Abstract
Anıl Ata, Derya Topuz Ata, Zeynep Tuba Odacı
Abstract
Authors
Institutions
No ROR-resolved institution is linked to this work yet.
Provenance
crossref
Confidence 100%
pubmed
Confidence 98%
unpaywall
Confidence 95%
datacite
Confidence 0%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
Analysis of protein complexes using mass spectrometry
10.1038/nrm2208 · 2007
Beyond immunoprecipitation: exploring new interaction spaces with proximity biotinylation
2017
The development of proximity labeling technology and its applications in mammals, plants, and microorganisms
10.1186/s12964-023-01310-1 · 2023
Proximity dependent biotinylation: key enzymes and adaptation to proteomics approaches
10.1074/mcp.r120.001941 · 2020
A comparison of two-hybrid approaches for detecting protein–protein interactions
2017
Tag thy neighbour: nanometre-scale insights into kinetoplastid parasites with proximity dependent biotinylation
10.3389/fcimb.2022.894213 · 2022
A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
10.1083/jcb.201112098 · 2012
Efficient proximity labeling in living cells and organisms with TurboID
10.1038/nbt.4201 · 2018
In vivo interactome profiling by enzyme-catalyzed proximity labeling
10.1186/s13578-021-00542-3 · 2021
MicroID2: a novel biotin ligase enables rapid proximity-dependent proteomics
10.1016/j.mcpro.2022.100256 · 2022
Engineering of UltraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells
10.1038/s42003-022-03604-5 · 2022
Recent advances in proximity labeling-based subcellular proteomic mapping
10.1016/j.mcpro.2026.101520 · 2026
LeishGEM: genome-wide deletion mutant fitness and protein localisations in leishmania
10.1016/j.pt.2024.06.003 · 2024
APEX2 proximity proteomics resolves flagellum subdomains and identifies flagellum tip-specific proteins in Trypanosoma brucei
10.1128/msphere.01090-20 · 2021
Identification of Cdc45-interacting partners uncovers two Leishmania donovani proteins involved in DNA replication
2025
Proteomics of plasma-derived extracellular vesicles from human patients identifies biomarkers for monitoring visceral leishmaniasis therapy
10.3389/fimmu.2025.1646335 · 2025
Contribution of proteomics of Leishmania spp. to the understanding of differentiation, drug resistance mechanisms, vaccine and drug development
10.1016/j.jprot.2011.05.005 · 2011
Moving from unsequenced to sequenced genome: reanalysis of the proteome of Leishmania donovani
10.1016/j.jprot.2013.04.021 · 2014
The protein map of the protozoan parasite leishmania (leishmania) amazonensis, leishmania (Viannia) braziliensis and leishmania (leishmania) infantum during growth phase transition and temperature stress
10.1016/j.jprot.2024.105088 · 2024
Membrane domains and flagellar pocket boundaries are influenced by the cytoskeleton in African trypanosomes
10.1073/pnas.0909289106 · 2009
A global protein interaction network of Leishmania donovani
2025
Global protein interaction network for Trypanosoma cruzi
10.1021/acs.jproteome.5c00649 · 2025
State-of-the-art and future directions in structural proteomics
10.1016/j.mcpro.2025.101065 · 2025
Functional and protein interaction analysis of Nop7 in trypanosomatid parasites
10.1016/j.jprot.2026.105675 · 2026
Quantitative proteomics of intracellular and axenic amastigote-like forms of Trypanosoma cruzi under replicative and non-replicative conditions
2026
An enzymatic cascade enables sensitive and specific proximity labeling proteomics in challenging biological systems
10.1038/s41467-025-65405-8 · 2025
PerTurboID, a targeted in situ method reveals the impact of kinase deletion on its local protein environment in the cytoadhesion complex of malaria-causing parasites
10.7554/elife.86367 · 2023
Intracristal space proteome mapping using super-resolution proximity labeling with isotope-coded probes
10.1038/s41467-025-62756-0 · 2025
Accurate structure prediction of biomolecular interactions with AlphaFold 3
10.1038/s41586-024-07487-w · 2024
Method of the year 2024: spatial proteomics
10.1038/s41592-024-02565-3 · 2024
BioID: a screen for protein–protein interactions
2018
2C-BioID: an advanced two component BioID system for precision mapping of protein interactomes
10.1016/j.isci.2018.11.023 · 2018
Protein translocation as a tool: the current rapamycin story
10.1016/j.febslet.2012.04.061 · 2012
Rapamycin-induced oligomer formation system of FRB–FKBP fusion proteins
10.1016/j.jbiosc.2015.12.004 · 2016
Filling the void: proximity-based labeling of proteins in living cells
10.1016/j.tcb.2016.09.004 · 2016
Comparative application of BioID and TurboID for protein-proximity biotinylation
10.3390/cells9051070 · 2020
Recent advances in proximity-based labeling methods for interactome mapping
10.12688/f1000research.16903.1 · 2019
Split-BioID: a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes
10.1038/ncomms15690 · 2017
Establishment of in vivo proximity labeling with biotin using TurboID in the filamentous fungus Sordaria macrospora
10.1038/s41598-022-22545-x · 2022
Split-TurboID enables contact-dependent proximity labeling in cells
10.1073/pnas.1919528117 · 2020
Cell surface proteomics provides insight into stage-specific remodeling of the host–parasite interface in Trypanosoma brucei
10.1074/mcp.m114.045146 · doi-reference
Architecture of a host–parasite interface: complex targeting mechanisms revealed through proteomics
