Results 51 to 60 of about 6,498,873 (334)
Evolutionary interplay between viruses and R‐loops
Viruses interact with specialized nucleic acid structures called R‐loops to influence host transcription, epigenetic states, latency, and immune evasion. This Perspective examines the roles of R‐loops in viral replication, integration, and silencing, and how viruses co‐opt or avoid these structures.
Zsolt Karányi+4 more
wiley +1 more source
Crystal structure of monomeric human β-2- microglobulin reveals clues to its amyloidogenic properties [PDF]
Dissociation of human β-2-microglobulin (β(2)m) from the heavy chain of the class I HLA complex is a critical first step in the formation of amyloid fibrils from this protein.
A. P. Kalverda+31 more
core +2 more sources
Disruption of SETD3‐mediated histidine‐73 methylation by the BWCFF‐associated β‐actin G74S mutation
The β‐actin G74S mutation causes altered interaction of actin with SETD3, reducing histidine‐73 methylation efficiency and forming two distinct actin variants. The variable ratio of these variants across cell types and developmental stages contributes to tissue‐specific phenotypical changes. This imbalance may impair actin dynamics and mechanosensitive
Anja Marquardt+8 more
wiley +1 more source
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Daggett, Valerie, van der Kamp, Marc W
core +1 more source
Purification tags markedly affect self‐aggregation of CPEB3
Although recombinant proteins are used to study protein aggregation in vitro, uncleaved tags can interfere with accurate interpretation. Our findings demonstrate that His₆‐GFP and His₁₂ tags significantly affect liquid droplet and amyloid fibril formation in the intrinsically disordered region (IDR) of mouse cytoplasmic polyadenylation element‐binding ...
Harunobu Saito+6 more
wiley +1 more source
Simple models of protein folding and of non--conventional drug design [PDF]
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learned how to extract this information to predict the three--dimensional, biologically active, native conformation of a protein ...
Abkkevich V I+25 more
core +1 more source
This study reveals how prime editing guide RNA (pegRNA) secondary structure and reverse transcriptase template length affect prime editing efficiency in correcting the phospholamban R14del cardiomyopathy‐associated mutation. Insights support the design of structurally optimized enhanced pegRNAs for precise gene therapy.
Bing Yao+7 more
wiley +1 more source
Single‐cell insights into the role of T cells in B‐cell malignancies
Single‐cell technologies have transformed our understanding of T cell–tumor cell interactions in B‐cell malignancies, revealing new T‐cell subsets, functional states, and immune evasion mechanisms. This Review synthesizes these findings, highlighting the roles of T cells in pathogenesis, progression, and therapy response, and underscoring their ...
Laura Llaó‐Cid
wiley +1 more source
On the optimal contact potential of proteins
We analytically derive the lower bound of the total conformational energy of a protein structure by assuming that the total conformational energy is well approximated by the sum of sequence-dependent pairwise contact energies.
Akira R. Kinjo+32 more
core +1 more source
Reading the three-dimensional structure of a protein from its amino acid sequence
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learnt how to extract this information so as to predict the detailed, biological active, three-dimensional structure of a protein ...
Broglia, R. A., Tiana, G.
core +1 more source