FEBS Letters

Journal: FEBS Letters

Abbreviation

FEBS lett.

Publisher

Elsevier

ISSN

0014-5793
1873-3468

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Publications 1 - 10 of 67

A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli
Fischer, Heinrich; Glockshuber, Rudi (1994)
FEBS Letters
Direct interaction of coenzyme M with the active-site Fe–S cluster of heterodisulfide reductase
Shokes, Jacob E.; Duin, Evert C.; Bauer, Carsten; et al. (2005)
FEBS Letters
Biochemical characterisation of TCTP questions its function as a guanine nucleotide exchange factor for Rheb
Rehmann, Holger; Brüning, M.; Berghaus, Carsten; et al. (2008)
FEBS Letters
Translationally controlled tumour protein (TCTP) is involved in malignant transformation and regulation of apoptosis. It has been postulated to serve as a guanine nucleotide exchange factor for the small G-protein Rheb. Rheb functions in the PI3 kinase/mTOR pathway. The study presented here was initiated to characterise the interaction between TCTP and Rheb biochemically. Since (i) no exchange activity of TCTP towards Rheb could be detected in vitro, (ii) no interaction between TCTP and Rheb could be detected by NMR spectroscopy, and (iii) no effect of TCTP depletion in cells on the direct downstream targets of Rheb could be observed in vivo, this study shows that TCTP is unlikely to be a guanine nucleotide exchange factor for Rheb. Structured summary: MINT-6741806:RAP1B (uniprotkb:P61224) physically interacts (MI:0218) with Epac1 (uniprotkb:O95398) by anti tag coimmunoprecipitation (MI:0007).
Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes
Bultot, Laurent; Horman, Sandrine; Neumann, Dietbert; et al. (2009)
FEBS Letters
In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed
Ochsner, Andrea M.; Müller, Jonas E.N.; Mora, Carlos Andrea; et al. (2014)
FEBS Letters
In the Gram-positive methylotroph Bacillus methanolicus, methanol oxidation is catalyzed by an NAD-dependent methanol dehydrogenase (Mdh) that belongs to the type III alcohol dehydrogenase (Adh) family. It was previously shown that the in vitro activity of B. methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase. Here we show that this feature is not unique, but more widespread among type III Adhs in combination with Act or other Act-like Nudix hydrolases. In addition, we studied the effect of site directed mutations in the predicted active site of Mdh and two other type III Adhs with regard to activity and activation by Act.
Helix swapping leads to dimerization of the N-terminal domain of the c-type cytochrome maturation protein CcmH from Escherichia coli
Ahuja, Umesh; Rozhkova, Anna; Glockshuber, Rudolf; et al. (2008)
FEBS Letters
AMPK beta subunits display isoform specific affinities for carbohydrates
Koay, Ann; Woodcroft, Ben; Petrie, Emma J.; et al. (2010)
FEBS Letters
Nuclear envelope localization of human UNC84A does not require nuclear lamins
Hasan, Sameez; Güttinger, Stephan; Mühlhäusser, Petra; et al. (2006)
FEBS Letters
Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases
Ritte, Gerhard; Heydenreich, Matthias; Mahlow, Sebastian; et al. (2006)
FEBS Letters
Structure-activity relationship of amyloid fibrils
Maji, Samir K.; Wang, Lei; Greenwald, Jason; et al. (2009)
FEBS Letters

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Journal: FEBS Letters

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