When conjugated polymers meet amyloid fibrils

Cliff I. Stains, Indraneel Ghosh

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In the early 1900s, Alois Alzheimer diagnosed one of his patients with a devastating neurological impairment, and this form of dementia became known as Alzheimer's disease (AD). Much research over the past century has clearly established that numerous human diseases, ranging from AD and Parkinson's disease to dialysis-related amyloidosis, are best characterized by the abnormal aggregation of specific proteins. However, in the case of AD, the true toxic molecular species is still debated. Thus, the recent development of new diagnostic agents capable of distinguishing between different morphologies of aggregated proteins is of much interest.

Original languageEnglish (US)
Pages (from-to)525-528
Number of pages4
JournalACS Chemical Biology
Volume2
Issue number8
DOIs
StatePublished - Aug 2007

Fingerprint

Conjugated polymers
Amyloid
Alzheimer Disease
Polymers
Poisons
Amyloidosis
Parkinson Disease
Dementia
Dialysis
Proteins
Research
Agglomeration

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

Cite this

When conjugated polymers meet amyloid fibrils. / Stains, Cliff I.; Ghosh, Indraneel.

In: ACS Chemical Biology, Vol. 2, No. 8, 08.2007, p. 525-528.

Research output: Contribution to journalArticle

Stains, Cliff I. ; Ghosh, Indraneel. / When conjugated polymers meet amyloid fibrils. In: ACS Chemical Biology. 2007 ; Vol. 2, No. 8. pp. 525-528.
@article{09119c10cf134eb2af849aa932047f1a,
title = "When conjugated polymers meet amyloid fibrils",
abstract = "In the early 1900s, Alois Alzheimer diagnosed one of his patients with a devastating neurological impairment, and this form of dementia became known as Alzheimer's disease (AD). Much research over the past century has clearly established that numerous human diseases, ranging from AD and Parkinson's disease to dialysis-related amyloidosis, are best characterized by the abnormal aggregation of specific proteins. However, in the case of AD, the true toxic molecular species is still debated. Thus, the recent development of new diagnostic agents capable of distinguishing between different morphologies of aggregated proteins is of much interest.",
author = "Stains, {Cliff I.} and Indraneel Ghosh",
year = "2007",
month = "8",
doi = "10.1021/cb700165v",
language = "English (US)",
volume = "2",
pages = "525--528",
journal = "ACS Chemical Biology",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "8",

}

TY - JOUR

T1 - When conjugated polymers meet amyloid fibrils

AU - Stains, Cliff I.

AU - Ghosh, Indraneel

PY - 2007/8

Y1 - 2007/8

N2 - In the early 1900s, Alois Alzheimer diagnosed one of his patients with a devastating neurological impairment, and this form of dementia became known as Alzheimer's disease (AD). Much research over the past century has clearly established that numerous human diseases, ranging from AD and Parkinson's disease to dialysis-related amyloidosis, are best characterized by the abnormal aggregation of specific proteins. However, in the case of AD, the true toxic molecular species is still debated. Thus, the recent development of new diagnostic agents capable of distinguishing between different morphologies of aggregated proteins is of much interest.

AB - In the early 1900s, Alois Alzheimer diagnosed one of his patients with a devastating neurological impairment, and this form of dementia became known as Alzheimer's disease (AD). Much research over the past century has clearly established that numerous human diseases, ranging from AD and Parkinson's disease to dialysis-related amyloidosis, are best characterized by the abnormal aggregation of specific proteins. However, in the case of AD, the true toxic molecular species is still debated. Thus, the recent development of new diagnostic agents capable of distinguishing between different morphologies of aggregated proteins is of much interest.

UR - http://www.scopus.com/inward/record.url?scp=34548556510&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34548556510&partnerID=8YFLogxK

U2 - 10.1021/cb700165v

DO - 10.1021/cb700165v

M3 - Article

VL - 2

SP - 525

EP - 528

JO - ACS Chemical Biology

JF - ACS Chemical Biology

SN - 1554-8929

IS - 8

ER -