The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The research target is Danio rerio trpm7 (UniProt Q563W7), a TRP melastatin-family cation channel fused to a C-terminal serine/threonine α-kinase (EC 2.7.11.1). Zebrafish genetics papers explicitly connect trpm7 to classic mutant alleles/aliases including touchdown/touchtone (tct) and describe the expected channel-kinase architecture, matching the UniProt description and domain composition (TRPM ion transport domain plus α-kinase domain). (low2011trpm7isrequired pages 1-2, elizondo2010trpm7regulationof pages 1-2, mcneill2007celldeathof pages 1-2)
TRPM7 is often described as a bifunctional channel-enzyme (chanzyme): (i) a nonselective cation channel with strong divalent permeability, and (ii) a cytosolic α-kinase domain that phosphorylates protein substrates on Ser/Thr residues and also autophosphorylates. (okada2023celldeathinduction pages 4-5, decker2015trpm7functionin pages 21-25)
High-level domain organization (per subunit): a large N-terminal TRPM homology region (MHR1–4); a 6-transmembrane channel domain (S1–S6) with a pore loop between S5–S6; a TRP helix and coiled-coil elements; and a C-terminal α-kinase domain (plus an autophosphorylation-rich Ser/Thr region). Cryo-EM shows the tetrameric channel and extensive bound lipids/cholesterol-like densities around the transmembrane region. (nadezhdin2023structuralmechanismsof pages 2-3, okada2023celldeathinduction pages 4-5, nadezhdin2023structuralmechanismsof pages 1-2)
Primary transport function: TRPM7 forms a plasma-membrane cation channel permeable to Mg2+, Ca2+, and Zn2+, with broader permeability to other divalent cations (e.g., Ba2+, Sr2+, Cd2+; and in some contexts other transition metals). (decker2015trpm7functionin pages 17-21, okada2023celldeathinduction pages 4-5)
A reported permeability ranking is Zn2+ ≈ Ni2+ >> Ba2+ > Co2+ > Mg2+ ≥ Mn2+ ≥ Sr2+ ≥ Cd2+ ≥ Ca2+, and the channel is not permeable to the trivalent blockers La3+ or Gd3+. (mittermeier2019thekinasecoupledtrpm7 pages 8-11)
Quantitative electrophysiology: a review summarizing primary measurements reports single-channel unitary conductance ~40 pS at ~−70 mV when extracellular Mg2+ is absent. (okada2023celldeathinduction pages 4-5)
TRPM7 is constitutively active but strongly regulated by intracellular divalents and phosphoinositides:
- Intracellular Mg2+ and Mg·ATP act as negative regulators. (mittermeier2019thekinasecoupledtrpm7 pages 8-11, sturgeon2020theroleof pages 15-18)
- Channel opening requires PIP2; receptor pathways that deplete PIP2 reduce TRPM7 activity. (decker2015trpm7functionin pages 17-21, mittermeier2019thekinasecoupledtrpm7 pages 8-11)
- Extracellular divalents (especially Mg2+) cause strong outward rectification in macroscopic currents via open-channel block. (okada2023celldeathinduction pages 4-5)
- TRPM7 is also described as pH-sensitive (including voltage-dependent pH effects) and responsive to osmotic/mechanical perturbations in some systems. (decker2015trpm7functionin pages 17-21, decker2015trpm7functionin pages 21-25)
A major recent advance is high-resolution cryo-EM defining open/closed gating rearrangements and druggable ligand pockets.
