W. Nartey

发表

The NMR solution structure of Mycobacterium tuberculosis F‐ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine

G. Grüber, T. Dick, Subhashri Kundu, 2018, The FEBS journal.

Low resolution solution structure of an enzymatic active AhpC10:AhpF2 ensemble of the Escherichia coli Alkyl hydroperoxide Reductase.

F. Eisenhaber, B. Eisenhaber, G. Grüber, 2016, Journal of structural biology.

Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol.

G. Grüber, A. M. Balakrishna, Arvind Kumar, 2016, Free radical biology & medicine.

Pyrazinoic Acid Inhibits Mycobacterial Coenzyme A Biosynthesis by Binding to Aspartate Decarboxylase PanD.

G. Grüber, T. Dick, V. Dartois, 2017, ACS infectious diseases.

Atomic structure and enzymatic insights into the vancomycin‐resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C

G. Grüber, S. Bhushan, A. M. Balakrishna, 2018, Free radical biology & medicine.

Crystallographic and solution structure of the N‐terminal domain of the Rel protein from Mycobacterium tuberculosis

G. Grüber, J. Jeyakanthan, A. M. Balakrishna, 2017, FEBS letters.

Key roles of the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress.

F. Eisenhaber, V. Kostyuchenko, T. Ng, 2014, Biochimica et biophysica acta.

Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli.

F. Eisenhaber, B. Eisenhaber, G. Grüber, 2014, Acta crystallographica. Section D, Biological crystallography.

Crystallographic and solution studies of NAD(+)- and NADH-bound alkylhydroperoxide reductase subunit F (AhpF) from Escherichia coli provide insight into sequential enzymatic steps.

F. Eisenhaber, B. Eisenhaber, G. Grüber, 2015, Biochimica et biophysica acta.

Structural and mechanistic insights into Mycothiol Disulphide Reductase and the Mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis.

G. Grüber, Joon Shin, Arvind Kumar, 2017, Biochimica et biophysica acta. General subjects.

NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2‐Cys peroxiredoxin machinery

F. Eisenhaber, G. Wagner, B. Eisenhaber, 2015, The FEBS journal.

Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ.

P. Bond, G. Grüber, S. Bhushan, 2019, Journal of structural biology.

NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2‐Cys peroxiredoxin machinery

F. Eisenhaber, G. Wagner, B. Eisenhaber, 2015, The FEBS journal.

Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli.

F. Eisenhaber, B. Eisenhaber, G. Grüber, 2014, Acta crystallographica. Section D, Biological crystallography.

Cryo-EM structure of DDM1-HELLS chimera bound to nucleosome reveals a mechanism of chromatin remodeling and disease regulation

A. A. Goodarzi, W. Nartey, Gareth J. Williams, 2023, bioRxiv.