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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Plan overview
- Verified identity and domain architecture for human RIMBP2 (UniProt O15034) and aligned literature accordingly (no symbol ambiguity detected) (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14, grauel2016rimbindingprotein2 pages 1-2).
- Curated recent primary/review sources (2023–2024 where available) and foundational studies on function, localization, interactions, synapse-type specificity, and phenotypes (wu2023theroleof pages 12-13, alvanos2023quantitativemolecularphysiology pages 25-27, brockmann2020atrioof pages 11-12, brockmann2019rimbp2primessynaptic pages 1-2, grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83).
- Extracted evidence on molecular function (binding partners, domain roles), active-zone localization, knockout effects on release probability and Ca2+ coupling, and synapse-type differences; summarized network/assembly context and disease relevance.

Table: Compact summary table of RIMBP2 (UniProt O15034) covering identity, molecular roles, localization, synapse-specific functions, knockout phenotypes, network context, disease links, and translational implications, with supporting source IDs for evidence.

Comprehensive research report: Human RIMBP2 (UniProt O15034)

1) Key concepts and definitions with current understanding
- Identity and family: RIMBP2 (RIMS-binding protein 2; RIM-BP2) is a presynaptic active-zone scaffold in the RIMBP family. Mammalian RIMBPs possess multiple SH3 domains and multiple fibronectin type III (FN3) domains plus proline-rich regions; RIMBP2 is the dominant CNS isoform in many synapses (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14). RIMBP2’s SH3 domains bind PxxP motifs in CaV channel C-termini and in binding partners; its central C-terminal SH3s form interaction hubs with RIMs and Munc13, supporting vesicle priming and Ca2+-channel tethering (alvanos2023quantitativemolecularphysiology pages 25-27). URLs: Alvanos 2023 (University of Göttingen repository; published 2023-07-17): https://doi.org/10.53846/goediss-10204; Torres & Inestrosa 2018 (Molecular Neurobiology; 2018-07): https://doi.org/10.1007/s12035-017-0661-9 (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14).
- Molecular role (overview): RIMBP2 couples the vesicle release machinery to voltage-gated Ca2+ channels (VGCCs) via direct and indirect interactions—binding RIMs, Munc13-1, Bassoon, and CaV channels (Cav2.1/2.2 at conventional synapses; Cav1.3 at auditory ribbon synapses). This positions channels near release sites, tunes release probability, and supports fast vesicle replenishment (grauel2016rimbindingprotein2 pages 1-2, brockmann2019rimbp2primessynaptic pages 1-2, alvanos2023quantitativemolecularphysiology pages 25-27, wu2023theroleof pages 12-13). URLs: PNAS 2016 (2016-09-27): https://doi.org/10.1073/pnas.1605256113; eLife 2019 (2019-09-06): https://doi.org/10.7554/eLife.43243; Frontiers in Neuroscience 2023 (2023-04-11): https://doi.org/10.3389/fnins.2023.1123561 (grauel2016rimbindingprotein2 pages 1-2, brockmann2019rimbp2primessynaptic pages 1-2, wu2023theroleof pages 12-13).
- Localization: RIMBP2 resides in nanoclusters at presynaptic active zones (AZs) and is present at conventional and ribbon-type synapses (grauel2016rimbindingprotein2 pages 1-2, alvanos2023quantitativemolecularphysiology pages 25-27, butola2017molecularphysiologyof pages 77-83). URLs: PNAS 2016 (2016-09-27): https://doi.org/10.1073/pnas.1605256113; Göttingen thesis 2017 (2017): https://doi.org/10.53846/goediss-6529; Göttingen thesis 2023 (2023-07-17): https://doi.org/10.53846/goediss-10204 (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).

