Understanding HAIs: Ally proteins in the fight against cancer

Publikation: Bidrag til tidsskriftKommentar/debatForskningfagfællebedømt

Standard

Understanding HAIs : Ally proteins in the fight against cancer. / Nonboe, Annika W.; Bald, Zuzanna H.; Vogel, Lotte K.

I: FEBS Journal, Bind 289, Nr. 12, 2022, s. 3416-3418.

Publikation: Bidrag til tidsskriftKommentar/debatForskningfagfællebedømt

Harvard

Nonboe, AW, Bald, ZH & Vogel, LK 2022, 'Understanding HAIs: Ally proteins in the fight against cancer', FEBS Journal, bind 289, nr. 12, s. 3416-3418. https://doi.org/10.1111/febs.16399

APA

Nonboe, A. W., Bald, Z. H., & Vogel, L. K. (2022). Understanding HAIs: Ally proteins in the fight against cancer. FEBS Journal, 289(12), 3416-3418. https://doi.org/10.1111/febs.16399

Vancouver

Nonboe AW, Bald ZH, Vogel LK. Understanding HAIs: Ally proteins in the fight against cancer. FEBS Journal. 2022;289(12):3416-3418. https://doi.org/10.1111/febs.16399

Author

Nonboe, Annika W. ; Bald, Zuzanna H. ; Vogel, Lotte K. / Understanding HAIs : Ally proteins in the fight against cancer. I: FEBS Journal. 2022 ; Bind 289, Nr. 12. s. 3416-3418.

Bibtex

@article{f78ec3f6011042248b88d8f2c217c350,
title = "Understanding HAIs: Ally proteins in the fight against cancer",
abstract = "Understanding how HAI-1 and HAI-2 regulate the epithelial serine protease matriptase may hold the key to curing epithelial-derived cancer. HAIs are serine protease inhibitors that inhibit matriptase and have a poorly understood effect on the presence of matriptase protein in cells. In this issue of The FEBS Journal, Yamashita et al. provide much-needed new insights into this effect, describing it as a {\textquoteleft}chaperone-like function{\textquoteright} of HAI-1. However, several observations suggest that matriptase folds correctly without HAIs and that HAIs are not chaperones. We introduce the concept of {\textquoteleft}ally proteins{\textquoteright} to categorize the poorly understood function of HAIs, distinguishing them from chaperones. Comment on: https://doi.org/10.1111/febs.16348.",
keywords = "ally protein, cancer, chaperone, HAI-1, HAI-2, malignant tumour, matriptase",
author = "Nonboe, {Annika W.} and Bald, {Zuzanna H.} and Vogel, {Lotte K.}",
note = "Publisher Copyright: {\textcopyright} 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies",
year = "2022",
doi = "10.1111/febs.16399",
language = "English",
volume = "289",
pages = "3416--3418",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Springer Verlag",
number = "12",

}

RIS

TY - JOUR

T1 - Understanding HAIs

T2 - Ally proteins in the fight against cancer

AU - Nonboe, Annika W.

AU - Bald, Zuzanna H.

AU - Vogel, Lotte K.

N1 - Publisher Copyright: © 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies

PY - 2022

Y1 - 2022

N2 - Understanding how HAI-1 and HAI-2 regulate the epithelial serine protease matriptase may hold the key to curing epithelial-derived cancer. HAIs are serine protease inhibitors that inhibit matriptase and have a poorly understood effect on the presence of matriptase protein in cells. In this issue of The FEBS Journal, Yamashita et al. provide much-needed new insights into this effect, describing it as a ‘chaperone-like function’ of HAI-1. However, several observations suggest that matriptase folds correctly without HAIs and that HAIs are not chaperones. We introduce the concept of ‘ally proteins’ to categorize the poorly understood function of HAIs, distinguishing them from chaperones. Comment on: https://doi.org/10.1111/febs.16348.

AB - Understanding how HAI-1 and HAI-2 regulate the epithelial serine protease matriptase may hold the key to curing epithelial-derived cancer. HAIs are serine protease inhibitors that inhibit matriptase and have a poorly understood effect on the presence of matriptase protein in cells. In this issue of The FEBS Journal, Yamashita et al. provide much-needed new insights into this effect, describing it as a ‘chaperone-like function’ of HAI-1. However, several observations suggest that matriptase folds correctly without HAIs and that HAIs are not chaperones. We introduce the concept of ‘ally proteins’ to categorize the poorly understood function of HAIs, distinguishing them from chaperones. Comment on: https://doi.org/10.1111/febs.16348.

KW - ally protein

KW - cancer

KW - chaperone

KW - HAI-1

KW - HAI-2

KW - malignant tumour

KW - matriptase

U2 - 10.1111/febs.16399

DO - 10.1111/febs.16399

M3 - Comment/debate

C2 - 35220685

AN - SCOPUS:85125421867

VL - 289

SP - 3416

EP - 3418

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 12

ER -

ID: 299491760