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Open AccessJournal ArticleDOI

Expression and analysis of heparin-binding regions of the amyloid precursor protein of alzheimer's disease

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TLDR
This study suggests that heparin‐binding domains may lie within regions high in α‐helical structure in the presence of heparan sulphate.
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This article is published in FEBS Letters.The article was published on 1997-10-06 and is currently open access. It has received 62 citations till now. The article focuses on the topics: Amyloid precursor protein & Pichia pastoris.

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Heterologous protein expression in the methylotrophic yeast Pichia pastoris

TL;DR: This paper reviews the P. pastoris expression system: how it was developed, how it works, and what proteins have been produced and describes new promoters and auxotrophic marker/host strain combinations which extend the usefulness of the system.
Journal ArticleDOI

Amyloid Precursor Protein Processing and Alzheimer's Disease

TL;DR: Why Aβ accumulates in the brains of elderly individuals is unclear but could relate to changes in APP metabolism or Aβ elimination, which will be crucial to the development of therapeutic targets to treat AD.
Journal ArticleDOI

Recombinant protein expression in Pichia pastoris.

TL;DR: Major advances in the development of new strains and vectors, improved techniques, and the commercial availability of these tools coupled with a better understanding of the biology of Pichia species have led to this microbe’s value and power in commercial and research labs alike.
Journal ArticleDOI

Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory.

TL;DR: Evidence is reviewed for a dedicated research effort aimed at understanding the behavioral consequences of altered levels and activity of the different APP fragments as a result of experience and disease, with particular attention to the contributions that APP fragments play in synaptic transmission and neural plasticity.
Journal ArticleDOI

Demystifying Heparan Sulfate–Protein Interactions

TL;DR: This review provides an overview of the various modes of interaction between heparan sulfate and HSBPs, emphasizing biochemical and structural insights that improve the understanding of the many biological functions of heparin sulfate.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
PatentDOI

Measurement of protein using bicinchoninic acid

TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
Journal ArticleDOI

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

TL;DR: A purified protein derived from the twisted beta-pleated sheet fibrils in cerebrovascular amyloidosis associated with Alzheimer's disease has been isolated and Amino acid sequence analysis and a computer search reveals this protein to have no homology with any protein sequenced thus far.
Journal ArticleDOI

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

TL;DR: An apparently full-length complementary DNA clone coding for the A4 polypeptide is isolated and sequenced and suggests that the cerebral amyloid deposited in Alzheimer's disease and aged Down's syndrome is caused by aberrant catabolism of a cell-surface receptor.
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