Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Details on Person Guanylate-binding protein 1 (GBP1) catalyzes a two-step GTP ...

Class:Id	Summation:9953142
_displayName	Guanylate-binding protein 1 (GBP1) catalyzes a two-step GTP ...
_timestamp	2025-08-01 05:19:27
created	[InstanceEdit:9953148] Shamovsky, Veronica, 2025-05-28
literatureReference	[LiteratureReference:9947890] Structural insights into the activation mechanism of antimicrobial GBP1 [LiteratureReference:9947931] How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP [LiteratureReference:9953141] The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP [LiteratureReference:9947914] Catalytic activity of human guanylate-binding protein 1 coupled to the release of structural restraints imposed by the C-terminal domain [LiteratureReference:9947878] The Molecular Mechanism of Polymer Formation of Farnesylated Human Guanylate-binding Protein 1 [LiteratureReference:9953145] hGBP1 Coordinates Chlamydia Restriction and Inflammasome Activation through Sequential GTP Hydrolysis [LiteratureReference:9953136] Insight into temperature dependence of GTPase activity in human guanylate binding protein-1 [LiteratureReference:9953147] Transient kinetic investigation of GTP hydrolysis catalyzed by interferon-gamma-induced hGBP1 (human guanylate binding protein 1) [LiteratureReference:9947909] Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions [LiteratureReference:9948009] Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms [LiteratureReference:9947948] Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria [LiteratureReference:9947832] Structural requirements for membrane binding of human guanylate-binding protein 1
modified	[InstanceEdit:9954263] Shamovsky, Veronica, 2025-06-06 [InstanceEdit:9962142] Shamovsky, Veronica, 2025-08-01
text	Guanylate-binding protein 1 (GBP1) catalyzes a two-step GTP hydrolysis reaction, initially converting GTP to GDP, followed by a second hydrolysis of GDP to GMP. This sequential mechanism is facilitated by conformational repositioning of the nucleotide within the catalytic pocket after the first cleavage event (Ghosh et al., 2006; Schwemmle & Staeheli, 1994; Ince et al., 2021; Weismehl M et al., 2024). GTP hydrolysis to GDP promotes GBP1 association with pathogen-containing membranes and drives its self-assembly into higher-order oligomers, that compromise microbial membrane integrity (Sistemich et al., 2020, 2021; Kutsch M et al., 2020) or facilitate lytic cell death via pyroptosis (Santos JC et al., 2020; Wandel MP et al., 2020). The subsequent conversion of GDP to GMP by GBP1 leads to metabolic production of uric acid, a potential trigger of NLRP3 inflammasome under certain cellular conditions (Xavier et al., 2020). Kinetic and thermodynamic studies suggest that the balance between GDP and GMP production by GBP1, along with nucleotide dissociation dynamics, regulates GBP1’s shift from direct antimicrobial defense to pro-inflammatory signaling (Kunzelmann S et al., 2006; Rani A et al., 2012).
(summation)	[Reaction:9947887] GBP1 hydrolyzes GDP [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by Guanylate-binding protein 1 (GBP1) catalyzes a two-step GTP ... (9953142)