Featured
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News |
Engineered antibodies cross blood–brain barrier
Technique could be used to design therapies for Alzheimer's and other diseases.
- Heidi Ledford
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News |
Reprogrammed cells trigger immune reactions in mice
Medical applications of induced pluripotent stem cells called into question.
- Erika Check Hayden
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News |
Drug giants turn their backs on RNA interference
A once much-touted technique faces a difficult transition to the clinic.
- Heidi Ledford
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Letter |
Antibodies to human serum amyloid P component eliminate visceral amyloid deposits
Systemic amyloidosis is a serious disease caused by accumulation of amyloid fibrils in the viscera and connective tissues. Serum amyloid P component (SAP) is a normal plasma protein that concentrates within the amyloid deposits. These authors find that a combination of a drug that depletes circulating SAP and an antibody that targets residual SAP within the deposits results in clearance of amyloid deposits in a mouse model of the disease.
- Karl Bodin
- , Stephan Ellmerich
- & Mark B. Pepys
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News |
Souped-up antibody fends off HIV
Targeted search yields proteins that neutralize nearly all HIV strains.
- Heidi Ledford
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Research Highlights |
Drug development: Virus knockdown
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Technology Feature |
From tools to therapies
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Technology Feature |
Homing in on delivery
The scientific community now seems convinced that small RNAs will become therapies, if new tools can help these large molecules to make it safely into cells. Monya Baker reports.
- Monya Baker
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Letter |
Evidence of RNAi in humans from systemically administered siRNA via targeted nanoparticles
It has previously been shown in mice and non-human primates that systemically delivered short RNA molecules can inhibit gene expression. Here it is shown that a short interfering RNA (siRNA) can be systemically delivered, using nanoparticles, to a solid tumour in humans. The siRNA mediates cleavage of its target mRNA, thereby also reducing levels of the encoded protein. This proof-of-principle study confirms the potential of this technology for treating human disease.
- Mark E. Davis
- , Jonathan E. Zuckerman
- & Antoni Ribas
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Research Highlights |
Regenerative biology: New nerve cells connect
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Letter |
Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
Heat shock protein 70 (Hsp70) is a molecular chaperone which, by inhibiting lysosomal membrane permeabilization, promotes the survival of stressed cells. Hsp70 is now shown to stabilize lysosomes by binding to an anionic phospholipid, BMP, resulting in stimulation of acid sphingomyelinase (ASM) activity. Notably, the decreased ASM activity and lysosomal stability seen in patients with Niemann–Pick disease can be corrected by treatment with recombinant Hsp70.
- Thomas Kirkegaard
- , Anke G. Roth
- & Marja Jäättelä
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