High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

Controlling and quantifying protein concentration in Escherichia coli

(2019) Shannon L. Speer et al.   PROTEIN SCIENCE

Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

(2019) Julia C. Heiby et al.   Nature Communications

A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein

(2018) Médoune Sarr et al.   FEBS Journal

Estimating Interprotein Pairwise Interaction Energies in Cell Lysates from a Single Native Mass Spectrum

(2018) Jelena Cveticanin et al.   ANALYTICAL CHEMISTRY

Hierarchical spidroin micellar nanoparticles as the fundamental precursors of spider silks

(2018) Lucas R. Parent et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Biomimetic spinning of artificial spider silk from a chimeric minispidroin

(2017) Marlene Andersson et al.   Nature Chemical Biology

Physicochemical code for quinary protein interactions inEscherichia coli

(2017) Xin Mu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Efficient protein production inspired by how spiders make silk

(2017) Nina Kronqvist et al.   Nature Communications

Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle

(2016) Yue Lu et al.   BIOCHEMISTRY

The formation, function and regulation of amyloids: insights from structural biology

(2016) M. Landreh et al.   JOURNAL OF INTERNAL MEDICINE

Microsecond Folding and Domain Motions of a Spider Silk Protein Structural Switch

(2014) Julia Ries et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Residue level quantification of protein stability in living cells

(2014) W. B. Monteith et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

(2014) Nina Kronqvist et al.   Nature Communications

Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains

(2014) Marlene Andersson et al.   PLOS BIOLOGY

The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening

(2013) Simone Schwarze et al.   Nature Communications

Control of amyloid assembly by autoregulation

(2012) Michael Landreh et al.   BIOCHEMICAL JOURNAL

pH‐Dependent Dimerization of Spider Silk N-Terminal Domain Requires Relocation of a Wedged Tryptophan Side Chain

(2012) Kristaps Jaudzems et al.   JOURNAL OF MOLECULAR BIOLOGY

Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation

(2011) Poh K. Teng et al.   PROTEIN SCIENCE

Hydrogen exchange mass spectrometry: what is it and what can it tell us?

(2010) Sean R. Marcsisin et al.   ANALYTICAL AND BIOANALYTICAL CHEMISTRY

pH-Dependent Dimerization and Salt-Dependent Stabilization of the N-terminal Domain of Spider Dragline Silk-Implications for Fiber Formation

(2010) Franz Hagn et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly

(2010) William A. Gaines et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A pH-Dependent Dimer Lock in Spider Silk Protein

(2010) Michael Landreh et al.   JOURNAL OF MOLECULAR BIOLOGY

Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

(2010) Glareh Askarieh et al.   NATURE

A conserved spider silk domain acts as a molecular switch that controls fibre assembly

(2010) Franz Hagn et al.   NATURE

Identifying the amylome, proteins capable of forming amyloid-like fibrils

(2010) Lukasz Goldschmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Biology of Amyloid: Structure, Function, and Regulation

(2010) Jason Greenwald et al.   STRUCTURE

H/D Exchange and Mass Spectrometry in the Studies of Protein Conformation and Dynamics: Is There a Need for a Top-Down Approach?

(2009) Igor A. Kaltashov et al.   ANALYTICAL CHEMISTRY

A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide

(2009) Dominic M. Walsh et al.   FEBS Journal

Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling

(2009) Rinat R. Abzalimov et al.   JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY

Amyloid formation by globular proteins under native conditions

(2008) Fabrizio Chiti et al.   Nature Chemical Biology

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

(2008) Lei Wang et al.   PLOS BIOLOGY