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 HTLV-I envelope glycoproteins: structure and functions.

Journal of acquired immune deficiency syndromes and human retrovirology : official publication of the International Retrovirology Association - 1 Jan 1996

Delamarre L, Rosenberg A R, Pique C, Pham D, Callebaut I, Dokhélar M C

Abstract excerpt

The human T-cell lymphotropic virus type I (HTLV-I) envelope has a structural organization shared by all retroviral envelopes, which contain two mature viral glycoproteins deriving from a common precursor: an external surface protein (SU), associated with a transmembrane protein (TM) responsible for anchoring the SU-TM complex at the cell surface or in the viral envelope. Our understanding of the tertiary...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Genetic Variation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycoproteins

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Receptors, Cell Surface

Share to T-Lymphocytes

Share to Viral Envelope Proteins

Source

Identifiers

PMID: 8797709
DOI: 10.1097/00042560-199600001-00015

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 HTLV-I envelope glycoproteins: structure and functions.PMID 8797709Read ↗

The Viral Class II Membrane Fusion Machinery: Divergent Evolution from an Ancestral HeterodimerSemantic proximity Read ↗

Potential roles of cellular proteins in HIV‐1Semantic proximity Read ↗

Structural and Functional Aspects of Ebola Virus ProteinsSemantic proximity Read ↗

The cytoplasmic domain of the human T-cell leukemia virus type I envelope can modulate envelope functions in a cell type-dependent manner.Semantic proximity Read ↗

The frantic play of the concealed HIV envelope cytoplasmic tailSemantic proximity Read ↗

Human herpesvirus 6 glycoprotein M is essential for virus growth and requires glycoprotein N for its maturationSemantic proximity Read ↗

The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and ImmunogensSemantic proximity Read ↗

Truncation of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Defines Elements Required for Fusion, Incorporation, and InfectivitySemantic proximity Read ↗

Cytopathic Mechanisms of HIV-1Semantic proximity Read ↗

In vivo genetic mutations define predominant functions of the human T-cell leukemia/lymphoma virus p12I protein.Semantic proximity Read ↗

Mutation of Glycosylation Sites in BST-2 Leads to Its Accumulation at Intracellular CD63-Positive Vesicles without Affecting Its Antiviral Activity against Multivesicular Body-Targeted HIV-1 and Hepatitis B Virus.Semantic proximity Read ↗

The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodiesSemantic proximity Read ↗

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