F. Löhr

发表

Probing metallo-β-lactamases with molecular fragments identified by consensus docking.

V. Dötsch, Franca-Maria Klingler, Daniel Moser, 2015, Bioorganic & medicinal chemistry letters.

Self-consistent 3J coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles

F. Löhr, J. Schmidt, M. Blümel, 1999, Journal of biomolecular NMR.

Solution structure and stability of the full-length excisionase from bacteriophage HK022.

Primoz Pristovsek, Heinz Rüterjans, F. Löhr, 2003, European journal of biochemistry.

Structural insights into Rcs phosphotransfer: the newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB.

Peter Güntert, Volker Dötsch, Frank Bernhard, 2011, Structure.

Nix is a selective autophagy receptor for mitochondrial clearance

Ivan Dikic, Volker Dötsch, Philipp Wild, 2010, EMBO reports.

Insights into Cotranslational Membrane Protein Insertion by Combined LILBID-Mass Spectrometry and NMR Spectroscopy.

V. Dötsch, F. Löhr, N. Morgner, 2017, Analytical chemistry.

COMPUTATIONAL TOOLS FOR AIRCRAFT SYSTEM ANALYSIS AND OPTIMIZATION

J. Palmberg, F. Löhr, 2008 .

Self-consistent Karplus parametrization of 3J couplings depending on the polypeptide side-chain torsion chi1.

F. Löhr, J. Schmidt, H. Rüterjans, 2001, Journal of the American Chemical Society.

H2NCO-E.COSY, a simple method for the sterospecific assignment of side-chain amide protons in proteins.

F. Löhr, H. Rüterjans, 1997, Journal of magnetic resonance.

High level cell-free expression and specific labeling of integral membrane proteins.

Heinz Rüterjans, Volker Dötsch, Birgit Schäfer, 2004, European journal of biochemistry.

Allosteric modulation of the farnesoid X receptor by a small molecule

M. Schubert-Zsilavecz, F. Löhr, E. Proschak, 2018, Scientific Reports.

1H, 13C and 15N assignment of stem-loop SL1 from the 5'-UTR of SARS-CoV-2

H. Schwalbe, B. Fürtig, C. Richter, 2021, Biomolecular NMR Assignments.

Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy

K. Saxena, H. Schwalbe, B. Fürtig, 2020, Nucleic acids research.

Correlation of backbone amide and side-chain (13)C resonances in perdeuterated proteins.

F. Löhr, H. Rüterjans, 2002, Journal of magnetic resonance.

Detection of Nitrogen–NitrogenJ-Couplings in Proteins

F. Löhr, H. Rüterjans, 1998 .

HNCCH-TOCSY, a triple resonance experiment for the correlation of backbone 13Cα and 15N resonances with aliphatic side-chain proton resonances and for measuring vicinal 13CO, 1Hβ coupling constants in proteins

F. Löhr, H. Rüterjans, R. Weisemann, 1994, Journal of biomolecular NMR.

Cofactor‐Apoprotein Hydrogen Bonding in Oxidized and Fully Reduced Flavodoxin Monitored by Trans‐Hydrogen‐Bond Scalar Couplings

F. Löhr, H. Rüterjans, S. Mayhew, 2004, Chembiochem : a European journal of chemical biology.

HNCAN pulse sequences for sequential backbone resonance assignment across proline residues in perdeuterated proteins

F. Löhr, H. Rüterjans, S. Pfeiffer, 2000, Journal of biomolecular NMR.

A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins

F. Löhr, H. Rüterjans, 1995, Journal of biomolecular NMR.

(H)NCAHA and (H)CANNH experiments for the determination of vicinal coupling constants related to the ϕ-torsion angle

Heinz Rüterjans, F. Löhr, H. Rüterjans, 1995 .

A Cost-effective Amino-acid-type Selective Isotope Labeling of Proteins Expressed in Leishmania tarentolae

V. Dötsch, F. Löhr, J. Lukeš, 2009, Journal of biomolecular structure & dynamics.

Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis.

