Karl A T Makepeace
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Explore the profile of Karl A T Makepeace including associated specialties, affiliations and a list of published articles.
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14
Citations
220
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Recent Articles
1.
Makepeace K, Rookyard A, Das L, Vardarajan B, Chakrabarty J, Jain A, et al.
Curr Protoc
. 2024 Mar;
4(3):e1014.
PMID: 38506436
This article presents a practical guide to mass spectrometry-based data-independent acquisition and label-free quantification for proteomics analysis applied to cerebrospinal fluid, offering a robust and scalable approach to probing the...
2.
Makepeace K, Mohammed Y, Rudashevskaya E, Petrotchenko E, Vogtle F, Meisinger C, et al.
Mol Cell Proteomics
. 2020 Feb;
19(4):624-639.
PMID: 32051233
An experimental and computational approach for identification of protein-protein interactions by chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS),...
3.
Makepeace K, Brodie N, Popov K, Gudavicius G, Nelson C, Petrotchenko E, et al.
J Proteomics
. 2019 Nov;
211:103544.
PMID: 31683063
For disordered proteins, ligand binding can be a critical event that changes their structural dynamics. The ability to characterize such changes would facilitate the development of drugs designed to stabilize...
4.
Popov K, Makepeace K, Petrotchenko E, Dokholyan N, Borchers C
Structure
. 2019 Oct;
27(11):1710-1715.e4.
PMID: 31628033
Combining structural proteomics experimental data with computational methods is a powerful tool for protein structure prediction. Here, we apply a recently developed approach for de novo protein structure determination based...
5.
Teixeira F, Tse E, Castro H, Makepeace K, Meinen B, Borchers C, et al.
Nat Commun
. 2019 Feb;
10(1):659.
PMID: 30737390
Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our...
6.
Groitl B, Horowitz S, Makepeace K, Petrotchenko E, Borchers C, Reichmann D, et al.
Nat Commun
. 2016 Jan;
7:10357.
PMID: 26787517
Stress-specific activation of the chaperone Hsp33 requires the unfolding of a central linker region. This activation mechanism suggests an intriguing functional relationship between the chaperone's own partial unfolding and its...
7.
Makepeace K, Serpa J, Petrotchenko E, Borchers C
Methods
. 2015 Mar;
89:74-8.
PMID: 25752848
Disulfide bonds are valuable constraints in protein structure modeling. The Cys-Cys disulfide bond undergoes specific fragmentation under CID and, therefore, can be considered as a CID-cleavable crosslink. We have recently...
8.
Solomonson M, Setiaputra D, Makepeace K, Lameignere E, Petrotchenko E, Conrady D, et al.
Structure
. 2015 Feb;
23(3):571-583.
PMID: 25684576
Mycobacterium tuberculosis (Mtb) uses the ESX-1 type VII secretion system to export virulence proteins across its lipid-rich cell wall, which helps permeabilize the host's macrophage phagosomal membrane, facilitating the escape...
9.
Petrotchenko E, Makepeace K, Borchers C
Curr Protoc Bioinformatics
. 2014 Dec;
48:8.18.1-8.18.19.
PMID: 25501944
Cross-linking combined with mass spectrometry for the study of proteins and protein complexes is greatly facilitated by the use of isotopically coded cleavable cross-linking reagents. The isotopic coding of the...
10.
Brodie N, Makepeace K, Petrotchenko E, Borchers C
J Proteomics
. 2014 Sep;
118:12-20.
PMID: 25192908
Biological Significance: Structural proteomics can be used for studying protein structures which may be difficult to examine by traditional structural biology methods such as NMR or X-ray crystallography. Crosslinking in...