Islet amyloid polypeptide, islet amyloid, and diabetes mellitus

P Westermark, A Andersson… - Physiological …, 2011 - journals.physiology.org
Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of
the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both …

Protein folding in the cell

MJ Gething, J Sambrook - Nature, 1992 - nature.com
In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

Oxidized redox state of glutathione in the endoplasmic reticulum

C Hwang, AJ Sinskey, HF Lodish - Science, 1992 - science.org
The redox state of the endoplasmic reticulum (ER) was measured with the peptide N-Acetyl-
Asn-Tyr-Thr-Cys-NH2. The peptide diffused across cellular membranes; some became …

Seed storage proteins: structures and biosynthesis.

PR Shewry, JA Napier, AS Tatham - The plant cell, 1995 - ncbi.nlm.nih.gov
The plant seed is not only an organ of propagation and dispersal but also the major plant
tissue harvested by humankind. The amount of protein present in seeds varies from-10%(in …

[PDF][PDF] Thioredoxin and glutaredoxin systems

A Holmgren - Journal of Biological Chemistry, 1989 - pdfs.semanticscholar.org
Thioredoxin is known as a hydrogen donor for ribonucleotide reductase, the essential
enzyme providing deoxyribonucleotides for DNA replication (1-4). Characterization of viable …

The role for endoplasmic reticulum stress in diabetes mellitus

DL Eizirik, AK Cardozo, M Cnop - Endocrine reviews, 2008 - academic.oup.com
Accumulating evidence suggests that endoplasmic reticulum (ER) stress plays a role in the
pathogenesis of diabetes, contributing to pancreatic β-cell loss and insulin resistance …

The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology

CJ Guerriero, JL Brodsky - Physiological reviews, 2012 - journals.physiology.org
Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation

F Hatahet, LW Ruddock - Antioxidants & redox signaling, 2009 - liebertpub.com
Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

The complete general secretory pathway in gram-negative bacteria

AP Pugsley - Microbiological reviews, 1993 - Am Soc Microbiol
The unifying feature of all proteins that are transported out of the cytoplasm of gram-negative
bacteria by the general secretory pathway (GSP) is the presence of a long stretch of …

Identification of a protein required for disulfide bond formation in vivo

JCA Bardwell, K McGovern, J Beckwith - Cell, 1991 - cell.com
We describe a mutation (d&A) that renders Escherichia coli severely defective in disulfide
bond formation. In d&A mutant cells, pulse-labeled P-lactamase, alkaline phosphatase, and …