V. Dötsch, F. Löhr, F. Bernhard, 2018, Progress in nuclear magnetic resonance spectroscopy.

Precursor-Based Selective Methyl Labeling of Cell-Free Synthesized Proteins.

V. Dötsch, F. Löhr, F. Bernhard, 2018, ACS chemical biology.

The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking.

S. Arold, F. Löhr, C. Roumestand, 2008, Journal of molecular biology.

Automated resonance assignment of the 21kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA.

P. Güntert, F. Löhr, M. Kainosho, 2014, Journal of magnetic resonance.

Letter to the Editor: Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state

F. Löhr, H. Rüterjans, C. Lücke, 2000 .

Ubiquitination in the ERAD Process

V. Dötsch, F. Löhr, V. Rogov, 2020, International journal of molecular sciences.

1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e

K. Saxena, H. Schwalbe, B. Fürtig, 2020, Biomolecular NMR assignments.

Structural Analysis of the DNA-binding Domain of theErwinia amylovora RcsB Protein and Its Interaction with the RcsAB Box*

Primoz Pristovsek, Kaushik Sengupta, Heinz Rüterjans, 2003, The Journal of Biological Chemistry.

Long-range nature of the interactions between titratable groups in Bacillus agaradhaerens family 11 xylanase: pH titration of B. agaradhaerens xylanase.

F. Löhr, H. Rüterjans, H. Wienk, 2004, Biochemistry.

Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes.

M. Nilges, F. Löhr, H. Rüterjans, 2004, Biochemistry.

An extended combinatorial 15N, 13Cα, and $$ ^{13} {\text{C}}^{\prime } $$13C′ labeling approach to protein backbone resonance assignment

V. Dötsch, F. Löhr, Franz Tumulka, 2015, Journal of biomolecular NMR.

Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment

V. Dötsch, F. Löhr, F. Bernhard, 2012, Journal of biomolecular NMR.

Efficient Measurement of 3JN,Cγ and 3JC′,Cγ Coupling Constants of Aromatic Residues in 13C, 15N-Labeled Proteins

F. Löhr, H. Rüterjans, 2000 .

Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7.

C. Walsh, Elizabeth M. Nolan, F. Löhr, 2008, Journal of the American Chemical Society.

The structure of the cytochrome p450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography.

Wei-Min Liu, H. Schwalbe, F. Löhr, 2013, Journal of molecular biology.

Gradient-purged isotope filter experiments for the detection of bound water in proteins

R. Boelens, F. Löhr, H. Rüterjans, 1999 .

A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1

V. Dötsch, F. Löhr, V. Rogov, 2021, International journal of molecular sciences.

An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5

P. Güntert, V. Dötsch, F. Löhr, 2020, Autophagy.

Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.

H. Schwalbe, C. Richter, F. Löhr, 2020, Journal of the American Chemical Society.

Binding Adaptation of GS-441524 Diversifies Macro Domains and Downregulates SARS-CoV-2 de-MARylation Capacity

H. Schwalbe, C. Richter, F. Löhr, 2022, Journal of Molecular Biology.

The cytochrome c peroxidase and cytochrome c encounter complex: The other side of the story

H. Schwalbe, F. Löhr, M. Ubbink, 2014, FEBS letters.

Construction and performance of an NMR tube with a sample cavity formed within magnetic susceptibility-matched glass.

J. Markley, F. Löhr, M. Kainosho, 2011, Journal of magnetic resonance.

Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification.

Peter Güntert, Ivan Dikic, Volker Dötsch, 2014, Chemistry & biology.

Lipid Conversion by Cell-Free Synthesized Phospholipid Methyltransferase Opi3 in Defined Nanodisc Membranes Supports an in Trans Mechanism.

