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M. Carmen Herrera

Researcher at Imperial College London

Publications -  11
Citations -  527

M. Carmen Herrera is an academic researcher from Imperial College London. The author has contributed to research in topics: Helicase & Pseudomonas putida. The author has an hindex of 10, co-authored 11 publications receiving 481 citations. Previous affiliations of M. Carmen Herrera include Spanish National Research Council & Max Planck Society.

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Journal ArticleDOI

An ORC/Cdc6/MCM2-7 Complex Is Formed in a Multistep Reaction to Serve as a Platform for MCM Double-Hexamer Assembly

Alejandra Fernández-Cid, +9 more
- 23 May 2013 - 
TL;DR: This work reveals multiple critical mechanisms that redefine the understanding of DNA licensing by discovering that Orc1 ATP-hydrolysis is equally important in this process and promoting the formation of the ORC/Cdc6/MCM2-7 (OCM) complex, which functions in MCM 2-7 double-hexamer assembly.
Journal ArticleDOI

A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2–7 onto DNA

Stefan A. Samel, +7 more
- 01 Aug 2014 - 
TL;DR: This study establishes the existence of a unique DNA entry gate for regulated helicase loading, revealing key mechanisms in helicaseloading, which has important implications for helicase activation.
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Identification of conditionally essential genes for growth of Pseudomonas putida KT2440 on minimal medium through the screening of a genome‐wide mutant library

M. Antonia Molina-Henares, +6 more
- 01 Jun 2010 - 
TL;DR: In vivo high-throughput analysis of single-gene P. putida KT2440 knockouts provides relevant insights into the metabolic cross-road of biosynthetic pathways in this microorganism, as well as valuable information for the fine tuning of current in silico metabolic models.
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In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2–7 hexamer dimerization

Cecile Evrin, +8 more
- 01 Mar 2013 - 
TL;DR: These findings illustrate how conserved Cdc6 AAA+ motifs modulate MCM2–7 recruitment, show that ATPase activity is required for MCM1–7 hexamer dimerization and demonstrate that MCM 2–7hexamers are recruited to origins in a consecutive process.
Journal ArticleDOI

Identification and characterization of the PhhR regulon in Pseudomonas putida

M. Carmen Herrera, +4 more
- 01 Jun 2010 - 
TL;DR: Pseudomonas putida is a soil microorganism that utilizes aromatic amino acids present in root exudates as a nitrogen source and the PhhR transcriptional regulator is a global regulator responsible for the activation of genes essential for phenylalanine degradation, phenylAlanine homeostasis and other genes of unknown function.