2) Recent developments and latest research (prioritize 2023–2024)
- 2023 synthesis on RIM/RIM-BPs: A 2023 review integrates roles of RIM-BPs (including RIMBP2) as scaffolds linking RIM/Munc13 to CaV channels and highlights evidence from ribbon synapses where RIM-BPs are required for efficient stimulus–secretion coupling and sound encoding (Frontiers in Neuroscience, 2023-04-11) (wu2023theroleof pages 12-13). URL: https://doi.org/10.3389/fnins.2023.1123561 (wu2023theroleof pages 12-13).
- 2023 quantitative active-zone physiology (auditory): A 2023 dissertation compiles quantitative models and experimental literature showing RIM-BP2 organizes CaV topography, supports tight Ca2+–secretion coupling, and in inner hair cell ribbon synapses regulates Cav1.3 number/kinetics to maintain indefatigable release; it also emphasizes RIMBP2–Munc13-1 recruitment at mossy-fiber synapses and multivalent SH3-mediated assemblies (University of Göttingen Repository, 2023-07-17) (alvanos2023quantitativemolecularphysiology pages 25-27). URL: https://doi.org/10.53846/goediss-10204 (alvanos2023quantitativemolecularphysiology pages 25-27).
- Presynapse assembly context: Although not specifically a RIMBP2 functional paper, a broader AZ-assembly perspective remains relevant: vertebrate AZ assembly relies on RIMs, RIM-BPs, Munc13, ELKS, Bassoon, and Liprin-α; RIM-BPs provide a key link between RIMs and CaV channels, supporting coupling (Molecular Neurobiology 2018; conceptual framework used by later studies) (torres2018vertebratepresynapticactive pages 13-14). URL: https://doi.org/10.1007/s12035-017-0661-9 (torres2018vertebratepresynapticactive pages 13-14).

3) Current applications and real-world implementations
- Sensory encoding and hearing: In auditory pathways (endbulb/calyx and hair-cell ribbon synapses), RIMBP2 organizes CaV channel topography, sustains high initial release probability, and supports fast replenishment—attributes necessary for reliable sound onset coding; deficits are predicted to degrade temporal precision of auditory signaling in vivo (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27). URLs: Göttingen thesis 2017 (2017): https://doi.org/10.53846/goediss-6529; Göttingen repository 2023 (2023-07-17): https://doi.org/10.53846/goediss-10204 (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).
- Synapse-type informed targets: Differential reliance on RIMBP2 at mossy-fiber vs CA3–CA1 synapses suggests that therapeutic modulation of RIMBP2–Munc13 versus RIMBP2–CaV interactions might be tailored by synapse class in synaptopathies (brockmann2019rimbp2primessynaptic pages 1-2, brockmann2020atrioof pages 11-12). URLs: eLife 2019 (2019-09-06): https://doi.org/10.7554/eLife.43243; Cell Reports 2020 (2020-08-11): https://doi.org/10.1016/j.celrep.2020.107960 (brockmann2019rimbp2primessynaptic pages 1-2, brockmann2020atrioof pages 11-12).

4) Expert opinions and analysis from authoritative sources
- RIM–RIMBP–Munc13 triad governs release: Expert synthesis of genetic/electrophysiological dissection argues that the RIMs, RIM-BPs and Munc13s form a functional triad governing vesicle priming and channel coupling; RIMBP2’s partnerships can bias synapses toward either higher coupling (channel recruitment) or enhanced priming (Munc13 recruitment), shaping release probability (Cell Reports 2020) (brockmann2020atrioof pages 11-12). URL: https://doi.org/10.1016/j.celrep.2020.107960 (brockmann2020atrioof pages 11-12).
- Active-zone positioning of channels: Super-resolution localization and functional analyses indicate RIMBP2 fine-tunes CaV positioning relative to release sites to set release probability and short-term plasticity (PNAS 2016) (grauel2016rimbindingprotein2 pages 1-2). URL: https://doi.org/10.1073/pnas.1605256113 (grauel2016rimbindingprotein2 pages 1-2).
- Active-zone assembly perspective: Reviews highlight RIMBPs as CaV-tethering scaffolds within the broader AZ network with RIM, Munc13, ELKS, Liprin-α, and Bassoon (Molecular Neurobiology 2018; Frontiers in Neuroscience 2023) (torres2018vertebratepresynapticactive pages 13-14, wu2023theroleof pages 12-13). URLs: https://doi.org/10.1007/s12035-017-0661-9; https://doi.org/10.3389/fnins.2023.1123561 (torres2018vertebratepresynapticactive pages 13-14, wu2023theroleof pages 12-13).

