ReviewCell adhesion & migration
Structure elucidation of dimeric transmembrane domains of bitopic proteins.
Review in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Transmembrane Homodimers Interface Identification: Predicting Interface Residues in Alpha-Helical Transmembrane Protein Homodimers Using Sequential and Structural Features.International journal of molecular sciences · 2025Article
- Article
- Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023Review
- Saturation Mutagenesis of the Transmembrane Region of HokC inInternational journal of molecular sciences · 2021Article
- Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors.International journal of molecular sciences · 2021Review
- Peripheral membrane associations of matrix metalloproteinases.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Death Receptor 5 Activation Is Energetically Coupled to Opening of the Transmembrane Domain Dimer.Biophysical journal · 2017Article
- Joint-based description of protein structure: its application to the geometric characterization of membrane proteins.Scientific reports · 2017Article
- New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability.Scientific reports · 2016Article
- Article
- Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014Review
- Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase.The Journal of biological chemistry · 2014Article
- Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies.Structure (London, England : 1993) · 2013Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Extracellular assembly and activation principles of oncogenic class III receptor tyrosine kinases.Nature reviews. Cancer · 2012Review
- Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments.Acta naturae · 2011Article
- Role of the Lipid Environment in the Dimerization of Transmembrane Domains of Glycophorin A.Acta naturaeArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between transmembrane helices is of great interest because it directly determines biological activity of a membrane protein. Either destroying or enhancing such interactions can result in many diseases related to dysfunction of different tissues in human body. One much studied form of membrane proteins known as bitopic protein is a dimer containing two membrane-spanning helices associating laterally. Establishing structure-function relationship as well as rational design of new types of drugs targeting membrane proteins requires precise structural information about this class of objects. At present time, to investigate spatial structure and internal dynamics of such transmembrane helical dimers, several strategies were developed based mainly on a combination of NMR spectroscopy, optical spectroscopy, protein engineering and molecular modeling. These approaches were successfully applied to homo- and heterodimeric transmembrane fragments of several bitopic proteins, which play important roles in normal and in pathological conditions of human organism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.