V. Dötsch, F. Löhr, N. Morgner, 2018, Biochemistry.

Mechanism of inhibition of TAp73 by ΔNp63 and structural basis of p63/p73 hetero-tetramerization

S. Knapp, P. Güntert, E. Salah, 2016 .

Fast Automated NMR Spectroscopy of Short‐Lived Biological Samples

P. Güntert, V. Dötsch, F. Löhr, 2012, ChemBioChem.

In‐Cell Solid‐State NMR as a Tool to Study Proteins in Large Complexes

V. Dötsch, F. Löhr, C. Glaubitz, 2012, Chembiochem : a European journal of chemical biology.

In‐Cell NMR Spectroscopy

Volker Dötsch, V. Dötsch, F. Löhr, 2005, Methods in enzymology.

Structural and functional analysis of the GABARAP interaction motif (GIM)

V. Dötsch, F. Löhr, I. Dikic, 2016, bioRxiv.

High-resolution insight into G-overhang architecture.

V. Dötsch, F. Löhr, L. Trantírek, 2013, Journal of the American Chemical Society.

The Apo-structure of the Low Molecular Weight Protein-tyrosine Phosphatase A (MptpA) from Mycobacterium tuberculosis Allows for Better Target-specific Drug Development*

K. Saxena, H. Schwalbe, C. Richter, 2012, The Journal of Biological Chemistry.

From nanodiscs to isotropic bicelles: a procedure for solution NMR studies of detergent sensitive integral membrane proteins

F. Löhr, E. Perozo, F. Bernhard, 2016 .

Structural Investigation of Cell‐Free Expressed Membrane Proteins

V. Dötsch, F. Löhr, F. Bernhard, 2012 .

Strategies for the cell-free expression of membrane proteins.

V. Dötsch, F. Löhr, F. Bernhard, 2010, Methods in molecular biology.

Binding Adaptation of GS-441524 Diversifies Macro Domains and Down- Capacity

H. Schwalbe, C. Richter, F. Löhr, 2022 .

1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b

K. Saxena, H. Schwalbe, B. Fürtig, 2020, Biomolecular NMR Assignments.

Letter to the Editor: Complete 1H, 15N and 13C assignment of a recombinant mouse major urinary protein

F. Löhr, H. Rüterjans, C. Lücke, 1999, Journal of biomolecular NMR.

Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy

J. Ferrell, V. Dötsch, G. Wagner, 2006, Nature Protocols.

NMR studies reveal the role of biomembranes in modulating ligand binding and release by intracellular bile acid binding proteins.

V. Dötsch, F. Löhr, M. Assfalg, 2009, Journal of molecular biology.

An extended combinatorial 15 N, 13 C a , and 13 C 0 labeling approach to protein backbone resonance assignment

V. Dötsch, F. Löhr, Franz Tumulka, 2015 .

Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment

V. Dötsch, F. Löhr, F. Bernhard, 2012, Journal of Biomolecular NMR.

Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 37 kDa surface antigen protein Bd37 from Babesia divergens

M. Strub, F. Löhr, C. Roumestand, 2005, Journal of biomolecular NMR.

Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase

A. Gavin, P. Güntert, O. Hantschel, 2017, Nature Communications.

Characterization of molecular interactions between ACP and halogenase domains in the Curacin A polyketide synthase.

P. Güntert, C. Walsh, V. Dötsch, 2012, ACS chemical biology.

Detection of Scalar Couplings Across NH···OP and OH···OP Hydrogen Bonds in a Flavoprotein

F. Löhr, H. Rüterjans, and Stephen G. Mayhew, 2000 .

1H, 13C and 15N resonance assignment of the cytosolic dithiol glutaredoxin 1 from the pathogen Trypanosoma brucei

M. Sturlese, F. Löhr, M. Bellanda, 2016, Biomolecular NMR assignments.

Structural basis for the selectivity of the external thioesterase of the surfactin synthetase

P. Güntert, M. Marahiel, C. Walsh, 2008, Nature.

Labeling of membrane proteins by cell-free expression.

