Martijn van Rosmalen
Overview
Explore the profile of Martijn van Rosmalen including associated specialties, affiliations and a list of published articles.
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Articles
6
Citations
199
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0
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Recent Articles
1.
van Rosmalen M, Ni Y, Vervoort D, Arts R, Ludwig S, Merkx M
Anal Chem
. 2018 Feb;
90(5):3592-3599.
PMID: 29443503
Monitoring the levels of therapeutic antibodies in individual patients would allow patient-specific dose optimization, with the potential for major therapeutic and financial benefits. Our group recently developed a new platform...
2.
van Rosmalen M, Krom M, Merkx M
Biochemistry
. 2017 Nov;
56(50):6565-6574.
PMID: 29168376
Flexible polypeptide linkers composed of glycine and serine are important components of engineered multidomain proteins. We have previously shown that the conformational properties of Gly-Gly-Ser repeat linkers can be quantitatively...
3.
van Rosmalen M, Janssen B, Hendrikse N, van der Linden A, Pieters P, Wanders D, et al.
J Biol Chem
. 2016 Dec;
292(4):1477-1489.
PMID: 27974464
Meditopes are cyclic peptides that bind in a specific pocket in the antigen-binding fragment of a therapeutic antibody such as cetuximab. Provided their moderate affinity can be enhanced, meditope peptides...
4.
Amir A, van Rosmalen M, Mayer G, Lebendiker M, Danieli T, Friedler A
Sci Rep
. 2015 Jul;
5:11629.
PMID: 26130271
We present a possible molecular basis for the opposite activity of two homologues proteins that bind similar ligands and show that this is achieved by fine-tuning of the interaction interface....
5.
Janssen B, van Rosmalen M, van Beek L, Merkx M
Angew Chem Int Ed Engl
. 2015 Jan;
54(8):2530-3.
PMID: 25573528
Oligonucleotide-based molecular circuits offer the exciting possibility to introduce autonomous signal processing in biomedicine, synthetic biology, and molecular diagnostics. Here we introduce bivalent peptide-DNA conjugates as generic, noncovalent, and easily...
6.
Karagoz G, Duarte A, Ippel H, Uetrecht C, Sinnige T, van Rosmalen M, et al.
Proc Natl Acad Sci U S A
. 2010 Dec;
108(2):580-5.
PMID: 21183720
The molecular chaperone Hsp90 is a protein folding machine that is conserved from bacteria to man. Human, cytosolic Hsp90 is dedicated to folding of chiefly signal transduction components. The chaperoning...