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Article ; Online: Pregnenolone sulfate: from steroid metabolite to TRP channel ligand.

Harteneck, Christian

2013 Volume 18, Issue 10, Page(s) 12012–12028

Abstract: Pregnenolone sulfate is a steroid metabolite with a plethora of actions and functions. As a neurosteroid, pregnenolone sulfate modulates a variety of ion channels, transporters, and enzymes. Interestingly, as a sulfated steroid, pregnenolone sulfate is ... ...

Abstract	Pregnenolone sulfate is a steroid metabolite with a plethora of actions and functions. As a neurosteroid, pregnenolone sulfate modulates a variety of ion channels, transporters, and enzymes. Interestingly, as a sulfated steroid, pregnenolone sulfate is not the final- or waste-product of pregnenolone being sulfated via a phase II metabolism reaction and renally excreted, as one would presume from the pharmacology textbook knowledge. Pregnenolone sulfate is also the source and thereby the starting point for subsequent steroid synthesis pathways. Most recently, pregnenolone sulfate has been functionally "upgraded" from modulator of ion channels to an activating ion channel ligand. This review will focus on molecular aspects of the neurosteroid, pregnenolone sulfate, its metabolism, concentrations in serum and tissues and last not least will summarize the functional data.
MeSH term(s)	Animals ; Humans ; Ligands ; Pregnenolone/physiology ; Receptors, GABA/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Signal Transduction ; Transient Receptor Potential Channels/metabolism
Chemical Substances	Ligands ; Receptors, GABA ; Receptors, N-Methyl-D-Aspartate ; Transient Receptor Potential Channels ; pregnenolone sulfate (04Y4D91RG0) ; Pregnenolone (73R90F7MQ8)
Language	English
Publishing date	2013-09-27
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules181012012
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Article ; Online: Pregnenolone Sulfate

Christian Harteneck

Molecules, Vol 18, Iss 10, Pp 12012-

From Steroid Metabolite to TRP Channel Ligand

2013 Volume 12028

Abstract	Pregnenolone sulfate is a steroid metabolite with a plethora of actions and functions. As a neurosteroid, pregnenolone sulfate modulates a variety of ion channels, transporters, and enzymes. Interestingly, as a sulfated steroid, pregnenolone sulfate is not the final- or waste-product of pregnenolone being sulfated via a phase II metabolism reaction and renally excreted, as one would presume from the pharmacology textbook knowledge. Pregnenolone sulfate is also the source and thereby the starting point for subsequent steroid synthesis pathways. Most recently, pregnenolone sulfate has been functionally “upgraded” from modulator of ion channels to an activating ion channel ligand. This review will focus on molecular aspects of the neurosteroid, pregnenolone sulfate, its metabolism, concentrations in serum and tissues and last not least will summarize the functional data.
Keywords	neurosteroids ; pregnenolone sulfate ; steroid metabolism ; ion channel modulation ; TRP channels ; Organic chemistry ; QD241-441
Language	English
Publishing date	2013-09-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: Hyperforin: To Be or Not to Be an Activator of TRPC(6).

Friedland, Kristina / Harteneck, Christian

Reviews of physiology, biochemistry and pharmacology

2015 Volume 169, Page(s) 1–24

Abstract: Meantime, it is well accepted that hyperforin, the chemical instable phloroglucinol derivative of Hypericum perforatum, St. John's wort, is the pharmacophore of St. John's wort extracts. With the decline of this scientific discussion, another ... ...

