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Zika: An Ancient Virus Incipient into New Spaces
Published in Jagriti Narang, Manika Khanuja, Small Bite, Big Threat, 2020
Bennet Angel, Neelam Yadav, Jagriti Narang, Surender Singh Yadav, Annette Angel, Vinod Joshi
Membrane proteins are present beneath the envelope protein and composed of loop and transmembrane domain. The loop is associated with the N terminus of protein, and transmembrane domains are associated with supporting the membrane protein in the lipid membrane. The transmembrane domains of envelope and membrane proteins are rooted in the lipid bilayer.
Molecular Biology of Calcium Pumps in Myometrium
Published in Robert E. Garfield, Thomas N. Tabb, Control of Uterine Contractility, 2019
Joanne O’Reilly, Ashok Kumar Grover
Based on hydropathy plots of amino acid sequence of PMCA1 and immunological data, secondary structure models for the PM Ca2+ pump have been developed. The most probable model is shown in Figure 2. The secondary structure model proposed by Verma et al.71 assigns ten putative transmembrane domains with three major globular domains protruding into the cytoplasm along with the amino terminus and the carboxyl terminus.71 Other models arrive at eight transmembrane domains with the same three globular domains. Thus the proposed models differ in the number of transmembrane domains present, but most agree on the three major intracellular globular domains.18,71
Benign Thyroid Disease
Published in John C Watkinson, Raymond W Clarke, Louise Jayne Clark, Adam J Donne, R James A England, Hisham M Mehanna, Gerald William McGarry, Sean Carrie, Basic Sciences Endocrine Surgery Rhinology, 2018
Christopher M. Jones, Kristien Boelaert
A single toxic adenoma is a benign tumour autonomously secreting sufficient thyroid hormone to suppress pituitary TSH secretion. Solitary adenomas tend to grow to at least 3 cm in diameter prior to causing overt hyperthyroidism.48 They are a rare cause of thyrotoxicosis and account for only around 5% of cases.48 A mutation in the TSH receptor gene occurs in 20–83% of cases.49 Several point mutations of this gene have been identified, mostly in the transmembrane domain. These are somatic and result in TSH receptor activation and consequent autonomous thyroid hormone secretion. Other activating mutations have been identified downstream in the stimulatory G protein pathway linked to cyclic AMP production.50, 51
Targeting outer membrane protein A (OmpA) – inhibitory effect of 2′-hydroxychalcone derivatives on Acinetobacter baumannii and Candida albicans dual-species biofilm formation
Published in Biofouling, 2023
Dušan Ušjak, Katarina Novović, Branka Ivković, Branko Tomić, Valentina Đorđević, Marina T. Milenković
Protein and ligand preparations and molecular docking calculations were performed with Webina 1.0.3 service, available at https://durrantlab.pitt.edu/webina/ (Kochnev et al. 2020). A. baumannii OmpA was constructed based on the related homologous protein Escherichia coli OmpA, by using homology modeling, available at I-TASSER online server (http://zhanglab.ccmb.med.umich.edu/I-TASSER/). Amino acid sequence of A. baumannii RUH134 OmpA was downloaded from Genbank, under accession number AXV53527.1, whereas the modeling template structure E. coli K-12 OmpA (P0A910) was taken from AlphaFold protein structure database (AF-P0A910-F1), which predicted the full-length protein structure based on 11 structures (5M2Q, 3JBU, 6ITC, 6LYR, 1QJP, 1BXW, 2JMM, 2MQE, 1G90, 2GE4 and 3NB3) present in Protein Data Bank (PDB) database. The border between an opening of transmembrane domain and flexible extracellular loops was selected as a ligand binding site based on the previously identified potentially druggable area (Vila-Farrés et al. 2017). Ligand preparation was done with PDBQTConvert App. BIOVIA discovery studio visualizer version 21.1.0.20298 (Dassault Systèmes, Vélizy-Villacoublay, France) was used for protein preparation and also for visualization of receptor-ligand interactions.
CAR-NK cells: a promising cellular immunotherapy in lymphoma
Published in Expert Opinion on Biological Therapy, 2023
Shaghayegh Khanmohammadi, Nima Rezaei
As mentioned before, CAR is a genetically engineered transmembrane receptor. A CAR has four main components [6]: (1) extracellular binding domain, (2) hinge region, (3) transmembrane domain, and (4) intracellular signaling domain(s). The extracellular binding domain contains a single-chain variable fragment (scFv) derived from tumor-specific antibodies. The transmembrane domain anchors the receptor on the cell membrane of the effector cell. After the recognition of tumor antigen by CAR, the intracellular activation domain(s) leads to the activation of downstream pathways (Figure 1) [6]. The first generation of CAR-NK cells only contains CD3ζ in the intracellular activation domain. In the second and third generation of CAR NK cells, one (second) or two (second) additional co-stimulatory molecules (e.g. CD28, ICOS, 4–1BB, CD27, OX40, and CD40) are present in the activation signaling domain. The presence of co-stimulatory molecules enhanced the activation, expansion, and survival of the cells. The fourth generation of CAR-NK cells can secrete cytokines that increase their persistence and anti-tumor activity. More than one co-stimulatory molecule, such as CD134, CD28, or CD137, is present in the fourth-generation CAR-NK cells, which enhances the anti-tumor activity of CAR-NK cells via the stimulation of the innate immune system [7,35,36].
Claudin-18.2 as a therapeutic target in cancers: cumulative findings from basic research and clinical trials
Published in Tissue Barriers, 2022
Daisuke Kyuno, Akira Takasawa, Kumi Takasawa, Yusuke Ono, Tomoyuki Aoyama, Kazufumi Magara, Yuna Nakamori, Ichiro Takemasa, Makoto Osanai
The two major components of tight junctions are occludin and claudin proteins, which bind to the PDZ domains of zonula occludens (ZO) proteins to anchor the actin cytoskeleton.3,4 Claudins are 20–27-kDa transmembrane proteins that form extremely tight associations with their counterparts on adjacent cells.4 These proteins have four transmembrane domains and two extracellular loops to maintain cell-cell integrity and regulate paracellular ion transport.3 Currently, there are 27 known members of the claudin family and cancer cells have a specific claudin expression pattern according to the tumor cell origin.5 In 2008, Sahin et al. demonstrated that the claudin-18 splice variant 2, claudin-18.2, is highly expressed in several tumors.6 Research on claudin-18.2 has gradually elucidated its expression patterns and functions in cancer cells. Moreover, clinical trials using anti-claudin-18.2 antibodies as a cancer-specific molecular targeted therapy for advanced gastric adenocarcinoma are ongoing.7–9 This accumulating body of evidence indicates that claudin-18.2 is one of the most clinically relevant tight junction proteins.