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Novel Bilobe Components in Trypanosoma brucei Identified Using Proximity-Dependent Biotinylation

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/bf00390368openalex-snapshot
Electron microscopy observations on Trypanosoma brucei: Freeze-cleaving and thin-sectioning study of the apical part of the flagellar pocket
inferredcites →https://doi.org/10.1016/j.jnutbio.2005.03.017openalex-snapshot
Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase
inferredcites →https://doi.org/10.1016/j.molbiopara.2009.05.001openalex-snapshot
The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein
inferredcites →https://doi.org/10.1016/j.protis.2007.08.005openalex-snapshot
A Repetitive Protein Essential for the Flagellum Attachment Zone Filament Structure and Function in Trypanosoma brucei
inferredcites →https://doi.org/10.1016/s0021-9258(18)93825-1openalex-snapshot
The Enzymatic Synthesis of Holotranscarboxylase from Apotranscarboxylase and (+)-Biotin
inferredcites →https://doi.org/10.1016/s0166-6851(99)00002-xopenalex-snapshot
A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
inferredcites →https://doi.org/10.1016/s1369-5274(03)00092-4openalex-snapshot
Host–parasite interactions and trypanosome morphogenesis: a flagellar pocketful of goodies
inferredcites →https://doi.org/10.1038/nature04541openalex-snapshot
Flagellar motility is required for the viability of the bloodstream trypanosome
inferredcites →https://doi.org/10.1074/jbc.m808859200openalex-snapshot
Combining RNA Interference Mutants and Comparative Proteomics to Identify Protein Components and Dependences in a Eukaryotic Flagellum
inferredcites →https://doi.org/10.1083/jcb.128.6.1163openalex-snapshot
Microtubule polarity and dynamics in the control of organelle positioning, segregation, and cytokinesis in the trypanosome cell cycle.
inferredcites →https://doi.org/10.1083/jcb.201112098openalex-snapshot
A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
inferredcites →https://doi.org/10.1091/mbc.e07-08-0749openalex-snapshot
Intraflagellar Transport and Functional Analysis of Genes Required for Flagellum Formation in Trypanosomes
inferredcites →https://doi.org/10.1093/nar/gkp851openalex-snapshot
TriTrypDB: a functional genomic resource for the Trypanosomatidae
inferredcites →https://doi.org/10.1098/rstb.1989.0037openalex-snapshot
The cell division cycle of Trypanosoma brucei brucei : timing of event markers and cytoskeletal modulations
inferredcites →https://doi.org/10.1101/gr.115089.110openalex-snapshot
High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome
inferredcites →https://doi.org/10.1110/ps.9.8.1530openalex-snapshot
Function of a conserved sequence motif in biotin holoenzyme synthetases
inferredcites →https://doi.org/10.1111/j.1365-2958.2012.07998.xopenalex-snapshot
An interplay between Centrin2 and Centrin4 on the bi‐lobed structure in Trypanosoma brucei
inferredcites →https://doi.org/10.1111/j.1365-2958.2012.08008.xopenalex-snapshot
The Trypanosoma brucei AIR9‐like protein is cytoskeleton‐associated and is required for nucleus positioning and accurate cleavage furrow placement
inferredcites →https://doi.org/10.1126/science.1119969openalex-snapshot
Golgi Duplication in Trypanosoma brucei Requires Centrin2
inferredcites →https://doi.org/10.1128/ec.00298-10openalex-snapshot
Structure-Function Analysis of Dynein Light Chain 1 Identifies Viable Motility Mutants in Bloodstream-Form Trypanosoma brucei
inferredcites →https://doi.org/10.1128/ec.05287-11openalex-snapshot
Morphology of the Trypanosome Bilobe, a Novel Cytoskeletal Structure
inferredcites →https://doi.org/10.1146/annurev.micro.53.1.629openalex-snapshot
The Cytoskeleton of Trypanosomatid Parasites
inferredcites →https://doi.org/10.1242/jcs.00938openalex-snapshot
Kinetics of endocytosis and recycling of the GPI-anchored variant surface glycoprotein inTrypanosoma brucei
inferredcites →https://doi.org/10.1242/jcs.030643openalex-snapshot
Centrin4 coordinates cell and nuclear division inT. brucei
inferredcites →https://doi.org/10.1242/jcs.045740openalex-snapshot
Three-dimensional cellular architecture of the flagellar pocket and associated cytoskeleton in trypanosomes revealed by electron microscope tomography
inferredcites →https://doi.org/10.1242/jcs.074161openalex-snapshot
Basal body movements orchestrate membrane organelle division and cell morphogenesis in Trypanosoma brucei