10.1074/mcp.m114.047647 · doi-reference
Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia
10.1002/anie.200300639 · doi-reference
Bioorthogonal photocatalytic decaging-enabled mitochondrial proteomics
10.1021/jacs.1c09171 · doi-reference
Off-the-shelf proximity biotinylation using ProtA-TurboID
10.1038/s41596-022-00748-w · doi-reference
In vivo discovery of RNA proximal proteins via proximity-dependent biotinylation
10.1080/15476286.2021.1917215 · doi-reference
A new method for studying RNA-binding proteins on specific RNAs
10.21769/bioprotoc.4022 · doi-reference
CBRPP: a new RNA-centric method to study RNA–protein interactions
10.1080/15476286.2021.1873620 · doi-reference
CRISPR-guided proximity labeling of RNA–protein interactions
10.3390/genes13091549 · doi-reference
Reliable identification of protein-protein interactions by crosslinking mass spectrometry
10.1038/s41467-021-23666-z · doi-reference
Meta-analysis defines principles for the design and analysis of co-fractionation mass spectrometry experiments
10.1038/s41592-021-01194-4 · doi-reference
Next-generation Interactomics: considerations for the use of co-elution to measure protein interaction networks
10.1074/mcp.r119.001803 · doi-reference
Protein interaction landscapes revealed by advanced in vivo cross-linking–mass spectrometry
10.1073/pnas.2023360118 · doi-reference
Cross-linking mass spectrometry (XL-MS): an emerging technology for interactomics and structural biology
10.1021/acs.analchem.7b04431 · doi-reference
Complex-centric proteome profiling by SEC-SWATH-MS for the parallel detection of hundreds of protein complexes
10.1038/s41596-020-0332-6 · doi-reference
Ultra-fast label-free quantification and comprehensive proteome coverage with narrow-window data-independent acquisition
10.1038/s41587-023-02099-7 · doi-reference
The future of a myriad of accelerated biodiscoveries lies in AI-powered mass spectrometry and multiomics integration
10.1002/jms.5157 · doi-reference
Proteomics: an in-depth review on recent technical advances and their applications in biomedicine
10.1002/med.22098 · doi-reference
Defeating the trypanosomatid trio: proteomics of the protozoan parasites causing neglected tropical diseases
10.1039/d0md00122h · doi-reference
AlphaFold3: an overview of applications and performance insights
10.3390/ijms26083671 · doi-reference
Discovery and significance of protein–protein interactions in health and disease
10.1016/j.cell.2024.10.038 · doi-reference
DIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes
10.1038/s41592-024-02211-y · doi-reference
A proximity-dependent biotinylation map of a human cell
10.1038/s41586-021-03592-2 · doi-reference
Computational and informatics strategies for identification of specific protein interaction partners in affinity purification mass spectrometry experiments
10.1002/pmic.201100537 · doi-reference
Proteomic analysis of Trypanosoma cruzi spliceosome complex
10.1016/j.jprot.2020.103822 · doi-reference
A cytoskeletal protein complex is essential for division of intracellular amastigotes of leishmania mexicana
10.1074/jbc.ra120.014065 · doi-reference
Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin
10.1073/pnas.2533726123 · doi-reference
Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export
10.1371/journal.pbio.3003024 · doi-reference
Flagellar targeting of an arginine kinase requires a conserved lipidated protein intraflagellar transport pathway in Trypanosoma brucei
10.1074/jbc.ra120.014287 · doi-reference
Basal body protein TbSAF1 is required for microtubule quartet anchorage to the basal bodies in Trypanosoma brucei
10.1128/mbio.00668-20 · doi-reference
FAZ27 cooperates with FLAM3 and ClpGM6 to maintain cell morphology in Trypanosoma brucei
10.1242/jcs.245258 · doi-reference
The CIF1 protein is a master orchestrator of trypanosome cytokinesis that recruits several cytokinesis regulators to the cytokinesis initiation site
10.1074/jbc.ra118.004888 · doi-reference
Identification of TOEFAZ1-interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis
10.1111/mmi.13986 · doi-reference
Faithful chromosome segregation in Trypanosoma brucei requires a cohort of divergent spindle-associated proteins with distinct functions
10.1093/nar/gky557 · doi-reference
Characterization of RBP9 and RBP10, two developmentally regulated RNA-binding proteins in Trypanosoma brucei
10.1098/rsob.160159 · doi-reference
An EF-hand-containing protein in Trypanosoma brucei regulates cytokinesis initiation by maintaining the stability of the cytokinesis initiation factor CIF1
10.1074/jbc.m116.726133 · doi-reference
The trypanosome-specific proteins FPRC and CIF4 regulate cytokinesis initiation by recruiting CIF1 to the cytokinesis initiation site
10.1074/jbc.ra119.010538 · doi-reference
Identification of the interactomes associated with SCD6 and RBP42 proteins in leishmania braziliensis
10.1016/j.jprot.2020.104066 · doi-reference
Proteomic identification of novel cytoskeletal proteins associated with TbPLK, an essential regulator of cell morphogenesis in Trypanosoma brucei
10.1091/mbc.e15-04-0219 · doi-reference
A resource for improved predictions of Trypanosoma and leishmania protein three-dimensional structure
10.1371/journal.pone.0259871 · doi-reference