De novo GTP biosynthesis is critical for virulence of the fungal pathogen Cryptococcus neoformans.

Autor: Carl A Morrow, Eugene Valkov, Anna Stamp, Eve W L Chow, I Russel Lee, Ania Wronski, Simon J Williams, Justine M Hill, Julianne T Djordjevic, Ulrike Kappler, Bostjan Kobe, James A Fraser

Publikováno v: PLoS Pathogens, Vol 8, Iss 10, p e1002957 (2012)

We have investigated the potential of the GTP synthesis pathways as chemotherapeutic targets in the human pathogen Cryptococcus neoformans, a common cause of fatal fungal meningoencephalitis. We find that de novo GTP biosynthesis, but not the alterna

Externí odkaz: https://doaj.org/article/33cc5f6ca2e241689d79d1cbab96ad8a

NMR structure of μ-conotoxin GIIIC : leucine 18 induces local repacking of the N-terminus resulting in reduced NaV channel potency

Autor: David J. Adams, Rocio K. Finol-Urdaneta, David J. Craik, Justine M. Hill, Jeffrey R. McArthur, Peta J. Harvey, Dorien Van Lysebetten, Thomas Durek, Thomas S. Dash, Nyoman D. Kurniawan

Publikováno v: MOLECULES
Molecules, Vol 23, Iss 10, p 2715 (2018)
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules
Volume 23
Issue 10

&mu
Conotoxins are potent and highly specific peptide blockers of voltage-gated sodium channels. In this study, the solution structure of &mu
conotoxin GIIIC was determined using 2D NMR spectroscopy and simulated annealing calculations. Des

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0fed3bc49dd832d4b3edda0afb5b305
https://biblio.ugent.be/publication/8601313/file/8601315

The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized

Autor: Kate Schroder, Gautier Robin, Justine M. Hill, Parimala R. Vajjhala, Stuart Kellie, Jennifer L. Martin, Bostjan Kobe, Kai-En Chen, Linda H.L. Lua, Matthew J. Sweet, Tom T. Caradoc-Davies, Ayanthi A. Richards

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 69:774-784

The caspase recruitment domain (CARD) is present in death-domain superfamily proteins involved in inflammation and apoptosis. BinCARD is named for its ability to interact with Bcl10 and inhibit downstream signalling. Human BinCARD is expressed as two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5be5590e38cc5113dd1825ff6859ea66
https://doi.org/10.1107/s0907444913001558

NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1

Autor: Justine M. Hill, Joshua S. Mylne, Caroline Mas

Publikováno v: Biomolecular NMR Assignments. 6:5-8

VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39 kDa prote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a90f41bfad558b17be8778d2a28abb3
https://doi.org/10.1007/s12104-011-9313-6

Structure and Dynamics of ASC2, a Pyrin Domain-only Protein That Regulates Inflammatory Signaling

Autor: Justine M. Hill, Ranajeet Ghose, Aswin Natarajan

Publikováno v: Journal of Biological Chemistry. 281:31863-31875

Pyrin domain (PYD)-containing proteins are key components of pathways that regulate inflammation, apoptosis, and cytokine processing. Their importance is further evidenced by the consequences of mutations in these proteins that give rise to autoimmun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89376d295866b3060dc6fc4dfbabc0be
https://doi.org/10.1016/s0021-9258(19)84101-7