Abstract	Meantime, it is well accepted that hyperforin, the chemical instable phloroglucinol derivative of Hypericum perforatum, St. John's wort, is the pharmacophore of St. John's wort extracts. With the decline of this scientific discussion, another controversial aspect has been arisen, the question regarding the underlying mechanism leading to the pharmacological profile of the plant extract used in therapy of depression. We will summarize the different concepts described for hyperforin's antidepressive activity. Starting with unspecific protein-independent mechanisms due to changes in pH, we will summarize data of protein-based concepts beginning with concepts based on involvement of a variety of proteins and will finally present concepts based on the modulation of a single protein.
MeSH term(s)	Animals ; Cytochrome P-450 Enzyme Inducers/pharmacology ; Drug Stability ; Humans ; Phloroglucinol/analogs & derivatives ; Phloroglucinol/chemistry ; Phloroglucinol/pharmacology ; TRPC Cation Channels/drug effects ; TRPC Cation Channels/physiology ; TRPC6 Cation Channel ; Terpenes/chemistry ; Terpenes/pharmacology
Chemical Substances	Cytochrome P-450 Enzyme Inducers ; TRPC Cation Channels ; TRPC6 Cation Channel ; TRPC6 protein, human ; Terpenes ; Phloroglucinol (DHD7FFG6YS) ; hyperforin (RM741E34FP)
Language	English
Publishing date	2015
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	125106-5
ISSN	1617-5786 ; 0303-4240
ISSN (online)	1617-5786
ISSN	0303-4240
DOI	10.1007/112_2015_25
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Article: Function and pharmacology of TRPM cation channels.

Harteneck, Christian

Naunyn-Schmiedeberg's archives of pharmacology

2005 Volume 371, Issue 4, Page(s) 307–314

Abstract: The physiological function and cellular role of some members of the TRPM family are poorly understood and still mysterious. Melastatin, the founding member of the TRPM group, is the most prominent example of the mysteries involved in understanding TRP ... ...

Abstract	The physiological function and cellular role of some members of the TRPM family are poorly understood and still mysterious. Melastatin, the founding member of the TRPM group, is the most prominent example of the mysteries involved in understanding TRP channel function. Melastatin or TRPM1 was first cloned in 1998 and since then it has been suggested that it functions as a tumor suppressor protein in melanocytes. On the other hand, TRPM8 and TRPA1 have been described as cold receptors, TRPM4 and TRPM5 as calcium-activated nonselective cation channels, TRPM6 and TRPM7 as magnesium-permeable and magnesium-modulated cation channels, TRPM2 as an ADP-ribose-activated channel of macrophages, and TRPM3 as a hypo-osmolarity- and sphingosine-activated channel. There are many unsolved questions and many studies have to be performed to understand the overall function of the TRPM family. In addition to electrophysiological recordings and biochemical characterization, the use of compounds modulating TRPM channel function has often been helpful to study TRPM channels in a cellular context. Therefore, the review will summarize the known functions, activation mechanisms, and pharmacological modulations of the TRPM channels.
MeSH term(s)	Animals ; Calcium/metabolism ; Cold Temperature ; Humans ; Magnesium/metabolism ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; TRPM Cation Channels/physiology
Chemical Substances	TRPM Cation Channels ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2005-04
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	121471-8
ISSN	1432-1912 ; 0028-1298
ISSN (online)	1432-1912
ISSN	0028-1298
DOI	10.1007/s00210-005-1034-x
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Article: Proteins modulating TRP channel function.

Harteneck, Christian

Cell calcium

2003 Volume 33, Issue 5-6, Page(s) 303–310

Abstract: TRP channels are involved in different signaling cascades; TRP channels can be activated via hormones and neurotransmitter in a receptor/G-protein-mediated manner or by osmotic, thermic or mechanic stimuli. The overall functional role of TRP channels ... ...

Abstract	TRP channels are involved in different signaling cascades; TRP channels can be activated via hormones and neurotransmitter in a receptor/G-protein-mediated manner or by osmotic, thermic or mechanic stimuli. The overall functional role of TRP channels within these processes of hormonal cellular control, nociception or cellular calcium homeostasis is still unclear, as these complex processes often involve macromolecular structures. Whereas the integration of Drosophila TRP in the phototransduction process is becoming clear, the understanding of the participation of mammalian TRP channels in signal transduction complexes is only beginning. TRP channels have been demonstrated to interact with PDZ domain proteins, and both scaffold and regulatory function have been shown for INAD, the PDZ domain protein of the Drosophila phototransduction complex. In mammalian cells, the interaction of NHERF and TRPC4 has been shown and it is anticipated that NHERF may abolish the apparent store-dependent regulation of TRPC4 and TRPC5. Whereas TRP channels and PDZ domain proteins form permanent heterodimeric proteins, the interaction of calcium-binding proteins is dependent on the calcium concentration and is, therefore, dynamic. The prototype of calcium-binding protein used for experiments is calmodulin; whether or not calmodulin is also the natural interaction partner of TRP channels is an open question.
MeSH term(s)	Amino Acid Sequence ; Animals ; Calcium/metabolism ; Calcium/pharmacology ; Calcium Channels/physiology ; Calmodulin/pharmacology ; Drosophila Proteins ; Eye Proteins/metabolism ; Humans ; Molecular Sequence Data ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Signal Transduction ; TRPC Cation Channels
Chemical Substances	Calcium Channels ; Calmodulin ; Drosophila Proteins ; Eye Proteins ; TRPC Cation Channels ; inaD protein, Drosophila ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2003-07-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/s0143-4160(03)00043-5
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Article ; Online: Calcium--a central regulator of keratinocyte differentiation in health and disease.

