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Details on Person Structural basis of antimicrobial membrane coat assembly by human GBP1

Class:IdLiteratureReference:9947892
_displayNameStructural basis of antimicrobial membrane coat assembly by human GBP1
_timestamp2025-05-14 12:50:39
author[Person:9947925] Kuhm, Tanja
[Person:9947882] Taisne, Clémence
[Person:9947941] de Agrela Pinto, Cecilia
[Person:9947895] Gross, Luca
[Person:9947840] Giannopoulou, Evdokia A
[Person:9947939] Huber, Stefan T
[Person:9941075] Pardon, Els
[Person:9941356] Steyaert, Jan
[Person:9947848] Tans, Sander J
[Person:9947881] Jakobi, Arjen J
created[InstanceEdit:9947847] Shamovsky, Veronica, 2025-05-14
journalNat Struct Mol Biol
pages172-184
pubMedIdentifier39394410
titleStructural basis of antimicrobial membrane coat assembly by human GBP1
volume32
year2025
(literatureReference)[Polymerisation:9947842] GBP1 hydrolyzes GTP forming GBP1 oligomers [Homo sapiens]
[Reaction:9947932] GBP1:GTP binds LPS on the bacterial surface [Homo sapiens]
[Pathway:9953170] GBP-mediated host defense [Homo sapiens]
[Reaction:9968553] GBP1 binds GTP [Homo sapiens]
[Summation:9947871] Guanylate-binding protein 1 (GBP1) localizes to the lipopoly...
[Summation:9947897] Guanylate-binding protein 1 (GBP1) membrane binding, dimer f...
[Summation:9948004] Guanylate-binding protein 1 (GBP1) is farnesylated at cystei...
[Summation:9962134] The human Guanylate Binding Proteins (GBPs) constitute a fam...
[Summation:9962589] Interferon (IFN)-inducible dynamin-like GTPases, including m...
[Summation:9968552] In its inactive nucleotide-free state, guanylate-binding pro...
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