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Topic: Transmembrane receptor

Related Topics

Cell adhesion

Integral membrane protein

G protein

Rhodopsin

Bacteriorhodopsin

Cell membrane

Ion channel

Signal recognition particle

Second messenger

Plasma membrane

Endomembrane system

Phosphorylation

Synapse

Cyclic AMP

Endoplasmic reticulum

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	Opioid Receptors
		receptor was accepted as a member of the "family" of opioid receptors on the basis of its structural homology towards the classical types, there is no corresponding pharmacological homology.
		The opioid receptor family, in common with the somatostatin receptor family, is somewhat unusual in that all of the cloned opioid receptor types belong to the G
		Among the receptors for the many neuropeptides that exist in the nervous system, the opioid receptors are unique in that there existed before the discovery of the natural agonists, an abundance of non-peptide ligands with which the pharmacology of the receptors was already defined.
	opioids.com /receptors (5011 words)

	Transmembrane receptor: Definition and Links by Encyclopedian.com
		Transmembrane receptors are integral membrane proteins, which reside and operate typically within a cell's plasma membrane, but also in the membranes of some subcellular compartments and organelles.
		a receptor's main function is to recognize and respond to a specific ligand, for example, a neurotransmitter or hormone (although certain receptors respond also to changes in transmembrane potential), and in many receptors these ligands bind to the extracellular domain.
		In some receptors, such as members of the 7TM superfamily, the transmembrane domain may contain the ligand binding pocket (evidence for this and for much of what else is known about this class of receptors is based in part on studies of bacteriorhodopsin[?], the detailed structure of which has been determined by crystallography).
	www.encyclopedian.com /tr/Transmembrane-receptor.html (556 words)

	PolyMedix
		Furthermore, phosphorylation of the water-solubilized receptor resulted in an increase in the stability of the pentameric form, just as is the case in the membrane-bound form of this protein.
		The solubilized receptor binds a toxin that is exquisitely sensitive to the biologically active three-dimensional structure of the protein.
		Given that important domains of the receptor structure are integral with the cell membrane, it has generally not been possible to reliably water solubilize and thus crystallize a GPCR for X-ray diffraction or high-field NMR studies.
	www.polymedix.com /02_01_membrane.htm (1306 words)

	Receptor (biochemistry) Summary
		In biochemistry, a receptor is a protein on the cell membrane or within the cytoplasm or cell nucleus that binds to a specific molecule (a ligand), such as a neurotransmitter, hormone, or other substance, and initiates the cellular response to the ligand.
		Many hormone receptors and neurotransmitter receptors are transmembrane proteins: transmembrane receptors are embedded in the lipid bilayer of cell membranes, that allow the activation of signal transduction pathways in response to the activation by the binding molecule, or ligand.
		Often, it is hard to determine whether the receptor is nonfunctional or the hormone is produced at decreased level; this gives rise to the "pseudo-hypo-" group of endocrine disorders, where there appears to be a decreased hormonal level while in fact it is the receptor that is not responding sufficiently to the hormone.
	www.bookrags.com /Receptor_(biochemistry) (1446 words)

	Kids.Net.Au - Encyclopedia > Transmembrane receptor (Site not responding. Last check: )
		Transmembrane receptors are integral membrane proteins, which reside and operate typically within a cell's plasma membrane, but also in the membranes of some subcellular compartments and organelles.
		Many transmembrane receptors are composed of two or more polypeptide chains which operate collectively ("oligomers") and may dissociate when ligands bind, fall off, or at another stage of their "activation" cycles.
		In some receptors, such as members of the 7TM superfamily, the transmembrane domain may contain the ligand binding pocket (evidence for this and for much of what else is known about this class of receptors is based in part on studies of bacteriorhodopsin[?], the detailed structure of which has been determined by crystallography).
	www.kids.net.au /encyclopedia-wiki/tr/Transmembrane_receptor (556 words)

	Transmembrane receptor (Site not responding. Last check: )
		Many transmembrane receptors are composed of two or more proteinsubunits which operate collectively and may dissociate when ligands bind, fall off,or at another stage of their "activation" cycles.
		a receptor's main function is to recognize and respond to a specific ligand, forexample, a neurotransmitter or hormone (although certain receptors respond also to changes in transmembrane potential), and in many receptors these ligands bind to the extracellular domain.
		In some receptors, such as members of the 7TMsuperfamily, the transmembrane domain may contain the ligand binding pocket (evidence for this and for much of what else is knownabout this class of receptors is based in part on studies of bacteriorhodopsin, the detailed structure of which has been determined by crystallography).
	www.therfcc.org /transmembrane-receptor-9911.html (498 words)

	Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after ...
		native aspartate receptor and is retained in the cytoplasm, and
		aspartate receptor in the presence and absence of aspartate; the
		of the soluble receptor in the presence and absence of aspartate;
	www.pnas.org /cgi/content/full/94/21/11201 (2721 words)

