Results 151 to 160 of about 39,475 (232)

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

A Hanks‐type bacterial kinase, PknS, directly phosphorylates the alternative sigma factor EcfK to promote resistance to protist predation

The FEBS Journal, EarlyView.
The Xanthomonas citri Hanks‐type kinase PknS autophosphorylates and directly phosphorylates the alternative sigma factor EcfK at five residues. Besides the conserved residue T51 in the σ2 domain, phosphorylation of a residue in the linker between σ2 and σ4 is critical for EcfK activation by promoting its interaction with a positively charged pocket in ...
Lídia dos Passos Lima, Dev Sriranganadane, Daiane Laise da Silva, Natália C. Drebes Dörr, Enzo Breviglieri Sichi Mello, Caio Vinicius dos Reis, Rogério Ferreira Lourenço, José Felipe Teixeira da Silva Santos, Anita Salmazo, Brenno Wendler Miranda, Katlin B. Massirer, Rafael M. Couñago, Cristina E. Alvarez‐Martinez   +12 more
wiley   +1 more source

Characterisation of a phylogenetically distinct PL25 family ulvan lyase from a seaweed biomass enriched metagenome

The FEBS Journal, EarlyView.
Ulvan is a polysaccharide available from green seaweed with beneficial properties for various applications. The full potential of ulvan requires enzymatic degradation of the polymer, thus producing ulvan oligosaccharides. This study expands the armoury of characterised ulvan lyases.
Andrius Jasilionis, Pavithra Sivakumar, Justyna M. Dobruchowska, Sune Fjermedal, Hörður Guðmundsson, Bjorn Thor Adalsteinsson, Guðmundur Ó. Hreggviðsson, Anne S. Meyer, Eva Nordberg Karlsson   +8 more
wiley   +1 more source

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

The 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, Ayumu Takahashi, So Murakami, Nami Adachi, Tina Fujimoto, Yohta Fukuda, Taku Yamashita, Tsuyoshi Inoue, Hirofumi Tsujino   +8 more
wiley   +1 more source

Insights into the catalytic mechanism of formate dehydrogenases from different microbial sources

The FEBS Journal, EarlyView.
This integrated study combines experimental enzyme kinetics with QM/MM simulations to map the catalytic mechanisms of four formate dehydrogenases at the atomic level. This approach reveals the key determinants of catalytic efficiency and guides the rational design of biocatalysts for effective CO2 reduction—a crucial step towards sustainable ...
Laura Legnani, Marco Gargiulo, Elia Lio, Enrico Mario Alessandro Fassi, Giovanni Grazioso, Maria Assunta Chiacchio, Barış Binay, Stefania Brocca, Francesco Secundo   +8 more
wiley   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

The FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy, Zsolt Fazekas, Nóra Wágner, Anna J. Kiss‐Szemán, Veronika Harmat, Zoltán Pozsonyi, Dóra K. Menyhárd, András Perczel   +7 more
wiley   +1 more source

KU80 suppresses endonuclease G activity to preserve genomic integrity

The FEBS Journal, EarlyView.
Under normal conditions, EndoG remains restricted to mitochondria and the genome remains intact. When KU80 is absent, EndoG translocates into the nucleus, where it promotes DNA fragmentation and genomic instability. Thus, this work highlights the importance of KU80 in tightly controlling EndoG localization to preserve genome stability.
Jargalan Batsaikhan, Kwang‐Hyun Park, Hae Ryung Chang, Eunyoung Jung, Myung‐Jin Kim, Jeeyoon Kang, Hyunjo Shim, Eui‐Jeon Woo, Yonghwan Kim   +8 more
wiley   +1 more source

Genetic dissection reveals distinct contributions of the eS31 N‐terminal domain to translational accuracy in Saccharomyces cerevisiae

The FEBS Journal, EarlyView.
The eukaryote‐specific N‐terminal domain (NTD) of eS31 uses two distinct strategies to maintain translation fidelity. During elongation, a positively charged “hotspot” fine‐tunes the selection of incoming aa‐tRNA. During termination, the entire NTD acts as a structural scaffold to ensure the correct positioning of the release factor eRF1.
Qingxuan Gao, Hiroshi Otsuka, Kei Endo, Koichi Ito   +3 more
wiley   +1 more source

Tyrosine residues at the substrate binding site in human NQO1 homodimer: Protein conformational dynamics and optimization of substrate binding geometry

The FEBS Journal, EarlyView.
Human NAD(P)H:quinone oxidoreductase 1 is a homodimeric flavoenzyme crucial for redox metabolism and linked to significant health issues. Point mutations at Tyr126 and Tyr128 demonstrate their essential roles in optimizing substrate binding geometry for catalysis, as well as in half‐site reactivity and conformational dynamics during the enzyme's ...
Maribel Rivero, Juan Luis Pacheco‐Garcia, Pavla Vankova, Dmitry Loginov, Isabel Quereda‐Moraleda, Jose Manuel Martin‐Garcia, Petr Man, Angel Luis Pey, Milagros Medina   +8 more
wiley   +1 more source

CОNSERVATION LAWSOF THE NONLINEAR SCHRODINGER EQUATION

Вестник Башкирского университета, 2023
Е. R. Shaihiev, R. D. Murtazina, A. D. Nezamova, N. A. Sidel’nikova, G. K. Galina   +4 more
openaire   +1 more source