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Holger Flechsig

Explore the profile of Holger Flechsig including associated specialties, affiliations and a list of published articles. Areas
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Articles 29
Citations 208
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Recent Articles
1.
Sumino A, Sumikama T, Zhao Y, Flechsig H, Umeda K, Kodera N, et al.
ACS Nano . 2024 Aug; 18(36):25018-25035. PMID: 39180186
α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid glutamate receptors (AMPARs) enable rapid excitatory synaptic transmission by localizing to the postsynaptic density of glutamatergic spines. AMPARs possess large extracellular N-terminal domains (NTDs), which are crucial...
2.
Akter L, Flechsig H, Marchesi A, Franz C
Int J Mol Sci . 2024 Feb; 25(4). PMID: 38396630
Laminins are trimeric glycoproteins with important roles in cell-matrix adhesion and tissue organization. The laminin α, ß, and γ-chains have short N-terminal arms, while their C-termini are connected via a...
3.
Hall D, Flechsig H, Sumikama T
Biophys Rev . 2024 Jan; 15(6):2041-2044. PMID: 38192340
Atomic Force Microscopy (AFM) is a structural determination technique that involves 'prodding' surfaces with a nanometer sized needle with concomitant measurement of the resisting force. Due to its ability to...
4.
Ye Z, Galvanetto N, Puppulin L, Pifferi S, Flechsig H, Arndt M, et al.
Nat Commun . 2024 Jan; 15(1):110. PMID: 38167485
Transmembrane protein 16 F (TMEM16F) is a Ca-activated homodimer which functions as an ion channel and a phospholipid scramblase. Despite the availability of several TMEM16F cryogenic electron microscopy (cryo-EM) structures,...
5.
Amyot R, Nakamoto K, Kodera N, Flechsig H
Front Mol Biosci . 2023 Dec; 10:1264161. PMID: 38094082
Atomic force microscopy (AFM) and high-speed AFM allow direct observation of biomolecular structures and their functional dynamics. Based on scanning the molecular surface of a sample deposited on a supporting...
6.
Ando T, Fukuda S, Ngo K, Flechsig H
Annu Rev Biophys . 2023 Dec; 53(1):19-39. PMID: 38060998
Structural biology is currently undergoing a transformation into dynamic structural biology, which reveals the dynamic structure of proteins during their functional activity to better elucidate how they function. Among the...
7.
Takeda K, Flechsig H, Muro I, Amyot R, Kobayashi F, Kodera N, et al.
Nano Lett . 2023 Dec; 23(24):11940-11948. PMID: 38055898
Ubiquitin (Ub) ligases E3 are important factors in selecting target proteins for ubiquitination and determining the type of polyubiquitin chains on the target proteins. In the HECT (homologous to E6AP...
8.
Tsujioka S, Sumino A, Nagasawa Y, Sumikama T, Flechsig H, Puppulin L, et al.
Sci Adv . 2023 Jun; 9(26):eadh1069. PMID: 37390213
Ca/calmodulin-dependent protein kinase II (CaMKII) plays a pivotal role in synaptic plasticity. It is a dodecameric serine/threonine kinase that has been highly conserved across metazoans for over a million years....
9.
Flechsig H, Ando T
Curr Opin Struct Biol . 2023 Apr; 80:102591. PMID: 37075535
High-speed atomic force microscopy (HS-AFM) allows direct observation of biological molecules in dynamic action. However, HS-AFM has no atomic resolution. This article reviews recent progress of computational methods to infer...
10.
Sumikama T, Hall D, Flechsig H
Biophys Rev . 2023 Mar; 15(1):17-18. PMID: 36909960
This Commentary describes an open call for submissions to an Issue Focus of the IUPAB journal on the topic of the, 'Computational biophysics of atomic force microscopy'. The Issue Focus...