5) Relevant statistics and data from recent studies
- Hippocampal synapses: Loss of RIMBP2 at CA3–CA1 synapses modestly reduces release probability and loosens Ca2+ coupling (increased EGTA sensitivity) without abolishing transmission, consistent with a role in fine-tuning CaV localization (PNAS 2016) (grauel2016rimbindingprotein2 pages 1-2). URL: https://doi.org/10.1073/pnas.1605256113 (grauel2016rimbindingprotein2 pages 1-2).
- Mossy-fiber synapses: RIMBP2 knockout disrupts stabilization of Munc13-1 clusters, impairs vesicle docking/priming, and lowers release probability, with active-zone architecture showing increased distances among RIMBP2/Munc13-1/RIM/Cav2.1 clusters (eLife 2019) (brockmann2019rimbp2primessynaptic pages 1-2). URL: https://doi.org/10.7554/eLife.43243 (brockmann2019rimbp2primessynaptic pages 1-2).
- Auditory synapses: In endbulb/calyx circuits, RIM-BP deficiency decreases initial release probability, shifts short-term plasticity toward facilitation, slows fast replenishment, and reduces docked or membrane-proximal vesicles despite near-normal whole-terminal Ca2+ influx; these phenotypes degrade sound-onset signaling (Göttingen theses 2017, 2023) (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27). URLs: https://doi.org/10.53846/goediss-6529; https://doi.org/10.53846/goediss-10204 (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).

Detailed functional annotation
- Domain architecture and binding partners:
- SH3 and FN3 domains: RIMBP2 contains three SH3 and three FN3 domains with proline-rich segments; SH3 domains mediate PxxP interactions with CaV channel tails and with partners including RIMs and Munc13-1, enabling channel tethering and vesicle priming (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14). URL: https://doi.org/10.53846/goediss-10204; https://doi.org/10.1007/s12035-017-0661-9 (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14).
- RIMs and Munc13-1: Biochemistry and imaging show RIMBP2 associates with RIM and Munc13-1 and is positioned near Bassoon/Munc13-1 nanodomains at the AZ; genetic dissection at MF synapses demonstrates RIMBP2-dependent recruitment/stabilization of Munc13-1 is essential for priming (grauel2016rimbindingprotein2 pages 1-2, brockmann2019rimbp2primessynaptic pages 1-2, brockmann2020atrioof pages 11-12). URLs: https://doi.org/10.1073/pnas.1605256113; https://doi.org/10.7554/eLife.43243; https://doi.org/10.1016/j.celrep.2020.107960 (grauel2016rimbindingprotein2 pages 1-2, brockmann2019rimbp2primessynaptic pages 1-2, brockmann2020atrioof pages 11-12).
- Voltage-gated Ca2+ channels: RIMBP2 fine-tunes CaV channel localization at hippocampal synapses (Cav2.1/2.2 family) and contributes to maintaining large numbers of Cav1.3 at ribbon synapses, promoting tight Ca2+–release coupling and fast replenishment (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27, wu2023theroleof pages 12-13). URLs: https://doi.org/10.1073/pnas.1605256113; https://doi.org/10.53846/goediss-6529; https://doi.org/10.53846/goediss-10204; https://doi.org/10.3389/fnins.2023.1123561 (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27, wu2023theroleof pages 12-13).
- Bassoon and AZ network: Imaging places RIMBP2 near Bassoon; network-level models include RIMBP2 within a hierarchical AZ scaffold with RIM, Munc13, ELKS, liprin-α, and Bassoon (grauel2016rimbindingprotein2 pages 1-2, torres2018vertebratepresynapticactive pages 13-14, brockmann2020atrioof pages 11-12). URLs: https://doi.org/10.1073/pnas.1605256113; https://doi.org/10.1007/s12035-017-0661-9; https://doi.org/10.1016/j.celrep.2020.107960 (grauel2016rimbindingprotein2 pages 1-2, torres2018vertebratepresynapticactive pages 13-14, brockmann2020atrioof pages 11-12).

• Subcellular localization: RIMBP2 is presynaptic and concentrated in the active zone in nanoclusters adjacent to release sites and AZ scaffolds; it is present at both conventional synapses and sensory ribbon synapses (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27). URLs: https://doi.org/10.1073/pnas.1605256113; https://doi.org/10.53846/goediss-6529; https://doi.org/10.53846/goediss-10204 (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).

• Synapse-type specificity and comparative roles:

• CA3–CA1 (Schaffer collateral) synapses: RIMBP2 sets release probability by fine-tuning CaV positioning; its loss mildly loosens Ca2+ coupling and increases release variability without large effects on RRP size (grauel2016rimbindingprotein2 pages 1-2). URL: https://doi.org/10.1073/pnas.1605256113 (grauel2016rimbindingprotein2 pages 1-2).
• Hippocampal mossy-fiber synapses: RIMBP2 is critical for recruitment/stabilization of Munc13-1, promoting vesicle docking/priming; its loss causes severe transmission deficits, reflecting MF-specific AZ architecture (brockmann2019rimbp2primessynaptic pages 1-2). URL: https://doi.org/10.7554/eLife.43243 (brockmann2019rimbp2primessynaptic pages 1-2).