Elsholz, Floriana / Harteneck, Christian / Muller, Walter / Friedland, Kristina

European journal of dermatology : EJD

2014 Volume 24, Issue 6, Page(s) 650–661

Abstract: Regular keratinocyte differentiation is crucial for the formation of an intact epidermal barrier and is triggered by extracellular calcium. Disturbances of epidermal barrier formation and aberrant keratinocyte differentiation are involved in the ... ...

Abstract	Regular keratinocyte differentiation is crucial for the formation of an intact epidermal barrier and is triggered by extracellular calcium. Disturbances of epidermal barrier formation and aberrant keratinocyte differentiation are involved in the pathophysiology of several skin diseases, such as psoriasis, atopic dermatitis, basal and squamous skin cancer, and genetic skin diseases such as Darier's disease and Olmstedt syndrome. In this review, we summarize current knowledge about the underlying molecular mechanisms of calcium-induced differentiation in keratinocytes. We provide an overview of calcium's genomic and non-genomic mechanisms to induce differentiation and discuss the calcium gradient in the epidermis, giving rise to cornified skin and lipid envelope formation. We focus on the calcium-sensing receptor, transient receptor potential channels, and STIM/Orai as the major constituents of calcium sensing and calcium entry in the keratinocytes. Finally, skin diseases linked to impaired differentiation will be discussed, paying special attention to disturbed TRP channel expression and TRP channel mutations.
MeSH term(s)	Calcium/metabolism ; Calcium Channels/metabolism ; Carcinoma, Basal Cell/metabolism ; Carcinoma, Squamous Cell/metabolism ; Cell Differentiation/genetics ; Cell Differentiation/physiology ; Darier Disease/metabolism ; Dermatitis, Atopic/metabolism ; Humans ; Keratinocytes/metabolism ; Keratinocytes/physiology ; Membrane Proteins/metabolism ; Neoplasm Proteins/metabolism ; ORAI1 Protein ; Psoriasis/metabolism ; Receptors, Calcium-Sensing/metabolism ; Skin Diseases/metabolism ; Skin Neoplasms/metabolism ; Stromal Interaction Molecule 1 ; Transient Receptor Potential Channels/metabolism
Chemical Substances	Calcium Channels ; Membrane Proteins ; Neoplasm Proteins ; ORAI1 Protein ; ORAI1 protein, human ; Receptors, Calcium-Sensing ; STIM1 protein, human ; Stromal Interaction Molecule 1 ; Transient Receptor Potential Channels ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014-11
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1128666-0
ISSN	1952-4013 ; 1167-1122
ISSN (online)	1952-4013
ISSN	1167-1122
DOI	10.1684/ejd.2014.2452
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Zs.A 3484: Show issues

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Article ; Online: Pharmacological modulation of diacylglycerol-sensitive TRPC3/6/7 channels.

Harteneck, Christian / Gollasch, Maik

Current pharmaceutical biotechnology

2010 Volume 12, Issue 1, Page(s) 35–41

Abstract: Members of the classic type of transient receptor potential channels (TRPC) represent important molecules involved in hormonal signal transduction. TRPC3/6/7 channels are of particular interest as they are components of phospholipase C driven signalling ... ...