Open-state mechanics: In a gain-of-function open structure, the pore widens near N1097/N1098 (reported pore radius change from <0.5 Å closed to >2.3 Å open), and the narrowest open constriction is near a ring of Y1085 residues (~1.4 Å). Mutational analysis indicates Y1085 hydroxyl chemistry is important for function. (nadezhdin2023structuralmechanismsof pages 4-5)
Key pore electrostatics: acidic vestibule residues are implicated in divalent attraction/selectivity (reviewed with reference to residues such as D1054/E1052 in human TRPM7), with D1054 affecting proton conduction. (okada2023celldeathinduction pages 4-5)
Catalyzed reaction: TRPM7’s α-kinase domain transfers phosphate from ATP to serine/threonine residues on protein substrates and on TRPM7 itself (autophosphorylation). (okada2023celldeathinduction pages 4-5, decker2015trpm7functionin pages 21-25)
Representative substrates (reported across systems; used here as mechanistic inference relevant to zebrafish ortholog): annexin 1/ANXA1, myosin II / myosin IIA heavy chain, eEF2 kinase, and STIM2 (linking to store-operated Ca2+ entry regulation). (decker2015trpm7functionin pages 21-25, mittermeier2019thekinasecoupledtrpm7 pages 8-11)
Domain separability: In zebrafish, at least one core behavioral function (touch-evoked escape) depends on TRPM7 channel activity, whereas TRPM7’s kinase activity and strict preference for divalents over monovalents were reported to be dispensable for that behavior. (low2011trpm7isrequired pages 1-2)
TRPM7 localizes to the plasma membrane and also to intracellular pools described as tubulovesicular/synaptic vesicle-like compartments. A mechanistic source also describes a population of acidic, glutathione-rich vesicles implicated in Zn2+ storage and redox-triggered Zn2+ release (not zebrafish-specific but relevant to inferred cellular roles of TRPM7). (decker2015trpm7functionin pages 21-25, mittermeier2019thekinasecoupledtrpm7 pages 8-11, mcneill2007celldeathof pages 1-2)
In zebrafish, trpm7 mRNA is broadly expressed, with particularly high abundance in kidney tubules (pronephric/mesonephric) and in the corpuscles of Stannius (an endocrine organ involved in ionic homeostasis), supporting a primary role in systemic divalent-cation regulation and renal physiology. (elizondo2010trpm7regulationof pages 1-2)
Functionally, TRPM7 is required within sensory neurons for normal activation of touch-evoked escape behavior. (low2011trpm7isrequired pages 1-2)
Zebrafish touchdown alleles of trpm7 carry mutations that abolish channel activity. Mutants show a transient deficit in touch-evoked escape: they do not respond between 52 and 63 hours post-fertilization (hpf) (reported n = 24 embryos from three clutches). Sensory neurons are present and tactile-responsive, suggesting the behavioral deficit arises downstream (consistent with altered synaptic neurotransmitter release). Elevated extracellular divalent cations can restore escape behavior, supporting a divalent-dependent synaptic mechanism. (low2011trpm7isrequired pages 1-2)
In trpm7 mutant embryos, melanophore loss results from cell death with necrotic features (not caspase-dependent apoptosis). Importantly, inhibition of melanin synthesis largely prevents melanophore death, supporting a model where Trpm7-dependent ionic homeostasis buffers pigment cells against toxic melanin-synthesis intermediates or associated stress. (mcneill2007celldeathof pages 1-2)
Zebrafish trpm7 mutants show reduced whole-embryo total magnesium and total calcium by early larval stages, consistent with TRPM7 acting as an in vivo regulator of organismal divalent-cation balance. Mutants also exhibit kidney stone formation and altered endocrine programs involving stanniocalcin 1 (stc1) and fgf23; mechanistically, fgf23 knockdown reduces kidney stones, linking Trpm7 to endocrine control of mineral homeostasis and renal mineralization. (elizondo2010trpm7regulationof pages 1-2)
Comparative developmental evidence across vertebrates supports that TRPM7 channel function is essential for early morphogenesis and cellular Mg2+ homeostasis, and that channel vs kinase contributions can be separable in some developmental contexts. This supports interpreting zebrafish phenotypes as primarily originating from divalent-cation homeostasis and associated signaling. (nethramangalath2024investigationofthe pages 16-20, sturgeon2020theroleof pages 15-18)