• Auditory endbulb/calyx and ribbon synapses: RIM-BP2 deficiency reduces initial release probability, slows fast replenishment, and changes STP toward facilitation; at inner hair-cell ribbon synapses, RIM-BP2 supports Cav1.3 channel abundance and indefatigable release, underpinning reliable sound encoding (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27). URLs: https://doi.org/10.53846/goediss-6529; https://doi.org/10.53846/goediss-10204 (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).

• Knockout/deficiency phenotypes (mechanistic):

• Reduced initial release probability and increased EGTA sensitivity (looser Ca2+–vesicle coupling) (butola2017molecularphysiologyof pages 77-83, grauel2016rimbindingprotein2 pages 1-2).
• Fewer docked/membrane-proximal vesicles; slowed fast vesicle replenishment after RRP depletion (butola2017molecularphysiologyof pages 77-83).
• Disrupted Munc13-1 clustering and impaired priming at MF synapses (brockmann2019rimbp2primessynaptic pages 1-2).
  URLs: 2017 thesis (2017): https://doi.org/10.53846/goediss-6529; PNAS 2016 (2016-09-27): https://doi.org/10.1073/pnas.1605256113; eLife 2019 (2019-09-06): https://doi.org/10.7554/eLife.43243 (butola2017molecularphysiologyof pages 77-83, grauel2016rimbindingprotein2 pages 1-2, brockmann2019rimbp2primessynaptic pages 1-2).

Disease relevance and variants
- Neurodevelopmental and psychiatric relevance: RIMBP2 is consistently placed in the synaptic active-zone machinery that is frequently implicated across neurodevelopmental disorders; expert reviews emphasize AZ scaffold disruptions (RIM/RIMBP/Munc13) as a mechanism class in synaptopathies (wu2023theroleof pages 12-13, torres2018vertebratepresynapticactive pages 13-14). URLs: Frontiers in Neuroscience 2023 (2023-04-11): https://doi.org/10.3389/fnins.2023.1123561; Molecular Neurobiology 2018 (2018-07): https://doi.org/10.1007/s12035-017-0661-9 (wu2023theroleof pages 12-13, torres2018vertebratepresynapticactive pages 13-14).
- Hearing and auditory function: Experimental models show RIM-BP2 deficiency degrades sound-onset coding, consistent with potential relevance to hearing phenotypes when AZ coupling is perturbed (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27). URLs: https://doi.org/10.53846/goediss-6529; https://doi.org/10.53846/goediss-10204 (butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).
- Genetic parallels in the family: While specific human RIMBP2 pathogenic variants are not detailed in the cited evidence set, the close paralog RIMBP1 (TSPOAP1) has biallelic loss-of-function variants causing autosomal recessive dystonia, underscoring the clinical importance of RIMBP scaffolds; this supports biological plausibility for RIMBP2’s disease relevance (Journal of Clinical Investigation 2021-04-01) (torres2018vertebratepresynapticactive pages 13-14). URL (for family context): https://doi.org/10.1172/JCI140625 (torres2018vertebratepresynapticactive pages 13-14).

Pathway and mechanistic integration
- RIMBP2 operates within the active-zone scaffold that organizes vesicle priming and Ca2+-channel coupling. The RIM zinc-finger activates Munc13, while RIMBP2’s SH3/FN3 modules anchor CaV channels and bind RIM/Munc13; this triad establishes the spatial coupling that sets release probability and short-term plasticity. Synapse-type differences in AZ architecture determine whether RIMBP2’s priming or channel-coupling role dominates (brockmann2020atrioof pages 11-12, brockmann2019rimbp2primessynaptic pages 1-2, grauel2016rimbindingprotein2 pages 1-2, torres2018vertebratepresynapticactive pages 13-14). URLs: https://doi.org/10.1016/j.celrep.2020.107960; https://doi.org/10.7554/eLife.43243; https://doi.org/10.1073/pnas.1605256113; https://doi.org/10.1007/s12035-017-0661-9 (brockmann2020atrioof pages 11-12, brockmann2019rimbp2primessynaptic pages 1-2, grauel2016rimbindingprotein2 pages 1-2, torres2018vertebratepresynapticactive pages 13-14).

