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

Interaction of human immunodeficiency virus type 1 Tat-derived peptides with TAR RNA.

Biochemistry - 11 Jul 1995

Long K S, Crothers D M

Abstract excerpt

Basic peptides from the carboxy terminus of the human immunodeficiency virus type 1 (HIV-1) Tat protein bind to the stem-loop region of TAR RNA, spanning a trinucleotide bulge, with high affinity and moderate specificity. Previous studies have demonstrated that TAR RNA contains a specific arginine binding pocket. A series of 24 amino acid Tat-derived peptides with one or two arginines has been evaluated as...

Topics

Amino Acid Sequence
Base Sequence
Gene Products, tat
HIV Long Terminal Repeat
HIV-1
Kinetics
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Peptide Fragments
RNA, Viral
Thermodynamics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

tat Gene Products, Human Immunodeficiency Virus

Source

Identifiers

PMID: 7612630
DOI: 10.1021/bi00027a041

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7612630-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction of human immunodeficiency virus type 1 Tat-derived peptides with TAR RNA.PMID 7612630Read ↗

Analysis of arginine-rich peptides from the HIV Tat protein reveals unusual features of RNA-protein recognition.Semantic proximity Read ↗

An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop.Semantic proximity Read ↗

Fluorescence correlation spectroscopy at single molecule level on the Tat-TAR complex and its inhibitors.Semantic proximity Read ↗

Identification of amino acids that promote specific and rigid TAR RNA-tat protein complex formation.Semantic proximity Read ↗

A comparative binding study of modified bovine immunodeficiency virus TAR RNA against its TAT peptide.Semantic proximity Read ↗

Binding sites of the viral RNA element TAR and of TAR mutants for various peptide ligands, probed with LILBID: a new laser mass spectrometry.Semantic proximity Read ↗

Detailed mutational analysis of TAR RNA: critical spacing between the bulge and loop recognition domains.Semantic proximity Read ↗

The Structure of the Human Immunodeficiency Virus Type-1 TAR RNA Reveals Principles of RNA Recognition by Tat ProteinSemantic proximity Read ↗

Structures of complete HIV-1 TAR RNA portray a dynamic platform poised for protein binding and structural remodelingSemantic proximity Read ↗

Human immunodeficiency virus type 1 TAR element revertant viruses define RNA structures required for efficient viral gene expression and replication.Semantic proximity Read ↗

Specific HIV-1 TAR RNA loop sequence and functional groups are required for human cyclin T1-Tat-TAR ternary complex formation.Semantic proximity Read ↗

Structural variety of arginine-rich RNA-binding peptides.Semantic proximity Read ↗

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