Results 61 to 70 of about 6,151,611 (255)

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

FEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang, Naoki Sunagawa, Toma Kashima, Kiyohiko Igarashi, Akimasa Miyanaga, Shinya Fushinobu   +5 more
wiley   +1 more source

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

FEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Tagelda n Kuku d tqerrabin d lǧerrat tinmettiyin i d-teǧǧa

Revue d'Histoire Méditerranéenne
Deg umagrad-a, nemmeslay-d ɣef yiwet n tgelda i yesɛan azal meqqren deg umezruy atrar n Lezzayer s umata ladɣa amezruy n tmurt n Leqbayel, tagi d tageda n Kuku i d-ibanen deg useggas 1511, seld tuṭṭfa n temdint n Bgayet s ɣur Spenyul deg useggas 1510 ...
BENCHIKHE Ali
doaj  

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

FEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang, Grace Du, Charity Yongo‐Luwawa, Angelina Lu, Brett Kinrade, Kim Munro, Karl E. Klose, William D. Lubell, Peter Davies, Shuaiqi Guo   +9 more
wiley   +1 more source

Quantum-group-invariant D n + 1 2 $$ {D}_{n+1}^{(2)} $$ models: Bethe ansatz and finite-size spectrum

Journal of High Energy Physics
We consider the quantum integrable spin chain models associated with the Jimbo R-matrix based on the quantum affine algebra D n + 1 2 $$ {D}_{n+1}^{(2)} $$ , subject to quantum-group-invariant boundary conditions parameterized by two discrete variables p
Holger Frahm, Sascha Gehrmann, Rafael I. Nepomechie, Ana L. Retore   +3 more
doaj   +1 more source

7-Azido-N,N-diethyl-4,5-O-isopropylidene-4-C-methyl-3,6-anhydro-7-deoxy-d-glycero-d-manno-heptonamide

Acta Crystallographica Section E, 2009
The reaction of 5-azido-5-deoxy-2,3-O-isopropylidene-2-C-methyl-d-ribose with N,N-diethyl-2-(dimethylsulfuranylidene)acetamide gave the title compound, C15H26N4O5, as the major product arising from initial formation of an epoxide which was subsequently ...
David J. Watkin, George W. J. Fleet, Maria-Soledad Pino-González, Chen Wang, Sarah F. Jenkinson   +4 more
doaj   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

FEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Crystal structure of 4,4′-(4,10-diphenyl-4,10-dihydropyreno[4,5-d:9,10-d′]diimidazole-5,11-diyl)bis(N,N-diphenylaniline), C66H44N6

Zeitschrift für Kristallographie - New Crystal Structures, 2018
C66H44N6, triclinic, P1̄ (no. 2), a = 9.773(2) Å, b = 14.406(3) Å, c = 18.385(4) Å, α = 72.64(3)°, β = 82.10(3)°, γ = 76.90(3)°, V = 2399.5(8) Å3, Z = 2, Rgt(F) = 0.0546, wRref(F2) = 0.1559, T = 153(2) K.
Liu Yulong, Dong Zhaojia, Guo Youquan, Fu Ying   +3 more
doaj   +1 more source