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Profil bibliographique

Pernille Seiffert

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

11Publications signalées
153Citations signalées
1Affiliations récentes

Les institutions déclarées

Les domaines associés

Cytokine Signaling Pathways and InteractionsGrowth Hormone and Insulin-like Growth FactorsT-cell and B-cell ImmunologyProtein Kinase Regulation and GTPase SignalingImmune Cell Function and Interaction

Les publications récentes

Accès ouvert 2023 article OpenAlex

The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate

Raul R. Araya-Secchi, Katrine Bugge, Pernille Seiffert, Amalie Petry et autres

Class 1 cytokine receptors transmit signals through the membrane by a single transmembrane helix to an intrinsically disordered cytoplasmic domain that lacks kinase activity. While specific binding to phosphoinositides has been reported for the prolactin receptor (PRLR), the role of lipids in …

dk, cl (code pays fourni par la source)

24 citations eLife
Accès ouvert 2023 article OpenAlex

Tyrosine kinases compete for growth hormone receptor binding and regulate receptor mobility and degradation

Yash Chhabra, Pernille Seiffert, Rachel S. Gormal, Manon Vullings et autres

Growth hormone (GH) acts via JAK2 and LYN to regulate growth, metabolism, and neural function. However, the relationship between these tyrosine kinases remains enigmatic. Through an interdisciplinary approach combining cell biology, structural biology, computation, and single-particle tracking on live cells, we find …

us, au, dk (code pays fourni par la source)

16 citations Cell Reports
Accès ouvert 2023 peer-review OpenAlex

Author response: The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate

Raul R. Araya-Secchi, Katrine Bugge, Pernille Seiffert, Amalie Petry et autres

The prolactin receptor, Janus kinase 2, and PI(4,5)P2 form a co-structure with the membrane resulting in orientations with different accessibility fixing the disordered juxtamembrane domain of the receptor in an extended structure.

dk, cl (code pays fourni par la source)

0 citations
Accès ouvert 2022 preprint OpenAlex

The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate

Raul R. Araya-Secchi, Katrine Bugge, Pernille Seiffert, Amalie Petry et autres

Abstract Class 1 cytokine receptors transmit signals through the membrane by a single transmembrane helix to an intrinsically disordered cytoplasmic domain that lacks kinase activity. While specific binding to phosphoinositides has been reported for the prolactin receptor (PRLR), the role of lipids …

dk, cl (code pays fourni par la source)

2 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2022 preprint OpenAlex

Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins

Francesco Pesce, Estella Anne Newcombe, Pernille Seiffert, Emil E. Tranchant et autres

ABSTRACT Diffusion measurements by pulsed field gradient NMR and fluorescence correlation spectroscopy can be used to probe the hydrodynamic radius of proteins, which contains information about the overall dimension of a protein in solution. The comparison of this value with structural models …

us, dk (code pays fourni par la source)

8 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2020 article OpenAlex

Orchestration of signaling by structural disorder in class 1 cytokine receptors

Pernille Seiffert, Katrine Bugge, Mads M. Nygaard, Gitte W. Haxholm et autres

BACKGROUND: Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), but …

dk (code pays fourni par la source)

34 citations Cell Communication and Signaling
Accès ouvert 2020 preprint OpenAlex

Orchestration of signaling by structural disorder in class 1 cytokine receptors

Pernille Seiffert, Katrine Bugge, Mads M. Nygaard, Gitte W. Haxholm et autres

Abstract Background: Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), …

dk (code pays fourni par la source)

1 citation Research Square

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