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

The role of salt and shear on the storage and assembly of spider silk proteins

(2010) Lukas Eisoldt et al.   JOURNAL OF STRUCTURAL 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

An Engineered Spider Silk Protein Forms Microspheres

(2008) Ute K. Slotta et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Structural Properties of Recombinant Nonrepetitive and Repetitive Parts of Major Ampullate Spidroin 1 fromEuprosthenops australis: Implications for Fiber Formation†

(2008) My Hedhammar et al.   BIOCHEMISTRY

Conformational and Orientational Transformation of Silk Proteins in the Major Ampullate Gland of Nephila clavipes Spiders

(2008) Thierry Lefèvre et al.   BIOMACROMOLECULES

Simulation of Flow in the Silk Gland

(2008) David N. Breslauer et al.   BIOMACROMOLECULES

Identification and characterization of multipleSpidroin 1genes encoding major ampullate silk proteins inNephila clavipes

(2008) W. A. Gaines IV et al.   INSECT MOLECULAR BIOLOGY

Assembly mechanism of recombinant spider silk proteins

(2008) S. Rammensee et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Multiple Recombining Loci Encode MaSp1, the Primary Constituent of Dragline Silk, in Widow Spiders (Latrodectus: Theridiidae)

(2007) N. A. Ayoub et al.   MOLECULAR BIOLOGY AND EVOLUTION