V. Dötsch, F. Löhr, F. Bernhard, 2015, Methods in enzymology.

The Electron Transfer Complex between Cytochrome c552 and the CuA Domain of the Thermus thermophilus ba3 Oxidase

F. Löhr, H. Rüterjans, Lucia Muresanu, 2006, Journal of Biological Chemistry.

Triple-Resonance Methods for Complete Resonance Assignment of Aromatic Protons and Directly Bound Heteronuclei in Histidine and Tryptophan Residues

V. Dötsch, F. Löhr, V. Rogov, 2005, Journal of biomolecular NMR.

Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy

V. Dötsch, F. Löhr, S. Reckel, 2011, Journal of biomolecular NMR.

Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies

H. Schwalbe, V. Dötsch, F. Löhr, 2012, Journal of Biomolecular NMR.

Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies

H. Schwalbe, V. Dötsch, F. Löhr, 2012, Journal of biomolecular NMR.

Small-molecule binding sites on proteins established by paramagnetic NMR spectroscopy.

Harald Schwalbe, Gregg Siegal, Simon P. Skinner, 2013, Journal of the American Chemical Society.

Variation in protein Cα‐related one‐bond J couplings

F. Löhr, M. Howard, C. Pérez, 2009, Magnetic resonance in chemistry : MRC.

Dynamics of Bacteriorhodopsin in the Dark‐Adapted State from Solution Nuclear Magnetic Resonance Spectroscopy

P. Güntert, B. Fürtig, F. Löhr, 2020, Angewandte Chemie.

Heteronuclear relayed E.COSY revisited: Determination of 3J(Hα,Cγ) couplings in Asx and aromatic residues in proteins

F. Löhr, C. Pérez, Jürgen M. Schmidt, 2000, Journal of biomolecular NMR.

Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1.

P. Güntert, V. Dötsch, F. Löhr, 2011, Journal of molecular biology.

Structural basis for phosphorylation-triggered autophagic clearance of Salmonella.

P. Güntert, V. Dötsch, F. Löhr, 2013, The Biochemical journal.

A Universal Expression Tag for Structural and Functional Studies of Proteins

P. Güntert, V. Dötsch, F. Löhr, 2012, Chembiochem : a European journal of chemical biology.

p63 uses a switch-like mechanism to set the threshold for induction of apoptosis

G. Hummer, S. Knapp, F. Pampaloni, 2020, Nature Chemical Biology.

Tracing the protectors path from the germ line to the genome

V. Dötsch, F. Löhr, D. Coutandin, 2010, Proceedings of the National Academy of Sciences.

Characterization of a natural variant of human NDP52 and its functional consequences on mitophagy

E. Papaleo, V. Dötsch, F. Löhr, 2021, Cell Death & Differentiation.

Solution structure of a recombinant mouse major urinary protein.

F. Löhr, H. Rüterjans, L. Franzoni, 1999, European journal of biochemistry.

1H, 13C, and 15N resonance assignments for the CTD-interacting domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA polymerase II

R. Stefl, F. Löhr, K. Kubícek, 2011, Biomolecular NMR assignments.

Structural evolution of C‐terminal domains in the p53 family

V. Dötsch, V. Vogel, W. Mäntele, 2007, The EMBO journal.

The parallel G-quadruplex structure of vertebrate telomeric repeat sequences is not the preferred folding topology under physiological conditions

E. Bamberg, V. Dötsch, F. Löhr, 2011, Nucleic acids research.

Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme.

G. Fritzsch, J. Koepke, F. Löhr, 2005, Biochemistry.

Refined NMR solution structures of proteins using homo- and heteronuclear couplings, relaxation time measurements and relaxation matrix analysis

F. Löhr, J. Schmidt, M. Blümel, 1996 .

Structural Basis for Tail-Anchored Membrane Protein Biogenesis by the Get3-Receptor Complex

Vladimir Denic, V. Dötsch, F. Löhr, 2011, Science.

Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL

Lars V. Schäfer, G. Hummer, R. Tampé, 2018, Scientific Reports.

Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR

V. Dötsch, F. Löhr, F. Bernhard, 2013, Journal of biomolecular NMR.

Comprehensive Fragment Screening of the SARS‐CoV‐2 Proteome Explores Novel Chemical Space for Drug Development

D. Laurents, J. Hoch, K. Saxena, 2022, Angewandte Chemie.

Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy.

E. Bamberg, H. Schwalbe, V. Dötsch, 2009, Journal of the American Chemical Society.

A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains.

V. Dötsch, F. Löhr, V. Rogov, 2006, Journal of molecular biology.

Dynein Binding of Competitive Regulators Dynactin and NudE Involves Novel Interplay between Phosphorylation Site and Disordered Spliced Linkers.

F. Löhr, E. Barbar, J. Jie, 2017, Structure.

Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR

V. Dötsch, F. Löhr, F. Bernhard, 2013, Journal of Biomolecular NMR.

Backbone dynamics of oxidized and reduced D. vulgaris flavodoxin in solution

F. Löhr, M. Blümel, S. Mayhew, 1997, Journal of biomolecular NMR.

A Disulfide Bridge Network within the Soluble Periplasmic Domain Determines Structure and Function of the Outer Membrane Protein RCSF*

V. Dötsch, F. Löhr, V. Rogov, 2011, The Journal of Biological Chemistry.

Structure and Biosynthesis of Fimsbactins A–F, Siderophores from Acinetobacter baumannii and Acinetobacter baylyi

F. Löhr, H. Bode, Peter Grün, 2013, Chembiochem : a European journal of chemical biology.

Cell‐free expression as an emerging technique for the large scale production of integral membrane protein

V. Dötsch, F. Löhr, F. Bernhard, 2006, The FEBS journal.

Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution

F. Löhr, H. Rüterjans, N. Spitzner, 1998, Journal of biomolecular NMR.

Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization

S. Knapp, P. Güntert, E. Salah, 2016, Cell Death and Differentiation.

Bovine β‐lactoglobulin: Interaction studies with palmitic acid

F. Löhr, H. Rüterjans, H. Molinari, 2000, Protein science : a publication of the Protein Society.

The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63‐branched ubiquitin chains

M. Selbach, V. Dötsch, F. Löhr, 2021, The EMBO journal.

Towards complete polypeptide backbone NH assignment via combinatorial labeling.

V. Dötsch, F. Löhr, Christopher Hein, 2019, Journal of magnetic resonance.

Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments.

V. Dötsch, F. Löhr, F. Bernhard, 2019, Methods in enzymology.

Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study

V. Dötsch, F. Löhr, Christopher Hein, 2017, Biopolymers.

In-cell NMR spectroscopy.

V. Dötsch, F. Löhr, S. Reckel, 2007, Chembiochem : a European journal of chemical biology.

The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation.

P. Güntert, V. Dötsch, F. Löhr, 2016, Molecular cell.

The CUE Domain of Cue 1 Aligns Growing Ubiquitin Chains with Ubc 7 for Rapid Elongation Graphical Abstract Highlights

P. Güntert, V. Dötsch, F. Löhr, 2016 .

Interactions of Yeast Dynein with Dynein Light Chain and Dynactin

F. Löhr, E. Barbar, J. Jie, 2015, The Journal of Biological Chemistry.

NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules.

F. Löhr, M. Blümel, H. Rüterjans, 1996, European journal of biochemistry.

Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio vulgaris flavodoxin. Sequential assignments and identification of secondary structure elements.

G. Curley, F. Löhr, H. Rüterjans, 1993, European journal of biochemistry.

Conformational Switches Modulate Protein Interactions in Peptide Antibiotic Synthetases

M. Marahiel, V. Dötsch, F. Löhr, 2006, Science.

Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition.

Donata K. Kirchner, P. Güntert, V. Dötsch, 2013, Journal of the American Chemical Society.