Abstract	Members of the classic type of transient receptor potential channels (TRPC) represent important molecules involved in hormonal signal transduction. TRPC3/6/7 channels are of particular interest as they are components of phospholipase C driven signalling pathways. Upon receptor-activation, G-protein-mediated stimulation of phospholipase C results in breakdown of phosphatidylinositides leading to increased intracellular diacylglycerol and inositol-trisphosphate levels. Diacylglycerol activates protein kinase C, but more interestingly diacylglycerol directly activates TRPC2/3/6/7 channels. Molecular cloning, expression and characterization of TRP channels enabled reassignment of traditional inhibitors of receptor-dependent calcium entry such as SKF-96365 and 2-APB as blockers of TRPC3/6/7 and several members of non-classic TRP channels. Furthermore, several enzyme inhibitors have also been identified as TRP channel blockers, such as ACA, a phospholipase A(2) inhibitor, and W-7, a calmodulin antagonist. Finally, the naturally occurring secondary plant compound hyperforin has been identified as TRPC6-selective drug, providing an exciting proof of concept that it is possible to generate TRPC-selective channel modulators. The description of Pyr3 as the first TRPC3-selective inhibitor shows that not only nature but also man is able to generate TRP-selective modulators. The review summarizes the data on pharmacological modification of TRPC3/6/7. Sheds lights on the current knowledge and historical development of pharmacological modulators of TRPC3/6/7. Our analysis indicates that Pyr3 and hyperforin provide promising core structures for the development of new, skeletive and more potent modulators of TRPC3/6/7 activity.
MeSH term(s)	Animals ; Calcium/metabolism ; Calcium Channel Blockers/pharmacology ; Diglycerides/pharmacology ; Humans ; Molecular Targeted Therapy ; Phospholipase C gamma/metabolism ; Signal Transduction ; TRPC Cation Channels/agonists ; TRPC Cation Channels/antagonists & inhibitors ; TRPC Cation Channels/metabolism ; TRPC6 Cation Channel ; Transient Receptor Potential Channels/agonists ; Transient Receptor Potential Channels/antagonists & inhibitors ; Transient Receptor Potential Channels/metabolism
Chemical Substances	1,2-diacylglycerol ; Calcium Channel Blockers ; Diglycerides ; TRPC Cation Channels ; TRPC3 cation channel ; TRPC6 Cation Channel ; TRPC6 protein, human ; TRPC7 protein, human ; Transient Receptor Potential Channels ; Phospholipase C gamma (EC 3.1.4.3) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2010-10-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2132197-8
ISSN	1873-4316 ; 1389-2010
ISSN (online)	1873-4316
ISSN	1389-2010
DOI	10.2174/138920111793937943
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Article ; Online: A novel form of capsaicin-modified amygdala LTD mediated by TRPM1.

Gebhardt, Christine / von Bohlen Und Halbach, Oliver / Hadler, Michael D / Harteneck, Christian / Albrecht, Doris

Neurobiology of learning and memory

2016 Volume 136, Page(s) 1–12

Abstract: Recently we have shown that capsaicin attenuates the strength of LTP in the lateral amygdala (LA) and demonstrated that this effect is mediated by the transient receptor potential (TRP) channel TRPV1. Here we further show that capsaicin, which is thought ...

Abstract	Recently we have shown that capsaicin attenuates the strength of LTP in the lateral amygdala (LA) and demonstrated that this effect is mediated by the transient receptor potential (TRP) channel TRPV1. Here we further show that capsaicin, which is thought to act primarily through TRPV1, modifies long term depression (LTD) in the LA. Yet the application of various TRPV1 antagonists does not reverse this effect and it remains in TRPV1-deficient mice. In addition, voltage gated calcium channels, nitric oxide and CB1 receptors are not involved. Using pharmacology and TRPM1
Language	English
Publishing date	2016-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	1223366-3
ISSN	1095-9564 ; 1074-7427
ISSN (online)	1095-9564
ISSN	1074-7427
DOI	10.1016/j.nlm.2016.09.005
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Article ; Online: Nanodiscs for INPHARMA NMR Characterization of GPCRs: Ligand Binding to the Human A2A Adenosine Receptor.