A major 2023 advance is a suite of TRPM7 cryo-EM structures (2.17–2.99 Å), including closed and open conformations and ligand-bound states. These structures link specific conformational changes (S6/TRP rearrangements and pore dilation) to activation and inhibition mechanisms and provide atomic details of lipid interactions. (nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof pages 2-3, nadezhdin2023structuralmechanismsof pages 4-5)
The 2023 structural work mapped:
- An intersubunit naltriben (NTB) binding/activation site involving residues D670, L671, M741, S744, N752, where mutations weaken NTB activation. (nadezhdin2023structuralmechanismsof pages 4-5, nadezhdin2023structuralmechanismsof media 0122cc1d)
- A vanilloid-like inhibitor pocket in the transmembrane domain for inhibitors such as VER155008 and NS8593, with key residues including A981, M991, W1111, F1118; these inhibitors stabilize a closed state (and compete with endogenous lipid occupancy in the pocket). (nadezhdin2023structuralmechanismsof media 0122cc1d, nadezhdin2023structuralmechanismsof media a1a7982d)
These findings are directly relevant to zebrafish trpm7 annotation because they provide a mechanistic basis for using agonists/antagonists to probe channel function in vivo (including in zebrafish). (nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof media 0122cc1d)
A 2023 review focusing on TRPM7 (in the context of stress and cell death) summarizes core biophysical properties (e.g., outward rectification with divalents; monovalent/divalent conduction; proton conduction) and emphasizes separability of channel and kinase functions. This reinforces TRPM7’s role as a broadly expressed stress- and homeostasis-relevant cation pathway. (okada2023celldeathinduction pages 4-5)
Zebrafish trpm7/tct mutants provide a tractable model to:
- Test how divalent-cation availability modulates neural circuit output (touch-evoked escape) in a defined developmental window. (low2011trpm7isrequired pages 1-2)
- Study pigment-cell survival and metabolic/ionic toxicity coupling (melanin-synthesis-dependent death). (mcneill2007celldeathof pages 1-2)
- Model renal mineralization/kidney stone formation and endocrine control of mineral homeostasis (stc1/fgf23 pathways). (elizondo2010trpm7regulationof pages 1-2)
The structurally mapped compounds naltriben (agonist) and inhibitors NS8593 and VER155008 provide mechanistically interpretable tools for perturbing TRPM7 gating, enabling sharper causal tests than older, less-specific modulators. (nadezhdin2023structuralmechanismsof pages 2-3, nadezhdin2023structuralmechanismsof media 0122cc1d)
The following table consolidates key annotation elements (domains, transport/kinase functions, localization, zebrafish phenotypes, and 2023 structural pharmacology).
| Aspect | Summary for zebrafish trpm7 (UniProt Q563W7) | Key evidence sources |
|---|---|---|
| Verified target identity | Danio rerio trpm7 corresponds to the zebrafish TRPM7 channel-kinase associated with classic mutant aliases touchdown/touchtone (tct) and cb495; literature describes a TRP melastatin family cation channel with a C-terminal serine/threonine α-kinase, matching UniProt Q563W7 domain architecture. | (elizondo2010trpm7regulationof pages 1-2, low2011trpm7isrequired pages 1-2, mcneill2007celldeathof pages 1-2) |
| Domain architecture | TRPM7 is a tetrameric plasma-membrane channel whose subunits contain an N-terminal TRPM homology region (MHR1-4/NTD), 6 transmembrane helices (S1-S6) with a pore loop between S5-S6, a TRP helix, coiled-coil region, serine/threonine-rich autophosphorylation/substrate domain, and a C-terminal α-kinase catalytic domain. Structural work places the CTD after the TMD and resolves extensive lipid interactions around the TMD. | (mittermeier2019thekinasecoupledtrpm7 pages 8-11, nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof pages 2-3, okada2023celldeathinduction pages 4-5) |
| Ion permeability / selectivity | TRPM7 is a divalent-permeable nonselective cation channel conducting Mg2+, Ca2+, Zn2+ and additional divalents; broader literature cited in the retrieved evidence also notes permeability to Fe2+, Cu2+, Mn2+, Co2+, Ba2+, Sr2+, Cd2+ and monovalents under some conditions. A reported permeability ranking is Zn2+ ≈ Ni2+ >> Ba2+ > Co2+ > Mg2+ ≥ Mn2+ ≥ Sr2+ ≥ Cd2+ ≥ Ca2+; the channel is not permeable to La3+ or Gd3+. Single-channel conductance is about 40 pS at ~−70 mV in the absence of extracellular Mg2+. | (decker2015trpm7functionin pages 17-21, mittermeier2019thekinasecoupledtrpm7 pages 8-11, sturgeon2020theroleof pages 15-18, okada2023celldeathinduction pages 4-5) |