	Protein List
		transmembrane - EGF family - Notch ligand - important in establishing neural cell fates
		transmembrane receptor- tk - EGF-R homology - during oogenesis helps set up egg polarity, determines the identity of cells in the ectoderm; during larval stages participates in the development of the eye and wing.
		transmembrane - segment polarity gene - receptor for Hedgehog
	www.biochem.northwestern.edu /holmgren/Glossary/Protein_list.html (337 words)

	Class II Cytokine Receptor Family
		The TNF receptor family of transmembrane glycoproteins includes the 55 kDa TNF receptor (TNF-RI) and the 75 kDa TNF receptor (TNF-RII), as well as CD40 and Fas.
		bind to the p55 receptor and the p75 receptor.
		The p55 receptor contains a conserved sequence motif called the "death domain" called TRADD that is involved in apoptosis.
	www.umdnj.edu /pathnweb/genpath/lec_1/Class_II_Cytokine_receptor_Fam/class_ii_cyto*receptor_fam.htm (354 words)

	Bioch. Comm.
		The binding of a ligand to the receptor presumably initiates a conformational change in the membrane protein that is transmitted to the cell interior.
		The alpha subunit in close proximity to the intracellular part of the transmembrane receptor and, when a ligand binds to the receptor, the change in its conformation causes it to bind to the G-protein at the alpha subunit.
		Ligand binding to these receptors stimulates tyrosine kinase catalytic activity in the intracellular domain of the receptor, and such intracellular protein phosphorylation events are now well-established as a means of transmembrane signal transduction.
	www.rpi.edu /dept/bcbp/molbiochem/BiochSci/sbello/bioch__comm_.htm (2510 words)

	Transmembrane receptor - Definition, explanation
		Many transmembrane receptors are composed of two or more protein subunits which operate collectively and may dissociate when ligands bind, fall off, or at another stage of their "activation" cycles.
		The extracellular domain is the part of the receptor that sticks out of the membrane on the outside of the cell or organelle.
		The intracellular (or cytoplasmic) domain of the receptor interacts with the interior of the cell or organelle, relaying the signal.
	www.calsky.com /lexikon/en/txt/t/tr/transmembrane_receptor.php (532 words)

	Robert Weis-Faculty-Department of Chemistry-University of Massachusetts Amherst
		Clustering receptors together either as stable oligomers or in response to ligand binding permits the system to exhibit cooperative and polyvalent interactions that have important consequences for transmembrane signaling and transport.
		Recent studies in the laboratory have shown that the kinase is in communication with a cluster of receptor molecules, which is evident in the cooperativity of enzyme regulation as a function of the ligand concentration.
		The strength of ligand-receptor interactions is measured in three situations: (1) when the ‘ligand’ (orange bars) is polyvalent and the ‘receptor’ (blue-dotted lime green wedge) is monovalent, (2) when the ligand is monovalent and the receptor is polyvalent, and (3) when both ligand and receptor are polyvalent.
	www.chem.umass.edu /Faculty/weis.htm (1080 words)

	The Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased ...
		The aspartate receptor is a dimer with two transmembrane sequences per subunit, for a total of four transmembrane sequences.
		the 'nonswarming' receptors 7RII-27B, 7RII-73 and 7RII-96 are
		The remaining cell culture from the receptor expression experiment was used to prepare membrane fractions and cytoplasmic fractions as described in the Materials and methods.
	peds.oxfordjournals.org /cgi/content/full/12/10/863 (5530 words)

	Multiple Transmembrane Amino Acid Requirements Suggest a Highly Specific Interaction between the Bovine Papillomavirus ...
		Fully shaded sequences were derived from the EGF receptor transmembrane domain, differentially shaded sequences were derived from the Neu receptor transmembrane domain, and unshaded sequences were derived from the wild-type PDGFßR transmembrane domain.
		Transformation-specific interaction of the bovine papillomavirus E5 oncoprotein with the platelet-derived growth factor receptor transmembrane domain and the epidermal growth factor receptor cytoplasmic domain.
		The bovine papillomavirus-1 E5 protein, the 16 kDa membrane pore-forming protein and the PDGF receptor exist in a complex that is dependent on hydrophobic transmembrane interactions.
	jvi.asm.org /cgi/content/full/76/16/7976 (6591 words)

	Molecular Examination of the Transmembrane Requirements of the Platelet-derived Growth Factor beta Receptor for a ...
		R transmembrane domain is identical to that of the mouse except for an Ile instead of a Val at position 514 (33, 34).
		The truncated receptor is recognized by the anti-PR antiserum because it retains the epitope to which the antiserum was raised.
		Complex formation between the receptor and E5 is indicated by the presence of receptor in E5 immunoprecipitates.
	www.jbc.org /cgi/content/full/277/49/47149 (7543 words)

