Search Results - "Zögg, Thomas"
-
1
The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier
Published in Cell (24-01-2019)“…Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open…”
Get full text
Journal Article -
2
Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM
Published in Nature methods (01-01-2021)“…Nanobodies are popular and versatile tools for structural biology. They have a compact single immunoglobulin domain organization, bind target proteins with…”
Get full text
Journal Article -
3
Allosteric nanobodies to study the interactions between SOS1 and RAS
Published in Nature communications (23-07-2024)“…Protein-protein interactions (PPIs) are central in cell metabolism but research tools for the structural and functional characterization of these PPIs are…”
Get full text
Journal Article -
4
An improved yeast surface display platform for the screening of nanobody immune libraries
Published in Scientific reports (23-01-2019)“…Fusions to the C-terminal end of the Aga2p mating adhesion of Saccharomyces cerevisiae have been used in many studies for the selection of affinity reagents by…”
Get full text
Journal Article -
5
Structural Basis of the Cofactor- and Substrate-Assisted Activation of Human Coagulation Factor IXa
Published in Structure (London) (09-12-2009)“…Human coagulation factor IX serves both to maintain and to control blood coagulation. The dual function of this hemophilic factor is implemented by a tiered…”
Get full text
Journal Article -
6
Structural basis of purine nucleotide inhibition of human uncoupling protein 1
Published in Science advances (02-06-2023)“…Mitochondrial uncoupling protein 1 (UCP1) gives brown adipose tissue of mammals its specialized ability to burn calories as heat for thermoregulation. When…”
Get full text
Journal Article -
7
Maturation of coagulation factor IX during Xase formation as deduced using factor VIII‐derived peptides
Published in FEBS open bio (01-08-2019)“…Blood coagulation involves extrinsic and intrinsic pathways, which merge at the activation step of blood coagulation factor X to factor Xa. This step is…”
Get full text
Journal Article -
8
Crystal Structures of the Viral Protease Npro Imply Distinct Roles for the Catalytic Water in Catalysis
Published in Structure (London) (04-06-2013)“…Npro is a key effector protein of pestiviruses such as bovine viral diarrhea virus and abolishes host cell antiviral defense mechanisms. Synthesized as the…”
Get full text
Journal Article -
9
A biosensor-based phage display selection method for automated, high-throughput Nanobody discovery
Published in Biosensors & bioelectronics (01-11-2024)Get full text
Journal Article -
10
The structural mechanism of transport by the mitochondrial ADP/ATP carrier
Published in Biochimica et biophysica acta. Bioenergetics (01-09-2018)Get full text
Journal Article -
11
The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers
Published in Scientific reports (27-09-2016)“…Proprotein Convertases (PCs) represent highly selective serine proteases that activate their substrates upon proteolytic cleavage. Their inhibition is a…”
Get full text
Journal Article -
12
Activation mechanisms of coagulation factor IX
Published in Biological chemistry (01-05-2009)“…Blood haemostasis is accomplished by a complex network of coagulatory and fibrinolytic processes. These processes have to be delicately balanced, as clinically…”
Get more information
Journal Article -
13
Complex Assemblies of Factors IX and X Regulate the Initiation, Maintenance, and Shutdown of Blood Coagulation
Published in Progress in Molecular Biology and Translational Science (2011)“…Blood hemostasis is accomplished by a complex network of (anti-)coagulatory and fibrinolytic processes. These physiological processes are implemented by the…”
Get full text
Book Chapter Journal Article -
14
Npro autoprotease fusion technology (NAFT), a platform for industrial peptide/protein production in E. coli
Published in New biotechnology (23-09-2012)“…The human enterobacterium Escherichia coli is still one of the most used hosts for protein/peptide production in industry because of the advantage of short…”
Get full text
Journal Article