inferredcites →https://doi.org/10.1242/jcs.087676openalex-snapshot
A coiled-coil- and C2-domain-containing protein is required for FAZ assembly and cell morphology in Trypanosoma brucei
inferredcites →https://doi.org/10.1242/jcs.5.1.163openalex-snapshot
On the surface coat and flagellar adhesion in trypanosomes
inferredcites →https://doi.org/10.1371/journal.pbio.0060105openalex-snapshot
Biogenesis of the Trypanosome Endo-Exocytotic Organelle Is Cytoskeleton Mediated
inferredcites →https://doi.org/10.1371/journal.pone.0009660openalex-snapshot
A Comparative Proteomic Analysis Reveals a New Bi-Lobe Protein Required for Bi-Lobe Duplication and Cell Division in Trypanosoma brucei

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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BioID: A Screen for Protein‐Protein Interactions
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Mass Spectrometry‐Based Methods to Investigate Protein–Protein Interactions in Cells and Their Application in Drug Discovery
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BioID: A Screen for Protein‐Protein Interactions
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Identifying Protein‐Protein Interactions by Proximity Biotinylation with AirID and splitAirID
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Meet the neighbors: Mapping local protein interactomes by proximity‐dependent labeling with BioID
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Proximity‐dependent labeling methods for proteomic profiling in living cells
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Proximity‐dependent labeling methods for proteomic profiling in living cells: An update
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Context-Specific and Proximity-Dependent Labeling for the Proteomic Analysis of Spatiotemporally Defined Protein Complexes with Split-BioID
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Identifying Protein-Protein Associations at the Nuclear Envelope with BioID
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BioID: A Method to Generate a History of Protein Associations
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BioID as a Tool for Protein-Proximity Labeling in Living Cells
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Proximity Labeling of the Chlamydia trachomatis Inclusion Membrane
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Cell Biology for Immune Evasion: Organizing Antigenic Variation, Surfaces, Trafficking, and Cellular Structures in Trypanosoma brucei
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Marked by association: techniques for proximity-dependent labeling of proteins in eukaryotic cells
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Proteomik-Analyse von dynamischen Proteinkomplexen
inferred← citeshttps://doi.org/10.1016/b978-0-12-800097-7.00004-xopenalex-snapshot
New Insights into the Molecular Mechanisms of Mitosis and Cytokinesis in Trypanosomes
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Proximity labeling approaches to study protein complexes during virus infection
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Probing mammalian centrosome structure using BioID proximity-dependent biotinylation
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BioID Identification of Lamin-Associated Proteins
inferred← citeshttps://doi.org/10.1016/bs.mie.2015.09.007openalex-snapshot
Proximity-Dependent Biotin Identification (BioID) in Dictyostelium Amoebae
inferred← citeshttps://doi.org/10.1016/j.bbadis.2016.04.003openalex-snapshot
Exclusive expression of the Rab11 effector SH3TC2 in Schwann cells links integrin-α6 and myelin maintenance to Charcot-Marie-Tooth disease type 4C
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The development of BioID: A tool for proximity proteomics in living cells
inferred← citeshttps://doi.org/10.1016/j.cub.2014.01.067openalex-snapshot
Proximity Interactions among Centrosome Components Identify Regulators of Centriole Duplication
inferred← citeshttps://doi.org/10.1016/j.ijmm.2017.07.007openalex-snapshot
Identification of novel parasitophorous vacuole proteins in P. falciparum parasites using BioID
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102647openalex-snapshot
A novel connection between Trypanosoma brucei mitochondrial proteins TbTim17 and TbTRAP1 is discovered using Biotinylation Identification (BioID)
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102726openalex-snapshot
Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.105340openalex-snapshot
The microtubule quartet protein SNAP1 in Trypanosoma brucei facilitates flagellum and cell division plane positioning by promoting basal body segregation
inferred← citeshttps://doi.org/10.1016/j.jprot.2014.09.011openalex-snapshot
Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes
inferred← citeshttps://doi.org/10.1016/j.jprot.2014.09.029openalex-snapshot
BioID identifies novel c-MYC interacting partners in cultured cells and xenograft tumors
inferred← citeshttps://doi.org/10.1016/j.jprot.2026.105739openalex-snapshot
Integrating high-resolution proximity labelling with orthogonal interactome benchmarks: Insights from Kinetoplastid systems
inferred← citeshttps://doi.org/10.1016/j.mcpro.2021.100128openalex-snapshot
A Toolbox for Efficient Proximity-Dependent Biotinylation in Zebrafish Embryos
inferred← citeshttps://doi.org/10.1016/j.mcpro.2021.100186openalex-snapshot
Subcellular Transcriptomics and Proteomics: A Comparative Methods Review
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2016.08.001openalex-snapshot
A unified approach towards Trypanosoma brucei functional genomics using Gibson assembly
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2023.111596openalex-snapshot
RNA editing catalytic complexes edit multiple mRNA sites non-processively in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1016/j.pt.2015.12.010openalex-snapshot
The Flagellum Attachment Zone: ‘The Cellular Ruler’ of Trypanosome Morphology
inferred← citeshttps://doi.org/10.1016/j.pt.2020.11.005openalex-snapshot
Trypanosomatid Flagellar Pocket from Structure to Function
inferred← citeshttps://doi.org/10.1016/j.tcb.2016.09.004openalex-snapshot
Filling the Void: Proximity-Based Labeling of Proteins in Living Cells
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Study on the interaction protein of transcription factor Smad3 based on TurboID proximity labeling technology
inferred← citeshttps://doi.org/10.1016/j.yjsbx.2020.100033openalex-snapshot
In situ structural analysis of the flagellum attachment zone in Trypanosoma brucei using cryo-scanning transmission electron tomography
inferred← citeshttps://doi.org/10.1021/pr500196bopenalex-snapshot
In Vivo Proximity Labeling for the Detection of Protein–Protein and Protein–RNA Interactions
inferred← citeshttps://doi.org/10.1021/pr500387mopenalex-snapshot
Proteomic Analysis of the EWS-Fli-1 Interactome Reveals the Role of the Lysosome in EWS-Fli-1 Turnover
inferred← citeshttps://doi.org/10.1038/nbt.4201openalex-snapshot
Efficient proximity labeling in living cells and organisms with TurboID
inferred← citeshttps://doi.org/10.1038/nprot.2016.018openalex-snapshot
Spatially resolved proteomic mapping in living cells with the engineered peroxidase APEX2
inferred← citeshttps://doi.org/10.1038/s41386-020-00840-3openalex-snapshot
Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau
inferred← citeshttps://doi.org/10.1038/s41467-022-33108-zopenalex-snapshot
A multi-adenylate cyclase regulator at the flagellar tip controls African trypanosome transmission
inferred← citeshttps://doi.org/10.1038/s41592-020-01010-5openalex-snapshot
Deciphering molecular interactions by proximity labeling
inferred← citeshttps://doi.org/10.1038/srep35826openalex-snapshot
Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation
inferred← citeshttps://doi.org/10.1039/d5cs00381dopenalex-snapshot
Chemical proteomics for a comprehensive understanding of functional activity and the interactome
inferred← citeshttps://doi.org/10.1042/bsr20254047openalex-snapshot
The cytoskeleton of pathogenic protists
inferred← citeshttps://doi.org/10.1042/bst20160112openalex-snapshot
The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
inferred← citeshttps://doi.org/10.1073/pnas.1406459111openalex-snapshot
Probing nuclear pore complex architecture with proximity-dependent biotinylation
inferred← citeshttps://doi.org/10.1073/pnas.1703553114openalex-snapshot
Protein diversity in discrete structures at the distal tip of the trypanosome flagellum
inferred← citeshttps://doi.org/10.1074/jbc.m115.694109openalex-snapshot
SAS-4 Protein in Trypanosoma brucei Controls Life Cycle Transitions by Modulating the Length of the Flagellum Attachment Zone Filament
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An EF-hand-containing Protein in Trypanosoma brucei Regulates Cytokinesis Initiation by Maintaining the Stability of the Cytokinesis Initiation Factor CIF1
