Results 91 to 100 of about 31,898 (266)

Nucleic Acid Therapeutics for “Undruggable” Cancer Targets: Mechanisms, Challenges, and Prospects

open access: yesAdvanced Science, EarlyView.
Nucleic acid therapeutics bypass the structural limitations of conventional drugs by targeting mRNA rather than proteins. This review examines how antisense oligonucleotides, siRNAs, miRNAs, aptamers, and mRNA vaccines intervene against historically undruggable oncoproteins including Ras, MYC, and p53, highlighting mechanistic advances, delivery ...
Feng Xu   +6 more
wiley   +1 more source

Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75

open access: yes, 2011
Histone acetylation and nucleosome remodeling regulate DNA damage repair, replication and transcription. Rtt109, a recently discovered histone acetyltransferase (HAT) from Saccharomyces cerevisiae, functions with the histone chaperone Asf1 to acetylate ...
Keck, James G.   +7 more
core   +1 more source

Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies

open access: yesAdvanced Science, EarlyView.
In this review, an integrated conceptual framework linking HSP90's molecular chaperone functions to its pathological roles in cancer is proposed. HSP90 serves as a central node that integrates oncogenic signaling, buffers proteotoxic stress, maintains cancer stem cell plasticity, and shapes tumor‐immune interactions, all of which converge to drive ...
Beibei Zhang   +4 more
wiley   +1 more source

In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP

open access: yesBiochemistry Research International, 2011
Nucleolin is a major nucleolar protein involved in various aspects of ribosome biogenesis such as regulation of polymerase I transcription, pre-RNA maturation, and ribosome assembly.
Xavier Gaume   +4 more
doaj   +1 more source

H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation

open access: yesNature Communications, 2023
Here the authors investigated the direct collaboration between ubiquitinated histone H2B (ubH2B) with FACT at the nucleosome level. They found ubH2B enhances FACT’s chaperone property, recruits FACT to form a stable altered nucleosome state, and provides
Anfeng Luo   +10 more
doaj   +1 more source

Enhanced ESC phenotype by histone variant and chaperone mutations.

open access: yes, 2016
Enhanced ESC phenotype by histone variant and chaperone mutations.
Devendran A. Sadasivam (2541448)   +1 more
core   +1 more source

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function

open access: yesAdvanced Science, EarlyView.
Ubiquilin (UBQLN), like many other human proteins, contains both well‐folded and disordered regions. Here, we show that intramolecular interactions between disordered regions and folded domains modulate between open and closed topologies of UBQLN proteins, altering their structure and function.
Jessica K. Niblo   +4 more
wiley   +1 more source

High-resolution visualization of H3 variants during replication reveals their controlled recycling

open access: yesNature Communications, 2018
Epigenetic modifications are a key contributor to cell identity, and their propagation is crucial for proper development. Here the authors use a super-resolution microscopy approach to reveal how histone variants are faithfully transmitted during genome ...
Camille Clément   +10 more
doaj   +1 more source

PRMT9 Aggravated Dopaminergic Neurodegeneration in Parkinson's Disease Model by Facilitating the Degradation of DUSP26 and Inducing Mitochondrial Dysfunction

open access: yesAdvanced Science, EarlyView.
In the pathological state of PD induced by MPP+, the upregulated PRMT9 in dopaminergic neurons translocates into mitochondrion and interacts with DUSP26 and catalyzes its arginine methylation, leading to the ubiquitin‐proteasomal degradation of DUSP26 mediated by Trim32.
Tengfei Liu   +13 more
wiley   +1 more source

Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46

open access: yesStructure, 2008
RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. We report here the crystal structure of human RbAp46 bound to histone H4.
Murzina, Natalia V.   +10 more
openaire   +2 more sources

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