Conclusions (functional annotation)
- Primary role: RIMBP2 is a presynaptic active-zone scaffold that coordinates vesicle priming (via Munc13-1 recruitment) and Ca2+-channel positioning (via interaction with RIMs and direct CaV binding), thereby determining release probability and the timing precision of neurotransmission. This is not an enzyme or transporter but an adapter/scaffold whose domain architecture (SH3/FN3) and multivalent interactions are essential for its function (grauel2016rimbindingprotein2 pages 1-2, brockmann2020atrioof pages 11-12, brockmann2019rimbp2primessynaptic pages 1-2, alvanos2023quantitativemolecularphysiology pages 25-27).
- Location of function: Presynaptic active zones of central synapses and sensory ribbon synapses (inner hair cells); enriched in AZ nanoclusters adjacent to Bassoon and Munc13-1 (grauel2016rimbindingprotein2 pages 1-2, butola2017molecularphysiologyof pages 77-83, alvanos2023quantitativemolecularphysiology pages 25-27).
- Pathways: Neurotransmitter release pathway at the active zone; vesicle docking/priming and Ca2+-triggered exocytosis via RIM–RIMBP2–Munc13 axis and CaV channel tethering (brockmann2020atrioof pages 11-12, torres2018vertebratepresynapticactive pages 13-14).

Limitations and open questions
- Human genetic data specifically for RIMBP2 remain limited in the cited set; while AZ scaffolding function strongly supports disease relevance, definitive catalogs of RIMBP2 variants and penetrance estimates will require targeted human genetics studies and curated databases beyond the present evidence (wu2023theroleof pages 12-13, torres2018vertebratepresynapticactive pages 13-14). URLs: https://doi.org/10.3389/fnins.2023.1123561; https://doi.org/10.1007/s12035-017-0661-9 (wu2023theroleof pages 12-13, torres2018vertebratepresynapticactive pages 13-14).

Verification of requested identity constraints
- Gene symbol/protein: Literature corresponds to RIMBP2 (RIM-BP2; RIMS-binding protein 2) with SH3/FN3 organization as provided; no conflicting symbol usage encountered (alvanos2023quantitativemolecularphysiology pages 25-27, grauel2016rimbindingprotein2 pages 1-2).
- Organism: Evidence primarily from mouse functional models and vertebrate reviews, applied to human ortholog RIMBP2; domain/family architecture and interactions are conserved and match the human UniProt entry (alvanos2023quantitativemolecularphysiology pages 25-27, torres2018vertebratepresynapticactive pages 13-14, grauel2016rimbindingprotein2 pages 1-2).

References (URLs and dates)
- Grauel MK et al. PNAS, 2016-09-27. RIMBP2 regulates release probability by fine-tuning calcium channel localization at hippocampal synapses. https://doi.org/10.1073/pnas.1605256113 (grauel2016rimbindingprotein2 pages 1-2)
- Brockmann MM et al. eLife, 2019-09-06. RIM-BP2 primes synaptic vesicles via recruitment of Munc13-1 at hippocampal mossy fiber synapses. https://doi.org/10.7554/eLife.43243 (brockmann2019rimbp2primessynaptic pages 1-2)
- Brockmann MM et al. Cell Reports, 2020-08-11. A trio of active zone proteins comprised of RIM-BPs, RIMs, and Munc13s governs neurotransmitter release. https://doi.org/10.1016/j.celrep.2020.107960 (brockmann2020atrioof pages 11-12)
- Butola T. PhD thesis, University Göttingen, 2017. Molecular physiology of signal transmission along the auditory pathway. https://doi.org/10.53846/goediss-6529 (butola2017molecularphysiologyof pages 77-83)
- Alvanos T. Dissertation, University Göttingen, 2023-07-17. Quantitative molecular physiology at active zones of calyceal synapses of the auditory pathway. https://doi.org/10.53846/goediss-10204 (alvanos2023quantitativemolecularphysiology pages 25-27)
- Wu S et al. Frontiers in Neuroscience, 2023-04-11. The role of RIM in neurotransmitter release. https://doi.org/10.3389/fnins.2023.1123561 (wu2023theroleof pages 12-13)
- Torres VI, Inestrosa NC. Molecular Neurobiology, 2018-07. Vertebrate presynaptic active zone assembly. https://doi.org/10.1007/s12035-017-0661-9 (torres2018vertebratepresynapticactive pages 13-14)

References

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2. (torres2018vertebratepresynapticactive pages 13-14): Viviana I. Torres and Nibaldo C. Inestrosa. Vertebrate presynaptic active zone assembly: a role accomplished by diverse molecular and cellular mechanisms. Molecular Neurobiology, 55:4513-4528, Jul 2018. URL: https://doi.org/10.1007/s12035-017-0661-9, doi:10.1007/s12035-017-0661-9. This article has 30 citations and is from a peer-reviewed journal.

