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Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse.
- Published in:
- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-32577-6
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- Article
Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.
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- Nucleic Acids Research, 2014, v. 42, n. 8, p. 5151
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- Article
A highly active S1‐P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c‐di‐GMP.
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- FEBS Letters, 2023, v. 597, n. 16, p. 2103, doi. 10.1002/1873-3468.14683
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- Article
The first structure–function study of GH151 α‐l‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity.
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- FEBS Journal, 2022, v. 289, n. 16, p. 4998, doi. 10.1111/febs.16387
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- Article
Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
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- Scientific Reports, 2019, v. 9, n. 1, p. N.PAG, doi. 10.1038/s41598-019-50105-3
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- Article
Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non–Specificity, and Inhibition.
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- PLoS ONE, 2016, v. 11, n. 12, p. 1, doi. 10.1371/journal.pone.0168832
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- Article
Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase.
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- FEBS Letters, 2019, v. 593, n. 9, p. 996, doi. 10.1002/1873-3468.13385
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- Article
Active site complementation and hexameric arrangement in the GH family 29; a structure–function study of α-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus.
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- Glycobiology, 2019, v. 29, n. 1, p. 59, doi. 10.1093/glycob/cwy078
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- Article