 200 of about 150,813 (294)

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

open access: yesThe 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   +11 more
wiley   +1 more source

How I Treat Tumor Lysis Syndrome.

open access: yesClin J Am Soc Nephrol, 2023
Joseph A, Zafrani L.
europepmc   +1 more source

Regulation of PHOX2B gene expression by the long non‐coding natural antisense RNA PHOX2B‐AS1

open access: yesThe FEBS Journal, EarlyView.
PHOX2B is a transcription factor essential for autonomic nervous system development. We identify and characterize PHOX2B‐AS1, a human long non‐coding antisense transcript at the PHOX2B locus, along with its murine counterpart. Our findings reveal bidirectional transcription and reciprocal regulation: PHOX2B activates PHOX2B‐AS1, whereas PHOX2B‐AS1 ...
Simona Di Lascio   +12 more
wiley   +1 more source

Successful Management of Tumor Lysis Syndrome Following Enfortumab Vedotin Plus Pembrolizumab Therapy in Metastatic Urothelial Carcinoma: A Case Report. [PDF]

open access: yesIJU Case Rep
Takemori D   +15 more
europepmc   +1 more source

Current perspectives on KMT2A fusion proteins and menin inhibition in paediatric acute myeloid leukaemia

open access: yesThe FEBS Journal, EarlyView.
Genetic rearrangements resulting in the expression of KMT2A fusion alleles can lead to dramatic transcriptional disturbances that contribute to the onset of acute leukaemias. Fortunately, menin inhibition has emerged as a promising new class of targeted therapy.
Lydia Elaine Roets   +2 more
wiley   +1 more source

Human IDO2 exhibits unique binding affinities distinct to those of human IDO1

open access: yesThe FEBS Journal, EarlyView.
Although indoleamine 2,3‐dioxygenase 2 (IDO2) is highly homologous to IDO1, it displays markedly lower catalytic activity. We found that IDO2 binds L‐tryptophan (L‐Trp) in a flipped orientation stabilized by the IDO2‐specific residue His143. Replacement of His143 with the IDO1‐equivalent tyrosine restored an IDO1‐like binding mode and increased ...
Shunsuke Nogi   +8 more
wiley   +1 more source

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