Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase

Julian Ugonotti; Harry C. Tjondro; Rebeca Kawahara; Sayantani Chatterjee; Ian Loke; Siyun Chen; Fabian Soltermann; Hannes Hinneburg; Benjamin L. Parker; Vignesh Venkatakrishnan; Regis Dieckmann; Oliver C. Grant; Johan Bylund; Alison Rodger; Robert J. Woods; Anna Karlsson-Bengtsson; Weston B. Struwe; Morten Thaysen-Andersen

Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase

Julian Ugonotti, Harry C. Tjondro, Rebeca Kawahara, Sayantani Chatterjee, Ian Loke, Siyun Chen, Fabian Soltermann, Hannes Hinneburg, Benjamin L. Parker, Vignesh Venkatakrishnan, Regis Dieckmann, Oliver C. Grant, Johan Bylund, Alison Rodger, Robert J. Woods, Anna Karlsson-Bengtsson, Weston B. Struwe, Morten Thaysen-Andersen

Biomolecular Discovery Research Centre

Research output: Contribution to journal › Meeting abstract

Original language	English
Pages (from-to)	1120-1121
Number of pages	2
Journal	Glycobiology
Volume	30
Issue number	12
Publication status	Published - Dec 2020
Event	Annual Meeting of the Society for Glycobiology, 2020 - Phoenix, United States Duration: 9 Nov 2020 → 12 Nov 2020

Cite this

Ugonotti, J., Tjondro, H. C., Kawahara, R., Chatterjee, S., Loke, I., Chen, S., Soltermann, F., Hinneburg, H., Parker, B. L., Venkatakrishnan, V., Dieckmann, R., Grant, O. C., Bylund, J., Rodger, A., Woods, R. J., Karlsson-Bengtsson, A., Struwe, W. B., & Thaysen-Andersen, M. (2020). Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase. Glycobiology, 30(12), 1120-1121.

@article{f490a45ccf74440a94f7a3b8ecf77906,

title = "Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase",

author = "Julian Ugonotti and Tjondro, {Harry C.} and Rebeca Kawahara and Sayantani Chatterjee and Ian Loke and Siyun Chen and Fabian Soltermann and Hannes Hinneburg and Parker, {Benjamin L.} and Vignesh Venkatakrishnan and Regis Dieckmann and Grant, {Oliver C.} and Johan Bylund and Alison Rodger and Woods, {Robert J.} and Anna Karlsson-Bengtsson and Struwe, {Weston B.} and Morten Thaysen-Andersen",

year = "2020",

month = dec,

language = "English",

volume = "30",

pages = "1120--1121",

journal = "Glycobiology",

issn = "0959-6658",

publisher = "Oxford University Press",

number = "12",

note = "Annual Meeting of the Society for Glycobiology, 2020 ; Conference date: 09-11-2020 Through 12-11-2020",

}

Ugonotti, J, Tjondro, HC, Kawahara, R, Chatterjee, S, Loke, I, Chen, S, Soltermann, F, Hinneburg, H, Parker, BL, Venkatakrishnan, V, Dieckmann, R, Grant, OC, Bylund, J, Rodger, A, Woods, RJ, Karlsson-Bengtsson, A, Struwe, WB & Thaysen-Andersen, M 2020, 'Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase', Glycobiology, vol. 30, no. 12, pp. 1120-1121.

TY - JOUR

T1 - Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase

AU - Ugonotti, Julian

AU - Tjondro, Harry C.

AU - Kawahara, Rebeca

AU - Chatterjee, Sayantani

AU - Loke, Ian

AU - Chen, Siyun

AU - Soltermann, Fabian

AU - Hinneburg, Hannes

AU - Parker, Benjamin L.

AU - Venkatakrishnan, Vignesh

AU - Dieckmann, Regis

AU - Grant, Oliver C.

AU - Bylund, Johan

AU - Rodger, Alison

AU - Woods, Robert J.

AU - Karlsson-Bengtsson, Anna

AU - Struwe, Weston B.

AU - Thaysen-Andersen, Morten

PY - 2020/12

Y1 - 2020/12

UR - https://doi.org/10.1093/glycob/cwaa094

M3 - Meeting abstract

SN - 0959-6658

VL - 30

SP - 1120

EP - 1121

JO - Glycobiology

JF - Glycobiology

IS - 12

T2 - Annual Meeting of the Society for Glycobiology, 2020

Y2 - 9 November 2020 through 12 November 2020

ER -

Hyper-truncated n-acetyl-beta-d-glucosamine signatures augment the activity and inhibition potential of neutrophil granule myeloperoxidase

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