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- Publications
- Influence
Posttranslational modification of CENP-A influences the conformation of centromeric chromatin
- A. Bailey, T. Panchenko, +9 authors D. Foltz
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 1 July 2013
Centromeres are chromosomal loci required for accurate segregation of sister chromatids during mitosis. The location of the centromere on the chromosome is not dependent on DNA sequence, but rather… Expand
NRMT is an α-N-methyltransferase that methylates RCC1 and Retinoblastoma Protein
- C. Tooley, J. Petkowski, +6 authors I. Macara
- Biology, Medicine
- Nature
- 20 July 2010
The post-translational methylation of α-amino groups was first discovered over 30 years ago on the bacterial ribosomal proteins L16 and L33 (refs 1, 2), but almost nothing is known about the function… Expand
NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1.
- J. Petkowski, Lindsay A. Bonsignore, +4 authors Christine E Schaner Tooley
- Biology, Medicine
- The Biochemical journal
- 15 December 2013
NRMT (N-terminal regulator of chromatin condensation 1 methyltransferase) was the first eukaryotic methyltransferase identified to specifically methylate the free α-amino group of proteins. Since the… Expand
Phosphine gas in the cloud decks of Venus
- J. Greaves, A. M. Richards, +16 authors Jim Hoge
- Physics
- 14 September 2020
Measurements of trace gases in planetary atmospheres help us explore chemical conditions different to those on Earth. Our nearest neighbour, Venus, has cloud decks that are temperate but hyperacidic.… Expand
Substrate specificity of mammalian N-terminal α-amino methyltransferase NRMT.
- J. Petkowski, Christine E Schaner Tooley, +6 authors I. Macara
- Biology, Medicine
- Biochemistry
- 31 July 2012
N-Terminal methylation of free α-amino groups is a post-translational modification of proteins that was first described 30 years ago but has been studied very little. In this modification, the… Expand
Crystal structures of TM0549 and NE1324—two orthologs of E. coli AHAS isozyme III small regulatory subunit
- J. Petkowski, M. Chruszcz, +8 authors W. Minor
- Biology, Medicine
- Protein science : a publication of the Protein…
- 1 July 2007
Crystal structures of two orthologs of the regulatory subunit of acetohydroxyacid synthase III (AHAS, EC 2.2.1.6) from Thermotoga maritima (TM0549) and Nitrosomonas europea (NE1324) were determined… Expand
Toward a List of Molecules as Potential Biosignature Gases for the Search for Life on Exoplanets and Applications to Terrestrial Biochemistry.
- S. Seager, W. Bains, J. Petkowski
- Environmental Science, Medicine
- Astrobiology
- 1 April 2016
UNLABELLED
Thousands of exoplanets are known to orbit nearby stars. Plans for the next generation of space-based and ground-based telescopes are fueling the anticipation that a precious few habitable… Expand
Structure of Escherichia coli RutC, a member of the YjgF family and putative aminoacrylate peracid reductase of the rut operon.
- A. A. Knapik, J. Petkowski, +5 authors W. Minor
- Biology, Medicine
- Acta crystallographica. Section F, Structural…
- 1 November 2012
RutC is the third enzyme in the Escherichia coli rut pathway of uracil degradation. RutC belongs to the highly conserved YjgF family of proteins. The structure of the RutC protein was determined and… Expand
Assembly and nuclear export of pre-ribosomal particles in budding yeast
- Stefan Gerhardy, A. M. Menet, C. Peña, J. Petkowski, V. Panse
- Biology, Medicine
- Chromosoma
- 11 May 2014
The ribosome is responsible for the final step of decoding genetic information into proteins. Therefore, correct assembly of ribosomes is a fundamental task for all living cells. In eukaryotes, the… Expand
Natural Products Containing a Nitrogen-Sulfur Bond.
- J. Petkowski, W. Bains, S. Seager
- Chemistry, Medicine
- Journal of natural products
- 24 January 2018
Only about 100 natural products are known to contain a nitrogen-sulfur (N-S) bond. This review thoroughly categorizes N-S bond-containing compounds by structural class. Information on biological… Expand