inferred← citeshttps://doi.org/10.1074/jbc.m116.757112openalex-snapshot
The Major Protein Arginine Methyltransferase in Trypanosoma brucei Functions as an Enzyme-Prozyme Complex
inferred← citeshttps://doi.org/10.1074/jbc.ra118.004888openalex-snapshot
The CIF1 protein is a master orchestrator of trypanosome cytokinesis that recruits several cytokinesis regulators to the cytokinesis initiation site
inferred← citeshttps://doi.org/10.1074/jbc.ra118.007074openalex-snapshot
Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4
inferred← citeshttps://doi.org/10.1074/jbc.ra120.014065openalex-snapshot
A cytoskeletal protein complex is essential for division of intracellular amastigotes of Leishmania mexicana
inferred← citeshttps://doi.org/10.1074/jbc.ra120.014237openalex-snapshot
Maintenance of hook complex integrity and centrin arm assembly facilitates flagellum inheritance in Trypanosoma brucei
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Capturing the Asc1p/Receptor for Activated C Kinase 1 (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast
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Protein Neighbors and Proximity Proteomics
inferred← citeshttps://doi.org/10.1091/mbc.e12-12-0911openalex-snapshot
Polo-like kinase phosphorylation of bilobe-resident TbCentrin2 facilitates flagellar inheritance inTrypanosoma brucei
inferred← citeshttps://doi.org/10.1091/mbc.e14-11-1530openalex-snapshot
SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
inferred← citeshttps://doi.org/10.1091/mbc.e15-04-0219openalex-snapshot
Proteomic identification of novel cytoskeletal proteins associated with TbPLK, an essential regulator of cell morphogenesis inTrypanosoma brucei
inferred← citeshttps://doi.org/10.1091/mbc.e15-12-0844openalex-snapshot
An improved smaller biotin ligase for BioID proximity labeling
inferred← citeshttps://doi.org/10.1093/g3journal/jkab077openalex-snapshot
Highly effective proximate labeling in Drosophila
inferred← citeshttps://doi.org/10.1098/rsob.130023openalex-snapshot
Evolutionary cell biology of chromosome segregation: insights from trypanosomes
inferred← citeshttps://doi.org/10.1098/rsob.160159openalex-snapshot
Characterization of RBP9 and RBP10, two developmentally regulated RNA-binding proteins in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1101/2019.12.28.889931openalex-snapshot
Discovery of new mitochondrial DNA segregation machinery components in Trypanosoma brucei : a comparison of three approaches
inferred← citeshttps://doi.org/10.1101/2021.07.18.452872openalex-snapshot
Intrabody induced cell death by targeting the T. brucei cytoskeletal protein Tb BILBO1
inferred← citeshttps://doi.org/10.1101/2022.03.15.484455openalex-snapshot
Characterisation of TbSmee1 indicates that endocytosis is required for access of surface-bound cargo to the trypanosome flagellar pocket
inferred← citeshttps://doi.org/10.1101/2025.03.23.644790openalex-snapshot
Flagellar pocket collar biogenesis: Cytoskeletal organization and novel structures in a unicellular parasite
inferred← citeshttps://doi.org/10.1101/826180openalex-snapshot
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats
inferred← citeshttps://doi.org/10.1111/cmi.12838openalex-snapshot
Identification and characterisation of a Theileria annulata proline-rich microtubule and SH3 domain-interacting protein (TaMISHIP) that forms a complex with CLASP1, EB1, and CD2AP at the schizont surface
inferred← citeshttps://doi.org/10.1111/mmi.13885openalex-snapshot
TbSmee1 regulates hook complex morphology and the rate of flagellar pocket uptake in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1111/mmi.13986openalex-snapshot
Identification of TOEFAZ1‐interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis
inferred← citeshttps://doi.org/10.1111/mmi.14958openalex-snapshot
Kinetoplastid‐specific X2 ‐family kinesins interact with a kinesin‐like pleckstrin homology domain protein that localizes to the trypanosomal microtubule quartet
inferred← citeshttps://doi.org/10.1124/mol.116.106906openalex-snapshot
AEE788 Inhibits Basal Body Assembly and Blocks DNA Replication in the African Trypanosome
inferred← citeshttps://doi.org/10.1126/science.1230593openalex-snapshot
Proteomic Mapping of Mitochondria in Living Cells via Spatially Restricted Enzymatic Tagging
inferred← citeshttps://doi.org/10.1128/ec.00094-15openalex-snapshot
A MORN Repeat Protein Facilitates Protein Entry into the Flagellar Pocket of Trypanosoma brucei
