Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 Å Resolution.

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Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 Å Resolution. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/CBIC.201700220
P8608Fatcat IDrelease_5attasks6zdc5o5jjcjl7rbts4
P698PubMed publication ID28489325

P50authorWolfram SaengerQ100392
Stefanie WedepohlQ38799454
Jens DerneddeQ56954435
P2093author name stringArdeschir Vahedi-Faridi
Rudolf Tauber
Haydar Bulut
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Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domainsQ27729350
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Glycosylation-directed quality control of protein foldingQ38606832
Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to Stabilize the High Affinity State under Force.Q39067711
Glycoprotein structural genomics: solving the glycosylation problemQ40159897
Lectins on a roll: the structure of E-selectin.Q40391868
Single-Step Purification of Monomeric l-Selectin via Aptamer Affinity ChromatographyQ42318600
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P433issue13
P304page(s)1338-1345
P577publication date2017-06-06
P1433published inChemBioChemQ634395
P1476titleReducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 Å Resolution
P478volume18

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Q49898832A head-to-tail view of L-selectin and its impact on neutrophil behaviourcites workP2860

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