| Key gating / regulation | Channel activity is constitutive but strongly regulated. Important negative regulators include intracellular Mg2+, Mg·ATP, and acidic extracellular pH; activation/opening requires PIP2. In whole-cell recordings, extracellular divalents produce strong outward rectification via open-channel block. TRPM7 is also reported as sensitive to pH, osmolarity/stretch/swelling, and receptor pathways that deplete PIP2. | (decker2015trpm7functionin pages 17-21, mittermeier2019thekinasecoupledtrpm7 pages 8-11, decker2015trpm7functionin pages 21-25, sturgeon2020theroleof pages 15-18, okada2023celldeathinduction pages 4-5) |
| Pore / permeation determinants | Acidic vestibule residues help attract permeant cations; D1054 and E1052 are highlighted as important for Mg2+/Ca2+ binding/selectivity in human TRPM7, and D1054A abolishes proton conductance. 2023 structural work found the closed-to-open transition widens the gate near N1097/N1098, with the narrowest open constriction near Y1085; Y1085F/S are loss-of-function, supporting a key permeation role. | (nadezhdin2023structuralmechanismsof pages 4-5, okada2023celldeathinduction pages 4-5) |
| Kinase activity | TRPM7 is a protein kinase EC 2.7.11.1 with a cytosolic α-kinase domain that autophosphorylates and phosphorylates serine/threonine residues on downstream targets. Genetic studies indicate channel and kinase functions can be partially separable, with some zebrafish behavioral phenotypes depending mainly on channel function rather than kinase catalytic activity. | (decker2015trpm7functionin pages 21-25, low2011trpm7isrequired pages 1-2, okada2023celldeathinduction pages 4-5) |
| Representative kinase substrates | Reported substrates in the retrieved evidence include annexin A1/annexin 1, myosin II / myosin IIA heavy chain, eEF2 kinase, STIM2, and histones after cleavage/nuclear translocation of the kinase fragment in some systems. These data mostly come from non-zebrafish mechanistic studies but are relevant to inferred molecular function of zebrafish Trpm7. | (mittermeier2019thekinasecoupledtrpm7 pages 8-11, decker2015trpm7functionin pages 21-25) |
| Subcellular localization | TRPM7 localizes primarily to the plasma membrane, but also to intracellular tubulovesicular/synaptic vesicle-like compartments; some evidence describes acidic glutathione-rich vesicles (M7V) implicated in Zn2+ storage/release. The kinase fragment has been reported to translocate to the nucleus after cleavage in some systems. | (mittermeier2019thekinasecoupledtrpm7 pages 8-11, decker2015trpm7functionin pages 21-25, mcneill2007celldeathof pages 1-2) |
| Zebrafish expression | In zebrafish, trpm7 mRNA is broadly expressed, with particularly strong expression in pronephric/mesonephric kidney tubules and the corpuscles of Stannius, consistent with roles in systemic cation homeostasis and renal physiology. | (elizondo2010trpm7regulationof pages 1-2) |
| Zebrafish role: ion homeostasis / kidney | Zebrafish mutants show reduced whole-embryo total magnesium and calcium by early larval stages, supporting a direct role in organismal divalent-cation balance. Mutants also show kidney stone formation and altered endocrine responses involving stanniocalcin 1 (stc1) and fgf23; fgf23 knockdown reduces stones. | (elizondo2010trpm7regulationof pages 1-2) |
| Zebrafish role: melanophore survival | trpm7 homozygous mutants lose melanophores during embryogenesis; melanophore death shows necrotic features rather than caspase-dependent apoptosis. Inhibition of melanin synthesis largely prevents melanophore death, suggesting Trpm7 is needed to maintain ionic/metabolic conditions that protect pigment cells from toxic melanin-synthesis intermediates. | (mcneill2007celldeathof pages 1-2) |
| Zebrafish role: touch-evoked escape | In touchdown/tct mutants, sensory neurons are present and can respond to tactile stimulation, but the animals fail to activate normal escape behavior during a defined developmental window: mutants do not respond between 52 and 63 hpf, based on n = 24 embryos from three clutches. Rescue experiments indicate channel activity, but not kinase activity or strict divalent-over-monovalent selectivity, is required for this behavior. Elevated extracellular divalents can restore escape behavior, consistent with a role in synaptic transmitter release/modulation. | (low2011trpm7isrequired pages 1-2) |
| Additional zebrafish phenotypes | Beyond pigmentation and touch behavior, zebrafish trpm7 mutants show impaired growth, defective skeletogenesis, and broader developmental abnormalities consistent with disrupted Mg2+/Ca2+ homeostasis. Maternal transcript contribution likely buffers the earliest stages, contributing to later onset/recovery of some phenotypes. | (elizondo2010trpm7regulationof pages 1-2, mcneill2007celldeathof pages 1-2) |
