s alphafold protein structure database (Cowie)
86
Structured Review
Cowie
s alphafold protein structure database
S Alphafold Protein Structure Database, supplied by Cowie, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/s+alphafold+protein+structure+database/alphafold+database+protein+s+structure/pm42159598-460-61-48
Average 86 stars, based on 1 article reviews
S Alphafold Protein Structure Database, supplied by Cowie, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/s+alphafold+protein+structure+database/alphafold+database+protein+s+structure/pm42159598-460-61-48
Average 86 stars, based on 1 article reviews
s alphafold protein structure database - by Bioz Stars,
2026-09
86/100 stars
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other:Article Title: Viral Dark Matter: Illuminating Protein Function, Ecology, and Biotechnological Promises. Article Snippet: 2025, 53, Article Title: A Global Ligandability Map of Tryptoline Butynamide Stereoprobes Identifies Covalent Inhibitors of the Actin Maturation Protease. Article Snippet: Covalent chemistry coupled with activity-based protein profiling (ABPP) offers a versatile approach for smallmolecule ligand discovery in native biological contexts.. The covalent ligandability maps generated by ABPP that target cysteine have frequently leveraged the acrylamide as a reactive group due to its tempered electrophilicity and presence in many advanced tool compounds and therapeutics.. More recently, alternative cysteinedirected reactive groups such as the butynamide have emerged as an additional source of covalent probes and drugs, but their global reactivity with the proteome remains largely unexplored. Article Title: Bridging Simulation and Sustainability: Laccase Immobilization on Bio-Polymeric Hybrids for Degradation of 17α-Ethinylestradiol in Water Systems Article Snippet: 2023, 51 ( Article Title: Improving AlphaFold2 Performance in Virtual Screens Targeting GPCRs by Enhancing Binding-Site Conformational Sampling. Article Snippet: Science 2021, 373 (6557), 871−876. (6) Article Title: Biochemical Characterization and Substrate Specificity Mechanism of an Exolytic Hyaluronate Lyase SinHL from Streptococcus iniae QMA0131. Article Snippet: Hyaluronate lyases are widely used for the degradation of hyaluronic acid (HA) and preparation of HA oligosaccharides.. Herein, a putative PL8 hyaluronate lyase SinHL (128.3 kDa) from Streptococcus iniae QMA0131 was expressed in Escherichia coli and biochemically characterized.. SinHL is a strictly HA-specific and exolytic hyaluronate lyase that does not degrade CSs and can produce a desired low-molecular-weight HA from high-molecular-weight HA (HMW-HA, 1.52 × 106 Da) under controlled reaction times. Article Title: ProtCross: Bridging the PDB-AlphaFold Gap for Binding Site Prediction with Protein Point Clouds. Article Snippet: AlphaFold2 (AF2) has greatly increased the availability of predicted protein structures, but many binding-site prediction methods trained on experimentally determined Protein Data Bank (PDB) complexes perform less well when applied to AF2 models.. This loss of accuracy reflects differences between ligand-bound experimental structures and predominantly apo-like predicted models, as well as nonuniform local structural reliability indicated by pLDDT scores.. To address this, we introduce ProtCross, a confidence-aware domain adaptation framework for residue-level binding-site prediction on predicted protein structures. Article Title: Lessons from Structural Biology for Understanding Drug Resistance in Gastrointestinal Stromal Tumors (GIST). Article Snippet: Gastrointestinal stromal tumors (GISTs) are primarily driven by activating mutations in the receptor tyrosine kinases KIT or PDGFRA.. Targeted therapies have significantly improved patient outcomes; however, acquired drug resistance continues to limit long-term efficacy.. Secondary and tertiary mutations across distinct regions of the kinase domain affect the conformational equilibrium or directly disrupt drug binding by alteration of critical residues. Article Title: Characterizing the Conformational Dynamics of the Ribose Transporter B Protein in Escherichia coli : Enhanced Sampling via Multiple Force Fields. Article Snippet: 1983, 79, 926−935. (41) |