A
Achim Brinker
Researcher at Genomics Institute of the Novartis Research Foundation
Publications - 26
Citations - 1976
Achim Brinker is an academic researcher from Genomics Institute of the Novartis Research Foundation. The author has contributed to research in topics: Binding domain & Embryonic stem cell. The author has an hindex of 15, co-authored 26 publications receiving 1901 citations.
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Journal ArticleDOI
In silico activity profiling reveals the mechanism of action of antimalarials discovered in a high-throughput screen
David Plouffe,Achim Brinker,Case W. McNamara,Kerstin Henson,Nobutaka Kato,Kelli Kuhen,Advait Nagle,Francisco Adrian,Jason T. Matzen,Paul A. Anderson,Tae-gyu Nam,Nathanael S. Gray,Arnab Chatterjee,Jeff Janes,S. Frank Yan,Richard E. Trager,Jeremy S. Caldwell,Peter G. Schultz,Yingyao Zhou,Elizabeth A. Winzeler +19 more
TL;DR: An efficient and robust high-throughput cell-based screen based on proliferation of Plasmodium falciparum in erythrocytes, which identified most known antimalarials and many novel chemical scaffolds, which likely act through both known and novel pathways.
Journal ArticleDOI
Synthetic small molecules that control stem cell fate
Sheng Ding,Tom Y.-H. Wu,Achim Brinker,Eric C. Peters,Wooyoung Hur,Nathanael S. Gray,Peter G. Schultz +6 more
TL;DR: Evidence is provided that GSK-3β is involved in the induction of mammalian neurogenesis in ESCs, and this and such other molecules are likely to provide insights into the molecular mechanisms that control stem cell fate, and may ultimately be useful to in vivo stem cell biology and therapy.
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Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
Arthur R. Salomon,Scott B. Ficarro,Laurence M. Brill,Achim Brinker,Qui T. Phung,Christer Ericson,Karsten Sauer,Ansgar Brock,David M. Horn,Peter G. Schultz,Eric C. Peters +10 more
TL;DR: A sensitive approach based on multidimensional liquid chromatography/mass spectrometry is described that enables the rapid identification of numerous sites of tyrosine phosphorylation on a number of different proteins from human whole cell lysates to enable the rapid generation of new insights into signaling pathways as they occur in states of health and disease.
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In vivo incorporation of unnatural amino acids to probe structure, dynamics and ligand binding in a large protein by Nuclear Magnetic Resonance spectroscopy
Susan E. Cellitti,David H. Jones,Leanna Lagpacan,Xueshi Hao,Qiong Zhang,Huiyong Hu,Scott M. Brittain,Achim Brinker,Jeremy S. Caldwell,Badry Bursulaya,Glen Spraggon,Ansgar Brock,Youngha Ryu,Tetsuo Uno,Peter G. Schultz,Bernhard H. Geierstanger +15 more
TL;DR: In vivo incorporation of isotopically labeled unnatural amino acids into large proteins drastically reduces the complexity of nuclear magnetic resonance (NMR) spectra and establishes a new avenue for the site-specific labeling of proteins at individual residues without altering the protein sequence.
Journal ArticleDOI
Immunoassay and antibody microarray analysis of the HUPO Plasma Proteome Project reference specimens: Systematic variation between sample types and calibration of mass spectrometry data
Brian B. Haab,Bernhard H. Geierstanger,George Michailidis,Frank Vitzthum,Sara Forrester,Ryan Okon,Petri Saviranta,Achim Brinker,Martin Sorette,Lorah T. Perlee,Shubha Suresh,Garry Drwal,Joshua N. Adkins,Gilbert S. Omenn +13 more
TL;DR: The conclusions from these initial analyses are that the optimal blood preparation method is variable between analytes and that the discovery of blood proteins by MS can be extended to concentrations below the ng/mL range under certain circumstances.