Towards revealing the structure of bacterial inclusion bodies

Solid-State NMR Spectroscopy Reveals thatE. coliInclusion Bodies of HET-s(218-289) are Amyloids

(2009) Christian Wasmer et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Widespread Abundance of Functional Bacterial Amyloid in Mycolata and Other Gram-Positive Bacteria

(2009) P. B. Jordal et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

Learning about protein solubility from bacterial inclusion bodies

(2009) Mónica Martínez-Alonso et al.   Microbial Cell Factories

Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

(2009) S. K. Maji et al.   SCIENCE

Amyloids in bacterial inclusion bodies

(2009) Natalia S. de Groot et al.   TRENDS IN BIOCHEMICAL SCIENCES

Polymorphism in an Amyloid‐Like Fibril‐Forming Model Peptide

(2008) René Verel et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Inclusion bodies: Specificity in their aggregation process and amyloid-like structure

(2008) Montse Morell et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

New properties of inclusion bodies with implications for biotechnology

(2008) Špela Peternel et al.   BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY

Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies

(2008) Silvia Maria Doglia et al.   Biotechnology Journal

Studies on bacterial inclusion bodies

(2008) Natalia S de Groot et al.   Future Microbiology

The surface layer protein ofBacillus thuringiensisCTC forms unique intracellular parasporal inclusion body

(2008) Chenguang Zhu et al.   JOURNAL OF BASIC MICROBIOLOGY

Native Conformation at Specific Residues in Recombinant Inclusion Body Protein in Whole Cells Determined with Solid-State NMR Spectroscopy

(2008) Jaime Curtis-Fisk et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Engineering inclusion bodies for non denaturing extraction of functional proteins

(2008) Špela Peternel et al.   Microbial Cell Factories

The fold of  -synuclein fibrils

(2008) M. Vilar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core

(2008) C. Wasmer et al.   SCIENCE

Amyloid as a Depot for the Formulation of Long-Acting Drugs

(2008) Samir K Maji et al.   PLOS BIOLOGY

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

(2008) Lei Wang et al.   PLOS BIOLOGY

Production of Nonclassical Inclusion Bodies from Which Correctly Folded Protein Can Be Extracted

(2005) Simona Jevševar et al.   BIOTECHNOLOGY PROGRESS