Author

D. N. Langelaan

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

A. D. Brown· 2 shared D. J. Dupre· 2 shared K. L. Vergunst· 2 shared C. Cranstone· 1 shared C. Kenward· 1 shared C. M. Blair· 1 shared G. S. Baillie· 1 shared M. Branch· 1 shared

Activity by Year

2022-2022 · peak 3/yr

Co-Author Collaboration Network

8 top collaborators · 18 mutual co-author links

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2 shared papersBiochemistry

A. D. Brown

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Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivAug 30, 2022

β-catenin interacts with the TAZ1 and TAZ2 domains of CBP/p300 to activate gene transcription

C. Cranstone, A. D. Brown, D. J. Dupre, D. N. Langelaan

This study identifies the interaction between β-catenin's C-terminal domain and CBP/p300's TAZ1/TAZ2 domains, revealing key residues critical for gene activation in Wnt/β-catenin signaling.

DOI 10.1016/j.ijbiomac.2023.124155

experimental assaychromatin & epigenetic regulation

𝕏 PostBluesky

BiochemistrybioRxivAug 29, 2022

Characterization of the structure and self-assembly of two distinct class IB hydrophobins

K. L. Vergunst, C. Kenward, D. N. Langelaan

This study determines the atomic structure of SLH4, a class IB hydrophobin, and compares its self-assembly behavior to SC16, revealing how surface properties influence function.

DOI 10.1007/s00253-022-12253-x

protein structureexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivAug 28, 2022

Structural basis of CBP/p300 recruitment by the microphthalmia-associated transcription factor

A. D. Brown, K. L. Vergunst, M. Branch…·D. N. Langelaan

This study identifies the structural basis of MITF's interaction with CBP/p300 TAZ domains, revealing an acidic motif essential for transcriptional activity and showing that E1A can inhibit this interaction.

DOI 10.1016/j.bbamcr.2023.119520

humanproteomics

𝕏 PostBluesky