Carlo P M van Mierlo
Overview
Explore the profile of Carlo P M van Mierlo including associated specialties, affiliations and a list of published articles.
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39
Citations
376
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Recent Articles
1.
Mitra R, Gadkari V, Meinen B, van Mierlo C, Ruotolo B, Bardwell J
Nat Commun
. 2021 Feb;
12(1):851.
PMID: 33558474
ATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation. These chaperones are thought to release their substrate proteins...
2.
Houwman J, Westphal A, Visser A, Borst J, van Mierlo C
Phys Chem Chem Phys
. 2018 Feb;
20(10):7059-7072.
PMID: 29473921
Flavodoxins have a protein topology that can be traced back to the universal ancestor of the three kingdoms of life. Proteins with this type of architecture tend to temporarily misfold...
3.
Westphal A, Geerke-Volmer A, van Mierlo C, van Berkel W
Biotechnol J
. 2017 Apr;
12(6).
PMID: 28403549
Production of hyperthermostable enzymes in mesophilic hosts frequently causes undesired aggregation of these proteins. During production of Pyrococcus furiosus endo-β-1,3 glucanase (LamA) in Escherichia coli, soluble and insoluble species form....
4.
Houwman J, van Mierlo C
FEBS J
. 2017 Apr;
284(19):3145-3167.
PMID: 28380286
The flavodoxin-like fold is a protein architecture that can be traced back to the universal ancestor of the three kingdoms of life. Many proteins share this α-β parallel topology and...
5.
Houwman J, Andre E, Westphal A, van Berkel W, van Mierlo C
J Biol Chem
. 2016 Oct;
291(50):25911-25920.
PMID: 27784783
Folding of proteins usually involves intermediates, of which an important type is the molten globule (MG). MGs are ensembles of interconverting conformers that contain (non-)native secondary structure and lack the...
6.
Rombouts W, de Kort D, Pham T, van Mierlo C, Werten M, de Wolf F, et al.
Biomacromolecules
. 2015 Jul;
16(8):2506-13.
PMID: 26175077
Recombinant protein polymers, which can combine different bioinspired self-assembly motifs in a well-defined block sequence, have large potential as building blocks for making complex, hierarchically structured materials. In this paper...
7.
Lindhoud S, Pirchi M, Westphal A, Haran G, van Mierlo C
J Mol Biol
. 2015 Jul;
427(19):3148-57.
PMID: 26163276
Molten globules (MGs) are compact, partially folded intermediates that are transiently present during folding of many proteins. These intermediates reside on or off the folding pathway to native protein. Conformational...
8.
van Son M, Lindhoud S, van der Wild M, van Mierlo C, Huber M
J Phys Chem B
. 2015 Jun;
119(43):13507-14.
PMID: 26101942
Protein folding is one of the important challenges in biochemistry. Understanding the folding process requires mapping of protein structure as it folds. Here we test the potential of distance determination...
9.
Houwman J, Westphal A, van Berkel W, van Mierlo C
Biochim Biophys Acta
. 2015 Jun;
1854(10 Pt A):1317-24.
PMID: 26073784
Correct folding of proteins is crucial for cellular homeostasis. More than thirty percent of proteins contain one or more cofactors, but the impact of these cofactors on co-translational folding remains...
10.
Lindhoud S, Westphal A, van Mierlo C, Visser A, Borst J
Int J Mol Sci
. 2014 Dec;
15(12):23836-50.
PMID: 25535076
Uniform labeling of proteins with fluorescent donor and acceptor dyes with an equimolar ratio is paramount for accurate determination of Förster resonance energy transfer (FRET) efficiencies. In practice, however, the...