Hendrik Sielaff
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Explore the profile of Hendrik Sielaff including associated specialties, affiliations and a list of published articles.
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Articles
21
Citations
461
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Recent Articles
1.
Sielaff H, Zhao Z
Int J Biochem Cell Biol
. 2024 Oct;
176:106667.
PMID: 39362301
Chromatin remodeling, carried out by four major subfamilies of ATP-dependent remodeler complexes across eukaryotes, alleviates the topological challenge posed by nucleosomes to regulate genome access. Recently, single-molecule and single-cell imaging...
2.
Engl W, Kunstar-Thomas A, Chen S, Ng W, Sielaff H, Zhao Z
Nat Commun
. 2024 Sep;
15(1):7646.
PMID: 39223123
Despite their prevalent cancer implications, the in vivo dynamics of SWI/SNF chromatin remodelers and how misregulation of such dynamics underpins cancer remain poorly understood. Using live-cell single-molecule tracking, we quantify...
3.
Ng W, Sielaff H, Zhao Z
Int J Mol Sci
. 2022 Jul;
23(14).
PMID: 35887384
As an effective and versatile strategy to compartmentalize cellular components without the need for lipid membranes, phase separation has been found to underpin a wide range of intranuclear processes, particularly...
4.
Sielaff H, Basu S, Zhao Z
Front Mol Biosci
. 2022 Jun;
9:929370.
PMID: 35669565
No abstract available.
5.
Sielaff H, Dienerowitz F, Dienerowitz M
Nanoscale
. 2022 Jan;
14(6):2327-2336.
PMID: 35084006
Single-molecule Förster resonance energy transfer (smFRET) is a key technique to observe conformational changes in molecular motors and to access the details of single-molecule static and dynamic disorder during catalytic...
6.
Bogdanovic N, Trifunovic D, Sielaff H, Westphal L, Bhushan S, Muller V, et al.
FEBS J
. 2019 Feb;
286(10):1894-1907.
PMID: 30791207
The Na translocating F F ATP synthase from Acetobacterium woodii shows a subunit stoichiometry of α :β :γ:δ:ε:a:b :(c ) :c and reveals an evolutionary path between synthases and pumps...
7.
Sielaff H, Yanagisawa S, Frasch W, Junge W, Borsch M
Molecules
. 2019 Feb;
24(3).
PMID: 30704145
F-ATP synthases use proton flow through the F domain to synthesize ATP in the F₁ domain. In , the enzyme consists of rotor subunits γε and stator subunits (αβ)₃δ₂. Subunits...
8.
Sielaff H, Duncan T, Borsch M
Biochim Biophys Acta Bioenerg
. 2018 Jun;
1859(9):775-788.
PMID: 29932911
F-type ATP synthases are extraordinary multisubunit proteins that operate as nanomotors. The Escherichia coli (E. coli) enzyme uses the proton motive force (pmf) across the bacterial plasma membrane to drive...
9.
Ragunathan P, Sielaff H, Sundararaman L, Biukovic G, Subramanian Manimekalai M, Singh D, et al.
J Biol Chem
. 2017 May;
292(27):11262-11279.
PMID: 28495884
The FF -ATP (F-ATP) synthase is essential for growth of , the causative agent of tuberculosis (TB). In addition to their synthase function most F-ATP synthases possess an ATP-hydrolase activity,...
10.
Singh D, Sielaff H, Borsch M, Gruber G
FEBS Lett
. 2017 Feb;
591(6):854-862.
PMID: 28231387
In archaea the A A ATP synthase uses a transmembrane electrochemical potential to generate ATP, while the soluble A domain (subunits A B DF) alone can hydrolyse ATP. The three...