inferred← citeshttps://doi.org/10.1128/iai.00442-22openalex-snapshot
Microbial Pathogenesis in the Era of Spatial Omics
inferred← citeshttps://doi.org/10.1128/mbio.00668-20openalex-snapshot
Basal Body Protein TbSAF1 Is Required for Microtubule Quartet Anchorage to the Basal Bodies in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1128/mbio.01352-21openalex-snapshot
A DOT1B/Ribonuclease H2 Protein Complex Is Involved in R-Loop Processing, Genomic Integrity, and Antigenic Variation in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1128/mbio.02120-16openalex-snapshot
Proximity Interactions among Basal Body Components in Trypanosoma brucei Identify Novel Regulators of Basal Body Biogenesis and Inheritance
inferred← citeshttps://doi.org/10.1128/mbio.02357-14openalex-snapshot
Novel Components of the Toxoplasma Inner Membrane Complex Revealed by BioID
inferred← citeshttps://doi.org/10.1128/mbio.02634-24openalex-snapshot
An orphan kinesin in Trypanosoma brucei regulates hook complex assembly and Golgi biogenesis
inferred← citeshttps://doi.org/10.1128/msphere.00522-17openalex-snapshot
BioID Reveals Novel Proteins of the Plasmodium Parasitophorous Vacuole Membrane
inferred← citeshttps://doi.org/10.1128/msphere.01090-20openalex-snapshot
APEX2 Proximity Proteomics Resolves Flagellum Subdomains and Identifies Flagellum Tip-Specific Proteins in Trypanosoma brucei
inferred← citeshttps://doi.org/10.11606/t.17.2018.tde-07062017-101013openalex-snapshot
Caracterização celular e molecular das proteínas gigantes do citoesqueleto de Trypanosoma brucei
inferred← citeshttps://doi.org/10.1186/s12915-019-0626-8openalex-snapshot
Transcriptome, proteome and draft genome of Euglena gracilis
inferred← citeshttps://doi.org/10.1186/s12964-023-01310-1openalex-snapshot
The development of proximity labeling technology and its applications in mammals, plants, and microorganisms
inferred← citeshttps://doi.org/10.1242/jcs.136515openalex-snapshot
Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation
inferred← citeshttps://doi.org/10.1242/jcs.146894openalex-snapshot
The endocytic activity of the flagellar pocket in Trypanosoma brucei is regulated by an adjacent phosphatidylinositol phosphate kinase
inferred← citeshttps://doi.org/10.1242/jcs.148015openalex-snapshot
The bi-lobe-associated LRRP1 regulates Ran activity in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1242/jcs.166447openalex-snapshot
A dynamic coordination of flagellum and cytoplasmic cytoskeleton assembly specifies cell morphogenesis in trypanosomes
inferred← citeshttps://doi.org/10.1242/jcs.168377openalex-snapshot
Assembly and maintenance of the flagellum attachment zone filament in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1242/jcs.171645openalex-snapshot
Flagellum attachment zone protein modulation and regulation of cell shape in Trypanosoma brucei life cycle transitions
inferred← citeshttps://doi.org/10.1242/jcs.183152openalex-snapshot
Flagellar pocket restructuring through theLeishmanialife cycle involves a discrete flagellum attachment zone
inferred← citeshttps://doi.org/10.1242/jcs.194308openalex-snapshot
Giant FAZ10 is required for flagellum attachment zone stabilization and furrow positioning in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1242/jcs.219071openalex-snapshot
The unusual flagellar-targeting mechanism and functions of the trypanosome ortholog of the ciliary GTPase Arl13b
inferred← citeshttps://doi.org/10.1242/jcs.261548openalex-snapshot
Characterisation of TbSmee1 suggests endocytosis allows surface-bound cargo to enter the trypanosome flagellar pocket
inferred← citeshttps://doi.org/10.12688/f1000research.16903.1openalex-snapshot
Recent advances in proximity-based labeling methods for interactome mapping
inferred← citeshttps://doi.org/10.1360/ssv-2024-0151openalex-snapshot
Protein-protein interaction techniques—a powerful tool for functional genomics
inferred← citeshttps://doi.org/10.1371/journal.pbio.2005895openalex-snapshot
Integrative proteomics and bioinformatic prediction enable a high-confidence apicoplast proteome in malaria parasites
inferred← citeshttps://doi.org/10.1371/journal.pntd.0008568openalex-snapshot
A comparison of three approaches for the discovery of novel tripartite attachment complex proteins in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1371/journal.pntd.0014511openalex-snapshot
Novel binding partners of the Vacuolar Transporter Chaperone (VTC) complex in Acidocalcisomes of Leishmania tarentolae
