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Jörg Hagmann

Researcher at Max Planck Society

Publications -  36
Citations -  2282

Jörg Hagmann is an academic researcher from Max Planck Society. The author has contributed to research in topics: DNA methylation & Genome. The author has an hindex of 18, co-authored 33 publications receiving 1962 citations.

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Modulation of Ambient Temperature-Dependent Flowering in Arabidopsis thaliana by Natural Variation of FLOWERING LOCUS M.

TL;DR: This work identifies insertion polymorphisms in the first intron of FLM as causative for accelerated flowering in many natural A. thaliana accessions, especially in cool (15°C) temperatures and presents evidence for a potential adaptive role of this structural variation and link it specifically to changes in the abundance ofFLM-ß.
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Differences in cortical actin structure and dynamics document that different types of blebs are formed by distinct mechanisms

TL;DR: A simplified classification scheme has been developed to relate the type of bleb to specific signals or cell functions and shows that spontaneously blebbing cells form almost exclusively type 1 blebs.
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KH domain protein RCF3 is a tissue-biased regulator of the plant miRNA biogenesis cofactor HYL1

TL;DR: Mechanistically, RCF3 affects miRNA biogenesis through nuclear interactions with the phosphatases C-TERMINAL DOMAIN PHOSPHATASE-LIKE1 and 2 (CPL1 and CPL2) and these interactions are essential to regulate the phosphorylation status, and thus the activity, of the double-stranded RNA binding protein and DICER-LIke1 cofactor HYPONASTIC LEAVES1 (HYL1).
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Long-term balancing selection drives evolution of immunity genes in Capsella.

TL;DR: Re reconstructing the evolution of the disease-related locus MLO2b, it is found that divergence between ancient haplotypes can be obscured by referenced based re-sequencing methods, and that trans-specific alleles can encode substantially diverged protein sequences.
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Structure and function of the C-terminal hypervariable region of K-Ras4B in plasma membrane targetting and transformation.

TL;DR: It is found that charge and a lipid residue are sufficient for plasma membrane localization and function of the constitutively active V12K-Ras4B and mutants with very highly charged domains that bind almost exclusively to the plasma membrane show less transforming potential than expected.