The prion protein and its ligands: Insights into structure-function relationships

Mohsin Shafiq; Stefano Da Vela; Ladan Amin; Neelam Younas; David A Harris; Inga Zerr; Hermann C Altmeppen; Dmitri Svergun; Markus Glatzel

doi:10.1016/j.bbamcr.2022.119240

The prion protein and its ligands: Insights into structure-function relationships

Standard

The prion protein and its ligands: Insights into structure-function relationships. / Shafiq, Mohsin; Da Vela, Stefano; Amin, Ladan; Younas, Neelam; Harris, David A; Zerr, Inga; Altmeppen, Hermann C; Svergun, Dmitri; Glatzel, Markus.

In: BBA-MOL CELL RES, Vol. 1869, No. 6, 119240, 06.2022.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Shafiq, M, Da Vela, S, Amin, L, Younas, N, Harris, DA, Zerr, I, Altmeppen, HC, Svergun, D & Glatzel, M 2022, 'The prion protein and its ligands: Insights into structure-function relationships', BBA-MOL CELL RES, vol. 1869, no. 6, 119240. https://doi.org/10.1016/j.bbamcr.2022.119240

APA

Shafiq, M., Da Vela, S., Amin, L., Younas, N., Harris, D. A., Zerr, I., Altmeppen, H. C., Svergun, D., & Glatzel, M. (2022). The prion protein and its ligands: Insights into structure-function relationships. BBA-MOL CELL RES, 1869(6), [119240]. https://doi.org/10.1016/j.bbamcr.2022.119240

Vancouver

Shafiq M, Da Vela S, Amin L, Younas N, Harris DA, Zerr I et al. The prion protein and its ligands: Insights into structure-function relationships. BBA-MOL CELL RES. 2022 Jun;1869(6). 119240. https://doi.org/10.1016/j.bbamcr.2022.119240

Bibtex

@article{781371386b6141b6849be22237247628,

title = "The prion protein and its ligands: Insights into structure-function relationships",

abstract = "The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that lead to prion protein fragments some of which are membrane-bound whereas others are soluble. A multitude of ligands bind to the prion protein and besides proteinaceous binding partners, interaction with metal ions and nucleic acids occurs. Although of great importance, information on structural and functional consequences of prion protein binding to its partners is limited. Here, we will reflect on the structure-function relationship of the prion protein and its binding partners considering the different folding states and prion protein fragments.",

keywords = "Humans, Ligands, Prion Diseases, Prion Proteins/genetics, Prions, Structure-Activity Relationship",

author = "Mohsin Shafiq and {Da Vela}, Stefano and Ladan Amin and Neelam Younas and Harris, {David A} and Inga Zerr and Altmeppen, {Hermann C} and Dmitri Svergun and Markus Glatzel",

year = "2022",

month = jun,

doi = "10.1016/j.bbamcr.2022.119240",

language = "English",

volume = "1869",

journal = "BBA-MOL CELL RES",

issn = "0167-4889",

publisher = "Elsevier",

number = "6",

}

RIS

TY - JOUR

T1 - The prion protein and its ligands: Insights into structure-function relationships

AU - Shafiq, Mohsin

AU - Da Vela, Stefano

AU - Amin, Ladan

AU - Younas, Neelam

AU - Harris, David A

AU - Zerr, Inga

AU - Altmeppen, Hermann C

AU - Svergun, Dmitri

AU - Glatzel, Markus

PY - 2022/6

Y1 - 2022/6

N2 - The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that lead to prion protein fragments some of which are membrane-bound whereas others are soluble. A multitude of ligands bind to the prion protein and besides proteinaceous binding partners, interaction with metal ions and nucleic acids occurs. Although of great importance, information on structural and functional consequences of prion protein binding to its partners is limited. Here, we will reflect on the structure-function relationship of the prion protein and its binding partners considering the different folding states and prion protein fragments.

AB - The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that lead to prion protein fragments some of which are membrane-bound whereas others are soluble. A multitude of ligands bind to the prion protein and besides proteinaceous binding partners, interaction with metal ions and nucleic acids occurs. Although of great importance, information on structural and functional consequences of prion protein binding to its partners is limited. Here, we will reflect on the structure-function relationship of the prion protein and its binding partners considering the different folding states and prion protein fragments.

KW - Humans

KW - Ligands

KW - Prion Diseases

KW - Prion Proteins/genetics

KW - Prions

KW - Structure-Activity Relationship

U2 - 10.1016/j.bbamcr.2022.119240

DO - 10.1016/j.bbamcr.2022.119240

M3 - SCORING: Journal article

C2 - 35192891

VL - 1869

JO - BBA-MOL CELL RES

JF - BBA-MOL CELL RES

SN - 0167-4889

IS - 6

M1 - 119240

ER -