Fredriksson, Kai / Lottmann, Philip / Hinz, Sonja / Onila, Iounut / Shymanets, Aliaksei / Harteneck, Christian / Müller, Christa E / Griesinger, Christian / Exner, Thomas E

Angewandte Chemie (International ed. in English)

2017 Volume 56, Issue 21, Page(s) 5750–5754

Abstract: G-protein-coupled-receptors (GPCRs) are of fundamental importance for signal transduction through cell membranes. This makes them important drug targets, but structure-based drug design (SBDD) is still hampered by the limitations for structure ... ...

Abstract	G-protein-coupled-receptors (GPCRs) are of fundamental importance for signal transduction through cell membranes. This makes them important drug targets, but structure-based drug design (SBDD) is still hampered by the limitations for structure determination of unmodified GPCRs. We show that the interligand NOEs for pharmacophore mapping (INPHARMA) method can provide valuable information on ligand poses inside the binding site of the unmodified human A
MeSH term(s)	Binding Sites ; Humans ; Ligands ; Lipids ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Protein Binding ; Protein Domains ; Receptor, Adenosine A2A/chemistry ; Receptors, G-Protein-Coupled/chemistry
Chemical Substances	ADORA2A protein, human ; Ligands ; Lipids ; Receptor, Adenosine A2A ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2017-04-21
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.201612547
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Article ; Online: Molecular basis for the sensitivity of TRP channels to polyunsaturated fatty acids.

Riehle, Marc / Tsvetkov, Dmitry / Gohlke, Björn-Oliver / Preissner, Robert / Harteneck, Christian / Gollasch, Maik / Nürnberg, Bernd

Naunyn-Schmiedeberg's archives of pharmacology

2018 Volume 391, Issue 8, Page(s) 833–846

Abstract: Transient receptor potential (TRP) channels represent a superfamily of unselective cation channels that are subdivided into seven subfamilies based on their sequence homology and differences in gating and functional properties. Little is known about the ... ...

Abstract	Transient receptor potential (TRP) channels represent a superfamily of unselective cation channels that are subdivided into seven subfamilies based on their sequence homology and differences in gating and functional properties. Little is known about the molecular mechanisms of TRP channel regulation, particularly of the "canonical" TRP (TRPC) subfamily and their activation by polyunsaturated fatty acids (PUFAs). Here, we analyzed the structure-function relationship of Drosophila fruit fly TRPC channels. The primary aim was to uncover the molecular basis of PUFA sensitivity of Drosophila TRP-like (TRPL) and TRPgamma channels. Amino acid (aa) sequence alignment of the three Drosophila TRPC channels revealed 50 aa residues highly conserved in PUFA-sensitive TRPL and TRPgamma channels but not in the PUFA-insensitive TRP channel. Substitution of respective aa in TRPL by corresponding aa of TRP identified 18 residues that are necessary for PUFA-mediated activation of TRPL. Most aa positions are located within a stretch comprising transmembrane domains S2-S4, whereas six aa positions have been assigned to the proximal cytosolic C-terminus. Interestingly, residues I465 and S471 are required for activation by 5,8,11,14-eicosatetraynoic acid (ETYA) but not 5,8,11-eicosatriynoic acid (ETI). As proof of concept, we generated a PUFA-sensitive TRP channel by exchanging the corresponding aa from TRPL to TRP. Our study demonstrates a specific aa pattern in the transmembrane domains S2-S4 and the proximal C-terminus essential for TRP channel activation by PUFAs.
MeSH term(s)	Calcium/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Fatty Acids, Unsaturated/pharmacology ; HEK293 Cells ; Humans ; Mutagenesis, Site-Directed ; Transient Receptor Potential Channels/genetics ; Transient Receptor Potential Channels/physiology
Chemical Substances	Drosophila Proteins ; Fatty Acids, Unsaturated ; Transient Receptor Potential Channels ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-05-08
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	121471-8
ISSN	1432-1912 ; 0028-1298
ISSN (online)	1432-1912
ISSN	0028-1298
DOI	10.1007/s00210-018-1507-3
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