scispace - formally typeset
M

Michael L. Nielsen

Researcher at University of Copenhagen

Publications -  134
Citations -  15189

Michael L. Nielsen is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Proteome & Mass spectrometry. The author has an hindex of 48, co-authored 123 publications receiving 13104 citations. Previous affiliations of Michael L. Nielsen include University of Copenhagen Faculty of Health Sciences & University of Southern Denmark.

Papers
More filters
Journal ArticleDOI

Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication

TL;DR: It is proposed that TLK signaling promotes histone supply in S phase by targeting histone-free Asf1 and stimulating its ability to shuttle histones to sites of chromatin assembly.
Journal ArticleDOI

Immunoaffinity enrichments followed by mass spectrometric detection for studying global protein tyrosine phosphorylation

TL;DR: It is shown that a combination of immunoaffinity enrichment using multiple antibodies of both intact and digested proteins in parallel experiments is required for best possible coverage of all possible P-Tyr proteins in a sample.
Journal ArticleDOI

Intramolecular hydrogen atom transfer in hydrogen-deficient polypeptide radical cations

TL;DR: The pattern of electronic excitation dissociation (EED) is consistent with hydrogen transfer prior to electron capture, and radical polypeptide dications can be viewed as hydrogen atom wires as mentioned in this paper.
Journal ArticleDOI

The molecular basis of ATM-dependent dimerization of the Mdc1 DNA damage checkpoint mediator

TL;DR: X-ray structures of free and complexed MDC1 FHA domain reveal a ‘head-to-tail’ dimerization mechanism that is closely related to that seen in pre-activated forms of the Chk2 DNA damage kinase, and which both positively and negatively influences Mdc1 F HA domain-mediated interactions in human cells prior to and following DNA damage.
Journal ArticleDOI

Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p

TL;DR: It is shown that biotin starvation and knockout of Hst4p cause alterations in cellular respiration and an increase in reactive oxygen species (ROS), which suggests that Hst 4p plays a pivotal role in biotin metabolism and cellular energy homeostasis, and supports that HSt4p is a functional yeast homologue of the sirtuin deacetylase SIRT3.