A strategy to obtain backbone resonance assignments of deuterated proteins in the presence of incomplete amide 2H/1H back-exchange

U. Günther, F. Löhr, H. Rüterjans, 2003, Journal of biomolecular NMR.

1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein

H. Schwalbe, B. Fürtig, C. Richter, 2020, Biomolecular NMR Assignments.

Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains.

V. Dötsch, F. Löhr, V. Rogov, 2004, Journal of molecular biology.

Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism.

F. Löhr, H. Rüterjans, J. Chen, 2006, Journal of the American Chemical Society.

Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins

V. Dötsch, F. Löhr, V. Rogov, 2007, Journal of biomolecular NMR.

Exploring the chemical space of multitarget ligands using aligned self-organizing maps.

Daniel Moser, Janosch Achenbach, Ewgenij Proschak, 2013, ACS medicinal chemistry letters.

Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications

Rachel W. Martin, D. Laurents, J. Hoch, 2021, Frontiers in Molecular Biosciences.

Design, Synthesis, and Evaluation of WD-Repeat-Containing Protein 5 (WDR5) Degraders.

B. Kuster, S. Knapp, C. Sotriffer, 2021, Journal of medicinal chemistry.

Design, Synthesis and Evaluation of WD-repeat containing protein 5 (WDR5) degraders

B. Kuster, S. Knapp, C. Sotriffer, 2021, bioRxiv.

Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs

P. Güntert, F. Löhr, O. Zerbe, 2019, Journal of Biomolecular NMR.

Application of H(N)CA,CO-E.COSY experiments for calibrating the φ angular dependences of vicinal couplings J(C′i−1,Hiα), J(C′i−1,Ciβ) and J(C′i−1,C′i) in proteins

F. Löhr, M. Blümel, H. Rüterjans, 1997 .

Heteronuclear relayed E.COSY applied to the determination of accurate 3J(HN,C′) and 3J(Hβ,C′) coupling constants in Desulfovibrio vulgaris flavodoxin

Heinz Rüterjans, F. Löhr, H. Rüterjans, 1996, Journal of biomolecular NMR.

Alternative E.COSY techniques for the measurement of 3J(Ci′−1,Ciβ) and 3J(HiN,Ciβ) coupling constants in proteins

F. Löhr, H. Rüterjans, 1999, Journal of biomolecular NMR.

Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications.

F. Löhr, V. Gervais, A. Milon, 2009, Journal of molecular biology.

Regulation of the Activity in the p53 Family Depends on the Organization of the Transactivation Domain.

J. Koch, P. Güntert, V. Dötsch, 2018, Structure.

Regulation of the Activity i n the p 53 Family Depends on the Organization of the Transactivation Domain Graphical

J. Koch, V. Dötsch, F. Löhr, 2022 .

Correlation of 2J couplings with protein secondary structure

F. Löhr, Jürgen M. Schmidt, Yixun Hua, 2010, Proteins.

Time-shared experiments for efficient assignment of triple-selectively labeled proteins.

V. Dötsch, F. Löhr, P. Connolly, 2014, Journal of magnetic resonance.

Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.

F. Löhr, H. Rüterjans, H. Wienk, 2003, Biochemistry.

Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Soluble Domain of the ba3 Oxidase Subunit II of Thermus Thermophilus in the Reduced State

F. Löhr, H. Rüterjans, B. Ludwig, 2004, Journal of biomolecular NMR.

Sequence-specific assignment of histidine and tryptophan ring 1H, 13C and 15N resonances in 13C/15N- and 2H/13C/15N-labelled proteins

F. Löhr, H. Rüterjans, J. Hartleib, 2002, Journal of biomolecular NMR.

Transmembrane segment enhanced labeling as a tool for the backbone assignment of α-helical membrane proteins

P. Güntert, V. Dötsch, F. Löhr, 2008, Proceedings of the National Academy of Sciences.

Ionization properties of titratable groups in ribonuclease T1

F. Löhr, H. Rüterjans, A. Karshikoff, 2001, European Biophysics Journal.

Solution NMR structure of proteorhodopsin.