| Developmental significance across vertebrates | Comparative evidence supports TRPM7 as essential for embryogenesis, gastrulation/cell movements, proliferation, and Mg2+ homeostasis. In vertebrate embryos, channel function is often more critical than kinase catalytic activity for early morphogenesis, which helps interpret zebrafish phenotypes mechanistically. | (nethramangalath2024investigationofthe pages 16-20, sturgeon2020theroleof pages 15-18) |
| 2023 structural highlight: open-state mechanism | Cryo-EM structures in 2023 resolved TRPM7 at 2.17-2.99 Å, including a 2.19 Å apo closed state and open conformations. A gain-of-function mutant (N1098Q) produced an open state in which the pore radius at N1097 increased from <0.5 Å to >2.3 Å; the narrowest constriction (~1.4 Å) is at Y1085. Gating involves S6 lengthening, TRP helix shortening/rotation, and a π-bulge in S6. | (nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof pages 4-5, nadezhdin2023structuralmechanismsof pages 2-3) |
| 2023 pharmacology highlight: naltriben activation site | The agonist naltriben (NTB) binds at an intersubunit site formed by the MHR4/Pre-S1 region of one subunit and the α21/α22 loop of the neighboring subunit. Key coordinating residues include D670, L671, M741, S744, N752; mutating these residues weakens NTB activation, defining a tractable activation pocket. | (nadezhdin2023structuralmechanismsof pages 4-5, nadezhdin2023structuralmechanismsof media 0122cc1d, nadezhdin2023structuralmechanismsof media c43cdd43, nadezhdin2023structuralmechanismsof media 5bbe4004, nadezhdin2023structuralmechanismsof media a1a7982d) |
| 2023 pharmacology highlight: inhibitor site | VER155008 and NS8593 were mapped to a vanilloid-like pocket in the TMD at the interface of the S1-S4 domain and pore domain, contributed by the N-terminal part of S3, C-terminal part of S4, S4-S5 linker, and TRP helix. Key residues include A981, M991, W1111, F1118. These inhibitors stabilize the closed state, supporting TRPM7 druggability. | (nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof pages 2-3, nadezhdin2023structuralmechanismsof media 0122cc1d, nadezhdin2023structuralmechanismsof media c43cdd43, nadezhdin2023structuralmechanismsof media 5bbe4004, nadezhdin2023structuralmechanismsof media a1a7982d) |
| Practical application / implementation | Zebrafish trpm7/tct mutants are a practical in vivo model for dissecting divalent-cation homeostasis, synaptic transmission, pigment-cell survival, and renal mineralization. Recent structural mapping of NTB, VER155008, and NS8593 provides a mechanistic framework for using pharmacologic probes in comparative TRPM7 studies, including zebrafish-based functional annotation. | (elizondo2010trpm7regulationof pages 1-2, low2011trpm7isrequired pages 1-2, nadezhdin2023structuralmechanismsof pages 1-2, nadezhdin2023structuralmechanismsof media 0122cc1d) |
Table: This table condenses the main functional annotation points for zebrafish trpm7/Q563W7, combining zebrafish-specific genetics with broader TRPM7 mechanistic and 2023 structural pharmacology evidence. It is useful as a quick-reference map linking domains, ion/kinase function, localization, phenotypes, and modern druggable sites.
Although the report prioritizes 2023 structural advances and zebrafish primary genetics/physiology, some detailed kinase-substrate assignments and intracellular vesicle models are derived from mechanistic studies in other systems and are used here as inference for the zebrafish ortholog (consistent with strong conservation of TRPM7 channel-kinase architecture). Where zebrafish-specific biochemical substrate validation is required, additional targeted zebrafish phosphoproteomics or in vivo substrate assays would be needed beyond the current evidence set. (decker2015trpm7functionin pages 21-25, mittermeier2019thekinasecoupledtrpm7 pages 8-11)
References
(low2011trpm7isrequired pages 1-2): Sean E. Low, Kimberly Amburgey, Eric Horstick, Jeremy Linsley, Shawn M. Sprague, Wilson W. Cui, Weibin Zhou, Hiromi Hirata, Louis Saint-Amant, Richard I. Hume, and John Y. Kuwada. Trpm7 is required within zebrafish sensory neurons for the activation of touch-evoked escape behaviors. The Journal of Neuroscience, 31:11633-11644, Aug 2011. URL: https://doi.org/10.1523/jneurosci.4950-10.2011, doi:10.1523/jneurosci.4950-10.2011. This article has 71 citations.
