Biophysical characterization of the DNA binding motif of human phospholipid scramblase 1.

Anisotropy DNA binding DNA–protein interaction Human phospholipid scramblase IP3R1P oligonucleotide

Journal

European biophysics journal : EBJ
ISSN: 1432-1017
Titre abrégé: Eur Biophys J
Pays: Germany
ID NLM: 8409413

Informations de publication

Date de publication:
Dec 2022
Historique:
received: 19 04 2022
accepted: 06 10 2022
revised: 04 10 2022
pubmed: 20 10 2022
medline: 23 11 2022
entrez: 19 10 2022
Statut: ppublish

Résumé

Human phospholipid scramblase 1 (hPLSCR1) is a 37 kDa multi-compartmental protein, which was initially identified as a Ca

Identifiants

pubmed: 36260146
doi: 10.1007/s00249-022-01621-0
pii: 10.1007/s00249-022-01621-0
doi:

Substances chimiques

Phospholipid Transfer Proteins 0
Phospholipids 0
Oligonucleotides 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

579-593

Informations de copyright

© 2022. European Biophysical Societies' Association.

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Auteurs

Sarika Rayala (S)

Applied and Industrial Microbiology Laboratory, Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.

Ulaganathan Sivagnanam (U)

Applied and Industrial Microbiology Laboratory, Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.

Sathyanarayana N Gummadi (SN)

Applied and Industrial Microbiology Laboratory, Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India. gummadi@iitm.ac.in.

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