Bågenholm V - Search Results

1

A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans.

Reddy SK, Bågenholm V, Pudlo NA, Bouraoui H, Koropatkin NM, Martens EC, Stålbrand H. Reddy SK, et al. Among authors: bagenholm v. FEBS Lett. 2016 Jul;590(14):2106-18. doi: 10.1002/1873-3468.12250. Epub 2016 Jun 28. FEBS Lett. 2016. PMID: 27288925 Free PMC article.

2

Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A β-MANNANASE.

Bågenholm V, Reddy SK, Bouraoui H, Morrill J, Kulcinskaja E, Bahr CM, Aurelius O, Rogers T, Xiao Y, Logan DT, Martens EC, Koropatkin NM, Stålbrand H. Bågenholm V, et al. J Biol Chem. 2017 Jan 6;292(1):229-243. doi: 10.1074/jbc.M116.746438. Epub 2016 Nov 21. J Biol Chem. 2017. PMID: 27872187 Free PMC article.

3

A surface-exposed GH26 β-mannanase from Bacteroides ovatus: Structure, role, and phylogenetic analysis of BoMan26B.

Bågenholm V, Wiemann M, Reddy SK, Bhattacharya A, Rosengren A, Logan DT, Stålbrand H. Bågenholm V, et al. J Biol Chem. 2019 Jun 7;294(23):9100-9117. doi: 10.1074/jbc.RA118.007171. Epub 2019 Apr 18. J Biol Chem. 2019. PMID: 31000630 Free PMC article.

4

Backbone ¹H, ¹³C, and ¹⁵N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus.

Wernersson S, Bågenholm V, Persson C, Upadhyay SK, Stålbrand H, Akke M. Wernersson S, et al. Among authors: bagenholm v. Biomol NMR Assign. 2019 Apr;13(1):213-218. doi: 10.1007/s12104-019-09879-w. Epub 2019 Feb 7. Biomol NMR Assign. 2019. PMID: 30734154 Free PMC article.

5

The Crystal Structure of Thermotoga maritima Class III Ribonucleotide Reductase Lacks a Radical Cysteine Pre-Positioned in the Active Site.

Aurelius O, Johansson R, Bågenholm V, Lundin D, Tholander F, Balhuizen A, Beck T, Sahlin M, Sjöberg BM, Mulliez E, Logan DT. Aurelius O, et al. Among authors: bagenholm v. PLoS One. 2015 Jul 6;10(7):e0128199. doi: 10.1371/journal.pone.0128199. eCollection 2015. PLoS One. 2015. PMID: 26147435 Free PMC article.

6

Structure and ion-release mechanism of P_IB-4-type ATPases.

Grønberg C, Hu Q, Mahato DR, Longhin E, Salustros N, Duelli A, Lyu P, Bågenholm V, Eriksson J, Rao KU, Henderson DI, Meloni G, Andersson M, Croll T, Godaly G, Wang K, Gourdon P. Grønberg C, et al. Among authors: bagenholm v. Elife. 2021 Dec 24;10:e73124. doi: 10.7554/eLife.73124. Elife. 2021. PMID: 34951590 Free PMC article.

7

Transition metal transporting P-type ATPases: terminal metal-binding domains serve as sensors for autoinhibitory tails.

Hu Q, Sitsel O, Bågenholm V, Grønberg C, Lyu P, Pii Svane AS, Andersen KR, Laursen NS, Meloni G, Nissen P, Juhl DW, Nielsen JT, Nielsen NC, Gourdon P. Hu Q, et al. Among authors: bagenholm v. FEBS J. 2024 Nov 28. doi: 10.1111/febs.17330. Online ahead of print. FEBS J. 2024. PMID: 39609265

8

The structure and function of P5A-ATPases.

Li P, Bågenholm V, Hägglund P, Lindkvist-Petersson K, Wang K, Gourdon P. Li P, et al. Among authors: bagenholm v. Nat Commun. 2024 Nov 6;15(1):9605. doi: 10.1038/s41467-024-53757-6. Nat Commun. 2024. PMID: 39505844 Free PMC article.

9

Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases.

Guo Z, Orädd F, Bågenholm V, Grønberg C, Ma JF, Ott P, Wang Y, Andersson M, Pedersen PA, Wang K, Gourdon P. Guo Z, et al. Among authors: bagenholm v. Nat Commun. 2024 Mar 27;15(1):2690. doi: 10.1038/s41467-024-47001-4. Nat Commun. 2024. PMID: 38538615 Free PMC article.

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