Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The HIV Tat protein transduction domain improves the biodistribution of beta-glucuronidase expressed from recombinant viral vectors.

Nature biotechnology - 1 Jul 2001

Xia H, Mao Q, Davidson B L

Abstract excerpt

Treatment of inherited genetic diseases of the brain remains an intractable problem. Methods to improve the distribution of enzymes that are injected or expressed from transduced cells will be required for many human brain therapies. Recent studies showed that a peptide, the protein transduction domain (PTD) from HIV Tat, could improve the distribution of cytoplasmic reporter proteins when administered...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 3T3 Cells
Share to Adenoviridae
Share to Brain Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endocytosis

Share to Gene Products, tat

Share to Glucuronidase

Share to Lysosomes

Share to Tissue Distribution

Source

Identifiers

PMID: 11433275
DOI: 10.1038/90242

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The HIV Tat protein transduction domain improves the biodistribution of beta-glucuronidase expressed from recombinant viral vectors.PMID 11433275Read ↗

Human β-glucuronidase: structure, function, and application in enzyme replacement therapy.Semantic proximity Read ↗

Functional correction of CNS phenotypes in a lysosomal storage disease model using adeno-associated virus type 4 vectors.Semantic proximity Read ↗

Effective gene therapy in an authentic model of Tay-Sachs-related diseasesSemantic proximity Read ↗

Sustained Production of β-Glucuronidase from Localized Sites after AAV Vector Gene Transfer Results in Widespread Distribution of Enzyme and Reversal of Lysosomal Storage Lesions in a Large Volume of Brain in Mucopolysaccharidosis VII MiceSemantic proximity Read ↗

Engineering Memory T Cells as a platform for Long-Term Enzyme Replacement Therapy in Lysosomal Storage DisordersSemantic proximity Read ↗

Engineering Brain Parasites for Intracellular Delivery of Therapeutic ProteinsSemantic proximity Read ↗

Novel Vector Design and Hexosaminidase Variant Enabling Self-Complementary Adeno-Associated Virus for the Treatment of Tay-Sachs Disease.Semantic proximity Read ↗

Sialic Acid Deposition Impairs the Utility of AAV9, but Not Peptide-modified AAVs for Brain Gene Therapy in a Mouse Model of Lysosomal Storage DiseaseSemantic proximity Read ↗

Biodistribution, kinetics, and efficacy of highly phosphorylated and non-phosphorylated beta-glucuronidase in the murine model of mucopolysaccharidosis VII.Semantic proximity Read ↗

Reversal of Pathology in the Entire Brain of Mucopolysaccharidosis Type VII Mice after Lentivirus-Mediated Gene TransferSemantic proximity Read ↗

Exploiting toxin internalization receptors to enhance delivery of proteins to lysosomes for enzyme replacement therapySemantic proximity Read ↗

RTB Lectin: a novel receptor-independent delivery system for lysosomal enzyme replacement therapies.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.