3. (grauel2016rimbindingprotein2 pages 1-2): M. Katharina Grauel, Marta Maglione, Suneel Reddy-Alla, Claudia G. Willmes, Marisa M. Brockmann, Thorsten Trimbuch, Tanja Rosenmund, Maria Pangalos, Gülçin Vardar, Alexander Stumpf, Alexander M. Walter, Benjamin R. Rost, Britta J. Eickholt, Volker Haucke, Dietmar Schmitz, Stephan J. Sigrist, and Christian Rosenmund. Rim-binding protein 2 regulates release probability by fine-tuning calcium channel localization at murine hippocampal synapses. Proceedings of the National Academy of Sciences, 113:11615-11620, Sep 2016. URL: https://doi.org/10.1073/pnas.1605256113, doi:10.1073/pnas.1605256113. This article has 115 citations and is from a highest quality peer-reviewed journal.

4. (wu2023theroleof pages 12-13): Shanshan Wu, Jiali Fan, Fajuan Tang, Lin Chen, Xiaoyan Zhang, Dongqiong Xiao, and Xihong Li. The role of rim in neurotransmitter release: promotion of synaptic vesicle docking, priming, and fusion. Frontiers in Neuroscience, Apr 2023. URL: https://doi.org/10.3389/fnins.2023.1123561, doi:10.3389/fnins.2023.1123561. This article has 23 citations and is from a peer-reviewed journal.

5. (brockmann2020atrioof pages 11-12): Marisa M. Brockmann, Fereshteh Zarebidaki, Marcial Camacho, M. Katharina Grauel, Thorsten Trimbuch, Thomas C. Südhof, and Christian Rosenmund. A trio of active zone proteins comprised of rim-bps, rims, and munc13s governs neurotransmitter release. Cell reports, 32 5:107960, Aug 2020. URL: https://doi.org/10.1016/j.celrep.2020.107960, doi:10.1016/j.celrep.2020.107960. This article has 57 citations and is from a highest quality peer-reviewed journal.

6. (brockmann2019rimbp2primessynaptic pages 1-2): Marisa M Brockmann, Marta Maglione, Claudia G Willmes, Alexander Stumpf, Boris A Bouazza, Laura M Velasquez, M Katharina Grauel, Prateep Beed, Martin Lehmann, Niclas Gimber, Jan Schmoranzer, Stephan J Sigrist, Christian Rosenmund, and Dietmar Schmitz. Rim-bp2 primes synaptic vesicles via recruitment of munc13-1 at hippocampal mossy fiber synapses. eLife, Sep 2019. URL: https://doi.org/10.7554/elife.43243, doi:10.7554/elife.43243. This article has 67 citations and is from a domain leading peer-reviewed journal.

7. (butola2017molecularphysiologyof pages 77-83): Tanvi Butola. Molecular physiology of signal transmission along the auditory pathway. PhD thesis, University Goettingen Repository, 2017. URL: https://doi.org/10.53846/goediss-6529, doi:10.53846/goediss-6529.

Citations

1. alvanos2023quantitativemolecularphysiology pages 25-27
2. torres2018vertebratepresynapticactive pages 13-14
3. brockmann2020atrioof pages 11-12
4. wu2023theroleof pages 12-13
5. butola2017molecularphysiologyof pages 77-83
6. https://doi.org/10.53846/goediss-10204;
7. https://doi.org/10.1007/s12035-017-0661-9
8. https://doi.org/10.1073/pnas.1605256113;
9. https://doi.org/10.7554/eLife.43243;
10. https://doi.org/10.3389/fnins.2023.1123561
11. https://doi.org/10.53846/goediss-6529;
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13. https://doi.org/10.1016/j.celrep.2020.107960
14. https://doi.org/10.1073/pnas.1605256113
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16. https://doi.org/10.7554/eLife.43243
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18. https://doi.org/10.1172/JCI140625
19. https://doi.org/10.1016/j.celrep.2020.107960;
20. https://doi.org/10.53846/goediss-6529
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