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Klára Kirsch

Researcher at Hungarian Academy of Sciences

Publications -  11
Citations -  159

Klára Kirsch is an academic researcher from Hungarian Academy of Sciences. The author has contributed to research in topics: Kinase & Medicine. The author has an hindex of 4, co-authored 7 publications receiving 107 citations. Previous affiliations of Klára Kirsch include Budapest University of Technology and Economics.

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Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases

TL;DR: It is proposed that short MAPK‐binding stretches are created in disordered protein segments through a variety of ways and they represent a major resource for ancient signaling enzymes to acquire new regulatory roles.
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Differential effects of cold acclimation and abscisic acid on free amino acid composition in wheat

TL;DR: Since cold acclimation induced the accumulation of most of the amino acids, while ABA had a significant effect only on Asn, the cold-induced changes in free amino acid levels were probably not mediated by ABA.
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Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38.

TL;DR: It is shown that the ATF2 TAD is controlled by functionally distinct signaling pathways (JNK and p38) through structurally different MAPK binding sites, andStructures of MAPK-TAD complexes and mechanistic modeling of ATF1 TAD phosphorylation in cells suggest that kinase binding motifs and phosphorylated sites line up to maximize MAPK based co-regulation.

regulation of free amino acid and polyamine levels during cold acclimation in wheat

TL;DR: It is shown that free amino acids and polyamines play an important role in the cold acclimation and their levels are regulated at the transcriptional level.
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MAP Kinase-Mediated Activation of RSK1 and MK2 Substrate Kinases.

TL;DR: It is identified that kinase heterodimers form structurally and functionally distinct complexes depending on the activation state of the MAPK, and it is shown that small-molecule inhibitors may affect the quaternary arrangement of kinase heterogeneity and thus influence downstream signaling in a specific manner.