Articles with "transmembrane" as a keyword



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Solvent accessibility of a GPCR transmembrane domain probed by in-membrane chemical modification (IMCM).

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Published in 2023 at "FEBS letters"

DOI: 10.1002/1873-3468.14627

Abstract: G protein-coupled receptors (GPCRs) transmit signals from drugs across cell membranes, leading to associated physiological effects. To study the structural basis of the transmembrane signaling, in-membrane chemical modification (IMCM) has previously been introduced for 19… read more here.

Keywords: imcm; transmembrane; membrane chemical; solvent accessibility ... See more keywords
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The transmembrane protein MaSho1 negatively regulates conidial yield by shifting the conidiation pattern in Metarhizium acridum

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Published in 2020 at "Applied Microbiology and Biotechnology"

DOI: 10.1007/s00253-020-10523-0

Abstract: Sho1 is an important membrane sensor upstream of the HOG-MAPK signaling pathway, which plays critical roles in osmotic pressure response, growth, and virulence in fungi. Here, a Sho1 homolog (MaSho1), containing four transmembrane domains and… read more here.

Keywords: transmembrane; metarhizium acridum; conidial yield; conidiation pattern ... See more keywords
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TMDIM: an improved algorithm for the structure prediction of transmembrane domains of bitopic dimers

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Published in 2017 at "Journal of Computer-Aided Molecular Design"

DOI: 10.1007/s10822-017-0047-0

Abstract: Abstract$$\alpha$$α-Helical transmembrane proteins are the most important drug targets in rational drug development. However, solving the experimental structures of these proteins remains difficult, therefore computational methods to accurately and efficiently predict the structures are in… read more here.

Keywords: transmembrane; bitopic dimers; tmdim improved; structure prediction ... See more keywords
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Molecular characterization and cellular localization of a transmembrane C-type lectin receptor in hemocytes from the scallop Argopecten purpuratus

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Published in 2022 at "Aquaculture"

DOI: 10.1016/j.aquaculture.2021.737293

Abstract: Abstract Recognition of potential pathogens is a crucial function of the immune system of every organism. In this context, great efforts have been made in the last years to characterize the diversity of pattern recognition… read more here.

Keywords: argopecten purpuratus; recognition; hemocytes scallop; transmembrane ... See more keywords
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Short TRPM2 prevents the targeting of full-length TRPM2 to the surface transmembrane by hijacking to ER associated degradation.

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Published in 2019 at "Biochemical and biophysical research communications"

DOI: 10.1016/j.bbrc.2019.10.065

Abstract: Membrane proteins are targeted to the surface transmembrane after folding and assembling in the endoplasmic reticulum (ER). Misfolded- and unassembled-proteins are degraded by proteasomes following ubiquitination, termed ER-associated degradation (ERAD). Transient receptor potential melastatin 2… read more here.

Keywords: transmembrane; full length; trpm2; short trpm2 ... See more keywords
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Mapping pathogenic mutations suggests an innovative structural model for the pendrin (SLC26A4) transmembrane domain.

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Published in 2017 at "Biochimie"

DOI: 10.1016/j.biochi.2016.10.002

Abstract: Human pendrin (SLC26A4) is an anion transporter mostly expressed in the inner ear, thyroid and kidney. SLC26A4 gene mutations are associated with a broad phenotypic spectrum, including Pendred Syndrome and non-syndromic hearing loss with enlarged… read more here.

Keywords: transmembrane; transmembrane domain; model; pendrin slc26a4 ... See more keywords
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The oligomerization mediated by the alanine 397 residue in the transmembrane domain is crucial to sydecan-3 functions.

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Published in 2020 at "Cellular signalling"

DOI: 10.1016/j.cellsig.2020.109544

Abstract: Syndecans are single-pass transmembrane proteins on the cell surface that are involved in various cellular functions. Previously, we reported that both homo- and hetero-form of syndecan dimers affected their functionality. However, little is known about… read more here.

Keywords: transmembrane; alanine 397; transmembrane domain; oligomer formation ... See more keywords

Beyond the AMPA receptor: Diverse roles of SynDIG/PRRT brain-specific transmembrane proteins at excitatory synapses

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Published in 2021 at "Current opinion in pharmacology"

DOI: 10.1016/j.coph.2021.03.011

Abstract: α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPARs) are responsible for fast excitatory transmission in the brain. Deficits in synaptic transmission underlie a variety of neurological and psychiatric disorders. However, drugs that target AMPARs are challenging to… read more here.

Keywords: syndig prrt; transmembrane; transmembrane proteins; ampar auxiliary ... See more keywords
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Roughness of Transmembrane Helices Reduces Lipid Membrane Dynamics

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Published in 2018 at "iScience"

DOI: 10.1016/j.isci.2018.11.026

Abstract: Summary The dynamics of cellular membranes is primarily determined by lipid species forming a bilayer. Proteins are considered mainly as effector molecules of diverse cellular processes. In addition to large assemblies of proteins, which were… read more here.

Keywords: transmembrane; membrane dynamics; helices reduces; roughness transmembrane ... See more keywords
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Topology prediction improvement of α-helical transmembrane proteins through helix-tail modeling and multiscale deep learning fusion.

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Published in 2019 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2019.12.007

Abstract: Transmembrane proteins (TMPs) play important roles in many biological processes, such as cell recognition and communication. Their structures are crucial for revealing complex functions but are hard to obtain. A variety of computational algorithms have… read more here.

Keywords: transmembrane; deep learning; multiscale deep; topology ... See more keywords
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A Transmembrane Crenarchaeal Mannosyltransferase Is Involved in N-Glycan Biosynthesis and Displays an Unexpected Minimal Cellulose-Synthase-like Fold.

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Published in 2020 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2020.06.016

Abstract: Protein glycosylation constitutes a critical post-translational modification that supports a vast number of biological functions in living organisms across all domains of life. A seemingly boundless number of enzymes, glycosyltransferases, are involved in the biosynthesis… read more here.

Keywords: biosynthesis; transmembrane; cellulose synthase; transmembrane crenarchaeal ... See more keywords