Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Heike Piechura"'
Autor:
Doris Metzler, Sandra Puetz, Lena Reimann, Mechthild M. Schroeter, Lubomir T. Lubomirov, Bettina Warscheid, Mona S. Hunger, Heike Piechura, Gabriele Pfitzer
Publikováno v:
Journal of Muscle Research and Cell Motility
Nitrovasodilators and agonists, via an increase in intracellular cyclic nucleotide levels, can induce smooth muscle relaxation without a concomitant decrease in phosphorylation of the regulatory light chains (RLC) of myosin. However, since cyclic nuc
Autor:
Günter A. Schaub, Helmut E. Meyer, Saskia Dittmeyer-Schäfer, Bettina Warscheid, Carsten Balczun, Heike Piechura, Christian Karl Meiser, Tanja Werner
Publikováno v:
Insect Biochemistry and Molecular Biology. 40:345-353
Triatomines inhibit the clotting of ingested blood in the stomach (anterior midgut). After verifying this phenomenon in Panstrongylus megistus using coagulation assays, a full-length cDNA encoding a Kazal-like inhibitor was amplified by PCR. The open
Autor:
Helmut E. Meyer, Carsten Balczun, Bettina Warscheid, Christian Karl Meiser, G. A. Schaub, Heike Piechura
Publikováno v:
Insect Molecular Biology. 19:409-421
A cDNA encoding a trypsin-like protease from the salivary glands of the haematophagous reduviid Panstrongylus megistus was cloned and sequenced. The deduced protein sequence showed similarities to serine proteases of other hemipterans but with substi
Autor:
David U. Mick, Milena Vukotic, Bettina Warscheid, Heike Piechura, Peter Rehling, Markus Deckers, Helmut E. Meyer
Publikováno v:
The Journal of Cell Biology
Coa3 and Cox14 form assembly intermediates with newly synthesized Cox1 and are required for association of the Mss51 translational activator with these complexes.
Regulation of eukaryotic cytochrome oxidase assembly occurs at the level of Cox1 t
Regulation of eukaryotic cytochrome oxidase assembly occurs at the level of Cox1 t
Autor:
Manuel P. Pinto, Jorge E. Azevedo, Clara Sá-Miranda, Heike Piechura, Bettina Warscheid, Cláudia P. Grou, Helmut E. Meyer, Sebastian Wiese, Andreia F. Carvalho
Publikováno v:
Journal of Biological Chemistry. 283:14190-14197
According to current models of peroxisomal biogenesis, newly synthesized peroxisomal matrix proteins are transported into the organelle by Pex5p. Pex5p recognizes these proteins in the cytosol, mediates their membrane translocation, and is exported b
Autor:
Kai Stühler, Helmut E. Meyer, Heike Piechura, Nadine Stoepel, Daniela Brunert, Anastasia Mashukova, Eva M. Neuhaus, Bettina Warscheid, Hanns Hatt, Barbara Sitek, Jon Barbour
Publikováno v:
Journal of Proteome Research. 7:1594-1605
The olfactory system is exposed to a plethora of chemical compounds throughout an organism's lifespan. Anticipation of stimuli and construction of appropriate neural filters present a significant challenge. This may be addressed via modulation of the
Autor:
Heike Piechura, Bettina Warscheid, Elmar Langenfeld, Christiane Lohaus, Helmut E. Meyer, Florian Tribl, Tanja Dombert, Katrin Marcus
Publikováno v:
PROTEOMICS. 8:1204-1211
HPLC has emerged as a valuable tool for separating proteins. To address the analysis of complex proteomes and quantitative changes of proteins therein, we developed a multidimensional LC (MDLC)-based approach followed by large gel 1-D SDS-PAGE. Here
Publikováno v:
International Journal of Peptide Research and Therapeutics. 13:413-421
The neurotrophin receptor p75 interacts with the GTPase Ras. Unstimulated it inactivates Ras while ligand binding induces Ras activation. We developed an inhibitory peptide (ip75RBD) which interferes with the binding domain of Ras of the intracellula
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 893
Through crucial advancements in quantitative mass spectrometry (MS), proteomics has evolved from taking mere "snapshots" of proteomes to thoroughly studying dynamic changes in entire proteomes and characterizing intricate protein-protein interaction
Publikováno v:
Methods in Molecular Biology ISBN: 9781617798849
Quantitative Methods in Proteomics
Quantitative Methods in Proteomics
Through crucial advancements in quantitative mass spectrometry (MS), proteomics has evolved from taking mere "snapshots" of proteomes to thoroughly studying dynamic changes in entire proteomes and characterizing intricate protein-protein interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f97e46e9d940cecfd1a0f1153c33fee8
https://doi.org/10.1007/978-1-61779-885-6_14
https://doi.org/10.1007/978-1-61779-885-6_14