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 buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme.

Journal of molecular biology - 15 Feb 2008

Merlino Antonello, Ercole Carmine, Picone Delia, Pizzo Elio, Mazzarella Lelio, Sica Filomena

Abstract excerpt

Bovine seminal ribonuclease exists in the native state as an equilibrium mixture of a swapped and an unswapped dimer. The molecular envelope and the exposed surface of the two isomers are practically indistinguishable and their diversity is almost completely buried in the interior of the protein. Surprisingly, the cytotoxic and antitumor activity of the enzyme is a peculiar property of the swapped dimer. This...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, Polyomavirus Transforming
Share to Buffers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Transformation, Viral

Share to Disulfides

Share to Endoribonucleases

Share to Isomerism

Share to Tetrazolium Salts

Share to X-Ray Diffraction

Source

Identifiers

PMID: 18164315
DOI: 10.1016/j.jmb.2007.11.008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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 buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme.PMID 18164315Read ↗

The multiple forms of bovine seminal ribonuclease: structure and stability of a C-terminal swapped dimer.Semantic proximity Read ↗

Toward an antitumor form of bovine pancreatic ribonuclease: the crystal structure of three noncovalent dimeric mutants.Semantic proximity Read ↗

Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities.Semantic proximity Read ↗

Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases.Semantic proximity Read ↗

Crystal structure of a hybrid between ribonuclease A and bovine seminal ribonuclease--the basic surface, at 2.0 A resolution.Semantic proximity Read ↗

Structural changes to ribonuclease A and their effects on biological activity.Semantic proximity Read ↗

Protein engineering of ribonucleases.Semantic proximity Read ↗

Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease.Semantic proximity Read ↗

Circular dichroism study of ribonuclease A mutants containing the minimal structural requirements for dimerization and swapping.Semantic proximity Read ↗

Extensive deamidation of RNase A inhibits its oligomerization through 3D domain swapping.Semantic proximity Read ↗

Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.Semantic proximity Read ↗

New muteins of RNase A with enhanced antitumor action.Semantic proximity Read ↗

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