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

Mixed reconstitution of mutated subunits of HIV-1 reverse transcriptase coexpressed in Escherichia coli - two tags tie it up.

European journal of biochemistry - 1 Apr 1999

Maier G, Dietrich U, Panhans B, Schröder B, Rübsamen-Waigmann H, Cellai L, Hermann T, Heumann H

Abstract excerpt

The active form of HIV-1 reverse transcriptase (RT) is a p66/p51 heterodimer, in which the p51 subunit is generated by C-terminal proteolytic cleavage of p66. A well-known problem of p66 recombinant expression is partial cleavage of a 15-kDa peptide from the C-terminus by host proteases that can not be completely suppressed. In order to analyse the contribution of specific residues to a particular function in one...

Read the complete abstract on PubMed

Topics

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

Share to Cloning, Molecular
Share to Dimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA, Viral

Share to Histidine

Share to HIV Reverse Transcriptase

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 10103027
DOI: 10.1046/j.1432-1327.1999.00304.x

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mixed reconstitution of mutated subunits of HIV-1 reverse transcriptase coexpressed in Escherichia coli - two tags tie it up.PMID 10103027Read ↗

Formation of heterodimers of human-immunodeficiency-virus-type-1 reverse transcriptase by recombination of separately purified subunits.Semantic proximity Read ↗

HIV-1 reverse transcriptase: polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer.Semantic proximity Read ↗

Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization.Semantic proximity Read ↗

Single-step purification of recombinant wild-type and mutant HIV-1 reverse transcriptase.Semantic proximity Read ↗

Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.Semantic proximity Read ↗

An integrated system to study multiply substituted human immunodeficiency virus type 1 reverse transcriptase.Semantic proximity Read ↗

Insertion of a small peptide of six amino acids into the beta7-beta8 loop of the p51 subunit of HIV-1 reverse transcriptase perturbs the heterodimer and affects its activities.Semantic proximity Read ↗

HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.Semantic proximity Read ↗

Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation.Semantic proximity Read ↗

Overexpression, Purification and Functional Characterisation of Wild-Type HIV-1 Subtype C Protease and Two Variants Using a Thioredoxin and His-Tag Protein Fusion System.Semantic proximity Read ↗

Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase.Semantic proximity Read ↗

Reverse transcriptase of human immunodeficiency virus type 1: functionality of subunits of the heterodimer in DNA synthesis.Semantic proximity Read ↗

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