Ute Lindenstrauss

发表

HypD is the scaffold protein for Fe-(CN)2CO cofactor assembly in [NiFe]-hydrogenase maturation.

R. Sawers, D. Nies, J. Heberle, 2013, Biochemistry.

The [NiFe]‐hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron‐ and carbon dioxide‐binding proteins

R. Sawers, J. Heberle, M. Herzberg, 2013, FEBS letters.

[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.

M. Herzberg, S. Stripp, Basem Soboh, 2014, The Biochemical journal.

Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl–Group Channeling during [NiFe]–Hydrogenase Cofactor Generation

R. Sawers, S. Stripp, Basem Soboh, 2015, PloS one.

The Influence of Oxygen on [NiFe]–Hydrogenase Cofactor Biosynthesis and How Ligation of Carbon Monoxide Precedes Cyanation

R. Sawers, S. Stripp, Basem Soboh, 2014, PloS one.

Conservation and Variation between Rhodobacter capsulatus and Escherichia coli Tat Systems

T. Brüser, Ute Lindenstrauss, 2006, Journal of bacteriology.

Ute Lindenstrauß and Thomas Brüser Tat Systems coli Escherichia and Rhodobacter capsulatus Conservation and Variation between

T. Brüser, Ute Lindenstrauss, 2006 .

Topological studies on the twin-arginine translocase component TatC.

T. Brüser, Ute Lindenstrauss, Kerstin Standar, 2004, FEMS microbiology letters.

Recombinant Expression of tatABC and tatAC Results in the Formation of Interacting Cytoplasmic TatA Tubes in Escherichia coli*

G. Hause, H. Lünsdorf, T. Brüser, 2008, Journal of Biological Chemistry.

Dissection of the Hydrogen Metabolism of the Enterobacterium Trabulsiella guamensis: Identification of a Formate-Dependent and Essential Formate Hydrogenlyase Complex Exhibiting Phylogenetic Similarity to Complex I

Ute Lindenstrauss, C. Pinske, Constanze Pinske, 2019, bioRxiv.

The TatBC complex formation suppresses a modular TatB‐multimerization in Escherichia coli

T. Brüser, Ute Lindenstrauss, J. Behrendt, 2007, FEBS letters.

YcdB from Escherichia coli Reveals a Novel Class of Tat-dependently Translocated Hemoproteins*

H. Lilie, T. Brüser, Ute Lindenstrauss, 2006, Journal of Biological Chemistry.

Metabolic Deficiences Revealed in the Biotechnologically Important Model Bacterium Escherichia coli BL21(DE3)

R. Sawers, S. Krüger, Markus Bönn, 2011, PloS one.

The N‐terminal domains of the paralogous HycE and NuoCD govern assembly of the respective formate hydrogenlyase and NADH dehydrogenase complexes

T. Friedrich, Ute Lindenstrauss, Christian Blumenscheit, 2020, FEBS open bio.

The dual-function chaperone HycH improves assembly of the formate hydrogenlyase complex.

F. Sargent, J. McDowall, Ute Lindenstrauss, 2017, The Biochemical journal.

Malfolded recombinant Tat substrates are Tat‐independently degraded in Escherichia coli

T. Brüser, Ute Lindenstrauss, C. F. Matos, 2010, FEBS letters.

Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins*

R. Bayliss, T. Brüser, Ute Lindenstrauss, 2007, Journal of Biological Chemistry.

Structural studies on a twin‐arginine signal sequence

C. Griesinger, H. Lilie, T. Carlomagno, 2003, FEBS letters.

Tat transport of linker-containing proteins in Escherichia coli.

T. Brüser, Ute Lindenstrauss, 2009, FEMS microbiology letters.