	Phorbol 12-Myristate 13-Acetate-Induced Release of the Colony-Stimulating Factor 1 Receptor Cytoplasmic Domain into the ...
		Control macrophages (lanes 1 and 4) or macrophages stimulated with PMA for 15 min (lanes 2 and 5) or for 1.5 h (lanes 3 and 6) were lysed and separated into a particulate fraction (lanes 1 to 3) and a soluble fraction (lanes 4 to 6).
		Control cells (lanes 1, 4, 8, and 11) or cell stimulated with PMA for 15 min (lanes 2, 5, 7, 9, 12, and 14) or for 1.5 h (lanes 3, 6, 10, and 13) were lysed and separated into a particulate fraction (lanes 1 to 7) and a soluble fraction (lanes 8 to 14).
		Intramembrane cleavage is dependent on the CSF-1 receptor transmembrane sequence and results in the release of the CD into the cytosol.
	mcb.asm.org /cgi/content/full/24/1/454 (6431 words)

	Antigen Receptors
		T-cell receptors (TCRs) enable the cell to bind to and, if additional signals are present, to be activated by and respond to an epitope presented by another cell called the antigen-presenting cell or APC.
		B-cell receptors (BCRs) enable the cell to bind to and, if additional signals are present, to be activated by and respond to an epitope on molecules of a soluble antigen.
		The antigen receptor on most T cells is made up of two transmembrane polypeptides designated alpha and beta (thus forming a heterodimer).
	users.rcn.com /jkimball.ma.ultranet/BiologyPages/A/AntigenReceptors.html (846 words)

	The Molecular History of Eukaryotic Life
		This shows that the receptor only triggers a pathway and the response is dependent on which neuron the gene is expressed in.
		If the cAMP receptors can carry out some of the same functions, but at a reduced efficiency, then this might be a vestige of the original receptor function without G-proteins.
		The seven transmembrane segments enclose a retinal attached to a lysine residue of the last helix by a schiffs base.
	drnelson.utmem.edu /MHEL.7TM.html (1607 words)

	[No title] (Site not responding. Last check: )
		Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [1, 2].
		The ionotropic glutamate receptors (IPR001320) have a distinct primary structure.
		Pashkov V.S. Maslennikov I.V. Tchikin L.D. Efremov R.G. Ivanov V.T. Arseniev A.S. Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR006029 (539 words)

	Nicotinic Receptor M3 Transmembrane Domain: Position 8' Contributes to Channel Gating -- De Rosa et al. 62 (2): 406 -- ...
		The nicotinic acetylcholine receptor (nAChR) is a pentamer of homologous subunits with composition
		The nicotinic acetylcholine receptor (nAChR) is a pentamer of homologous subunits.
		Grosman C and Auerbach A (2000) Asymmetric and independent contribution of the second transmembrane segment 12' residues to diliganded gating of acetylcholine receptor channels.
	molpharm.aspetjournals.org /cgi/content/full/62/2/406 (5418 words)

	Acris Antibodies - The antibody website - Homepage
		097 Antibodies to Estrogen Related Receptors (ERR alpha, -beta, and -gamma)
		093 Antibodies to Endothelial Differentiation Gene Receptors (EDG-1,-2,-4,-5,-6,-7 and -8)
		080 Antibodies to Leukotriene B4 Receptor (BLTR and BLTR2)
	www.acris-antibodies.com (434 words)

	Seven-Transmembrane Receptor Signaling Through {beta}-Arrestin -- Shenoy and Lefkowitz 2005 (308): cm10 -- Science's ... (Site not responding. Last check: )
		Abstract: Cell surface receptors are important communicators of external stimuli to the cell interior where they lead to initiation of various signaling pathways and cellular responses.
		The largest receptor family is the seven-transmembrane receptor (7TMR) family, with approximately 1000 coding genes in the human genome.
		Activated receptors are rapidly phosphorylated on serine and threonine residues by specialized enzymes called G protein–coupled receptor kinases.
	stke.sciencemag.org /cgi/content/abstract/2005/308/cm10 (449 words)

	Exploiting pathogenic Escherichia coli to model transmembrane receptor signalling: Nature Reviews Microbiology
		Transmembrane receptors are also linked to actin filaments (F-actin) by associated adaptor proteins, and form static cell–cell connections at tight junctions and cell–substratum contacts at focal adhesions.
		Although extracellular ligands often transduce transmembrane signals by inducing conformational changes in their receptors that permit the intracellular engagement or disassociation of cytoplasmic proteins, binary ligand–receptor interactions are seldom sufficient to trigger a robust cellular response.
		Nevertheless, the host transmembrane receptor CD44, which associates with inactive c-Fyn, is recruited to sites of attachment and might act as a co-receptor.
	www.nature.com /uidfinder/10.1038/nrmicro1391 (7684 words)

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