H. Schwalbe, P. Güntert, V. Dötsch, 2011, Angewandte Chemie.

Improved Measurement of 3J(Hαi, Ni+1) Coupling Constants in H2O Dissolved Proteins

F. Löhr, H. Rüterjans, Jürgen M. Schmidt, 2001 .

Structural investigation of the C-terminal catalytic fragment of presenilin 1

Peter Güntert, Slawomir Filipek, Volker Dötsch, 2010, Proceedings of the National Academy of Sciences.

A General Model for Preferential Hetero-oligomerization of LIN-2/7 Domains

W. Lim, V. Dötsch, F. Löhr, 2005, Journal of Biological Chemistry.

Cell-free expression and stable isotope labelling strategies for membrane proteins

V. Dötsch, F. Löhr, F. Bernhard, 2010, Journal of biomolecular NMR.

NMR studies of flavoproteins.

F. Lederer, F. Löhr, M. Blümel, 1996, Biochemical Society transactions.

Combination of cell‐free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins

Volker Dötsch, Birgit Schäfer, Frank Bernhard, 2006, Magnetic resonance in chemistry : MRC.

Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies.

V. Dötsch, F. Löhr, F. Bernhard, 2007, Methods.

Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [15N,1H]-TROSY-HNC experiment

F. Löhr, H. Rüterjans, H. Wienk, 2003, Journal of biomolecular NMR.

V. Dötsch, F. Löhr, C. Missero, 2023, Cell death & disease.

Novel Pulse Sequences for the Resonance Assignment of Aromatic Side Chains in13C-Labeled Proteins

F. Löhr, H. Rüterjans, 1996 .

From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins.

V. Dötsch, F. Löhr, E. Perozo, 2016, Structure.

Small-molecule binding sites on proteins established by paramagnetic NMR spectroscopy.

H. Schwalbe, G. Siegal, P. Keizers, 2013, Journal of the American Chemical Society.

A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.

Primoz Pristovsek, Heinz Rüterjans, Frank Hannemann, 2002, Biochemistry.

Structural features of LC8-induced self-association of swallow.

F. Löhr, E. Barbar, M. Hare, 2013, Biochemistry.

Simultaneous Measurement of 3JHN,Hα and 3JHα,Hβ Coupling Constants in 13C,15N-Labeled Proteins

F. Löhr, H. Rüterjans, A. Schmidt, 1999 .

Correlation of 2J couplings with protein secondary structure

F. Löhr, Jürgen M. Schmidt, Yixun Hua, 2010, Proteins.

Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study

V. Dötsch, F. Löhr, Christopher Hein, 2017, Biopolymers.

Refinement of Protein Tertiary Structure by Using Spin-Spin Coupling Constants from Nuclear Magnetic Resonance Measurements

F. Löhr, Jürgen M. Schmidt, 2012 .

Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy.

E. Bamberg, H. Schwalbe, V. Dötsch, 2009, Journal of the American Chemical Society.

High-resolution insight into G-overhang architecture.

V. Dötsch, F. Löhr, L. Trantírek, 2013, Journal of the American Chemical Society.

Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain

H. Schwalbe, V. Dötsch, F. Löhr, 2016, Protein science : a publication of the Protein Society.

One‐bond and two‐bond j couplings help annotate protein secondary‐structure motifs: J‐coupling indexing applied to human endoplasmic reticulum protein ERp18

F. Löhr, M. Howard, R. Williamson, 2011, Proteins.

Efficient strategy for the rapid backbone assignment of membrane proteins.

Volker Dötsch, Frank Bernhard, V. Dötsch, 2005, Journal of the American Chemical Society.

E. coli “Stablelabel” S30 lysate for optimized cell-free NMR sample preparation

V. Dötsch, F. Löhr, F. Bernhard, 2023, Journal of Biomolecular NMR.