(elizondo2010trpm7regulationof pages 1-2): Michael R. Elizondo, Erine H. Budi, and David M. Parichy. Trpm7 regulation of in vivo cation homeostasis and kidney function involves stanniocalcin 1 and fgf23. Endocrinology, 151 12:5700-9, Dec 2010. URL: https://doi.org/10.1210/en.2010-0853, doi:10.1210/en.2010-0853. This article has 64 citations and is from a domain leading peer-reviewed journal.
(mcneill2007celldeathof pages 1-2): Matthew S. McNeill, Jennifer Paulsen, Gregory Bonde, Erin Burnight, Mei-Yu Hsu, and Robert A. Cornell. Cell death of melanophores in zebrafish trpm7 mutant embryos depends on melanin synthesis. The Journal of investigative dermatology, 127 8:2020-30, Aug 2007. URL: https://doi.org/10.1038/sj.jid.5700710, doi:10.1038/sj.jid.5700710. This article has 114 citations.
(okada2023celldeathinduction pages 4-5): Yasunobu Okada, Tomohiro Numata, Ravshan Z. Sabirov, Makiko Kashio, Peter G. Merzlyak, and Kaori Sato-Numata. Cell death induction and protection by activation of ubiquitously expressed anion/cation channels. part 3: the roles and properties of trpm2 and trpm7. Frontiers in Cell and Developmental Biology, Sep 2023. URL: https://doi.org/10.3389/fcell.2023.1246955, doi:10.3389/fcell.2023.1246955. This article has 7 citations.
(decker2015trpm7functionin pages 21-25): Amanda R. Decker. Trpm7 function in zebrafish dopaminergic neurons. ArXiv, 2015. URL: https://doi.org/10.17077/etd.7i42ocad, doi:10.17077/etd.7i42ocad. This article has 1 citations.
(nadezhdin2023structuralmechanismsof pages 2-3): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(nadezhdin2023structuralmechanismsof pages 1-2): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(decker2015trpm7functionin pages 17-21): Amanda R. Decker. Trpm7 function in zebrafish dopaminergic neurons. ArXiv, 2015. URL: https://doi.org/10.17077/etd.7i42ocad, doi:10.17077/etd.7i42ocad. This article has 1 citations.
(mittermeier2019thekinasecoupledtrpm7 pages 8-11): Lorenz Mittermeier. The kinase-coupled trpm7 channel is the central gatekeeper of intestinal mineral absorption. Dissertation, Jan 2019. URL: https://doi.org/10.5282/edoc.24107, doi:10.5282/edoc.24107. This article has 0 citations.
(sturgeon2020theroleof pages 15-18): The role of magnesium homeostasis in embryonic melanocytes and dopamine neurons
(nadezhdin2023structuralmechanismsof pages 4-5): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(nethramangalath2024investigationofthe pages 16-20): Thushara Nethramangalath. Investigation of the trpm7 complex in mouse embryonic stem cells. Text, Jan 2024. URL: https://doi.org/10.7282/t3-7gay-vw34, doi:10.7282/t3-7gay-vw34. This article has 0 citations and is from a peer-reviewed journal.
(nadezhdin2023structuralmechanismsof media 0122cc1d): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(nadezhdin2023structuralmechanismsof media a1a7982d): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(nadezhdin2023structuralmechanismsof media c43cdd43): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.
(nadezhdin2023structuralmechanismsof media 5bbe4004): Kirill D. Nadezhdin, Leonor Correia, Chamali Narangoda, Dhilon S. Patel, Arthur Neuberger, Thomas Gudermann, Maria G. Kurnikova, Vladimir Chubanov, and Alexander I. Sobolevsky. Structural mechanisms of trpm7 activation and inhibition. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38362-3, doi:10.1038/s41467-023-38362-3. This article has 81 citations and is from a highest quality peer-reviewed journal.