Mapping SP-C co-chaperone binding sites reveals molecular consequences of disease-causing mutations on protein maturation

Disposing of misfolded ER proteins: A troubled substrate's way out of the ER

(2019) Christina Oikonomou et al.   MOLECULAR AND CELLULAR ENDOCRINOLOGY

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends

(2018) Kristine Faye R. Pobre et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control

(2016) Julia Behnke et al.   MOLECULAR CELL

A novel surfactant protein C gene mutation associated with progressive respiratory failure in infancy

(2016) Melissa Kaori Silva Litao et al.   PEDIATRIC PULMONOLOGY

Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane Segment

(2015) Alejandra Sáenz et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation

(2015) Nadinath B. Nillegoda et al.   NATURE

Glycoprotein maturation and quality control

(2015) Maurizio Molinari et al.   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY

The Large Hsp70 Grp170 Binds to Unfolded Protein Substratesin Vivowith a Regulation Distinct from Conventional Hsp70s

(2013) Julia Behnke et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Protein Folding in the Endoplasmic Reticulum

(2013) I. Braakman et al.   Cold Spring Harbor Perspectives in Biology

Breaking the amyloidogenicity code: Methods to predict amyloids from amino acid sequence

(2012) Abdullah B. Ahmed et al.   FEBS LETTERS

High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C

(2012) H. Willander et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Protein Folding and Quality Control in the ER

(2012) K. Araki et al.   Cold Spring Harbor Perspectives in Biology

Protein Folding and Modification in the Mammalian Endoplasmic Reticulum

(2011) Ineke Braakman et al.   Annual Review of Biochemistry

Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity

(2011) Xinping Xu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Protein Sorting Receptors in the Early Secretory Pathway

(2010) Julia Dancourt et al.   Annual Review of Biochemistry

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

(2010) Harm H. Kampinga et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

C-terminal, endoplasmic reticulum-lumenal domain of prosurfactant protein C - structural features and membrane interactions

(2009) Cristina Casals et al.   FEBS Journal

New surfactant protein C gene mutations associated with diffuse lung disease

(2009) L Guillot et al.   JOURNAL OF MEDICAL GENETICS

Identification of a consensus motif in substrates bound by a Type I Hsp40

(2009) P. Kota et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment

(2009) Hanna Johansson et al.   PROTEIN SCIENCE

ERdj3, a Luminal ER DnaJ Homologue, Binds Directly to Unfolded Proteins in the Mammalian ER: Identification of Critical Residues†

(2008) Yi Jin et al.   BIOCHEMISTRY

The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding

(2008) Jennifer L. Goeckeler et al.   FEBS LETTERS

ERdj4 and ERdj5 Are Required for Endoplasmic Reticulum-associated Protein Degradation of Misfolded Surfactant Protein C

(2008) Mei Dong et al.   MOLECULAR BIOLOGY OF THE CELL

Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones

(2008) Fernanda Rodriguez et al.   MOLECULAR CELL

ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER

(2008) R. Ushioda et al.   SCIENCE