inferred← citeshttps://doi.org/10.1371/journal.pone.0234918openalex-snapshot
ZapE/Afg1 interacts with Oxa1 and its depletion causes a multifaceted phenotype
inferred← citeshttps://doi.org/10.1371/journal.pone.0242677openalex-snapshot
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats
inferred← citeshttps://doi.org/10.1371/journal.ppat.1004654openalex-snapshot
BILBO1 Is a Scaffold Protein of the Flagellar Pocket Collar in the Pathogen Trypanosoma brucei
inferred← citeshttps://doi.org/10.1371/journal.ppat.1006710openalex-snapshot
Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1371/journal.ppat.1008494openalex-snapshot
Role for the flagellum attachment zone in Leishmania anterior cell tip morphogenesis
inferred← citeshttps://doi.org/10.21236/ada612607openalex-snapshot
Targeting Androgen Receptor by Lysosomal Degradation in Prostate Cancer
inferred← citeshttps://doi.org/10.2174/1381612827666210119105008openalex-snapshot
Basic Biology of Trypanosoma brucei with Reference to the Development of Chemotherapies
inferred← citeshttps://doi.org/10.32657/10356/73069openalex-snapshot
An early role for zebrafish hoxd4a and its cofactors in hematopoiesis
inferred← citeshttps://doi.org/10.3389/fcimb.2022.894213openalex-snapshot
Tag Thy Neighbour: Nanometre-Scale Insights Into Kinetoplastid Parasites With Proximity Dependent Biotinylation
inferred← citeshttps://doi.org/10.3389/fcimb.2022.900878openalex-snapshot
Paving the Way: Contributions of Big Data to Apicomplexan and Kinetoplastid Research
inferred← citeshttps://doi.org/10.3390/cells4040726openalex-snapshot
Form, Fabric, and Function of a Flagellum-Associated Cytoskeletal Structure
inferred← citeshttps://doi.org/10.3390/cells5010009openalex-snapshot
The Trypanosome Flagellar Pocket Collar and Its Ring Forming Protein—TbBILBO1
inferred← citeshttps://doi.org/10.3390/microorganisms9112234openalex-snapshot
Novel Cytoskeleton-Associated Proteins in Trypanosoma brucei Are Essential for Cell Morphogenesis and Cytokinesis
inferred← citeshttps://doi.org/10.3390/microorganisms9112334openalex-snapshot
Bhalin, an Essential Cytoskeleton-Associated Protein of Trypanosoma brucei Linking TbBILBO1 of the Flagellar Pocket Collar with the Hook Complex
inferred← citeshttps://doi.org/10.3410/f.717975978.793555473openalex-snapshot
Faculty Opinions recommendation of Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging.
inferred← citeshttps://doi.org/10.3410/f.718304645.793492539openalex-snapshot
Faculty Opinions recommendation of Proximity interactions among centrosome components identify regulators of centriole duplication.
inferred← citeshttps://doi.org/10.3410/f.726171801.793555487openalex-snapshot
Faculty Opinions recommendation of An improved smaller biotin ligase for BioID proximity labeling.
inferred← citeshttps://doi.org/10.3791/57479openalex-snapshot
Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
inferred← citeshttps://doi.org/10.3791/57479-vopenalex-snapshot
Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
inferred← citeshttps://doi.org/10.53846/goediss-6518openalex-snapshot
Analysis of the Asc1p/RACK1 microenvironment in Saccharomyces cerevisiae using proximity-dependent Biotin Identification (BioID) and high-resolution mass spectrometry
inferred← citeshttps://doi.org/10.64898/2025.12.23.690766openalex-snapshot
In situ cryo-ET reveals restricted docking of intraflagellar transport at the base of the trypanosome flagellum
inferred← citeshttps://doi.org/10.70675/354eedf0za680z4ad4z8c56ze227941da313openalex-snapshot
Characterisation and Nanobody Targeting of Essential Cytoskeletal Proteins of Trypanosoma brucei
inferred← citeshttps://doi.org/10.70675/ea27a504z9095z4adbza177z7fbddfc6be73openalex-snapshot
Décryptage de la relation structure-fonction entre BILBO1 et ses partenaires et leurs rôles dans la biogénèse du collier de la poche flagellaire chez le pathogène Trypanosoma brucei.
inferred← citeshttps://doi.org/10.7554/elife.110793openalex-snapshot
Polo-like kinase phosphorylation of the orphan kinesin KIN-G negatively regulates centrin arm biogenesis in Trypanosoma brucei
inferred← citeshttps://doi.org/10.7554/elife.110793.1openalex-snapshot
Polo-like kinase phosphorylation of the orphan kinesin KIN-G negatively regulates centrin arm biogenesis in Trypanosoma brucei
inferred← citeshttps://doi.org/10.7554/elife.110793.4openalex-snapshot
Polo-like kinase phosphorylation of the orphan kinesin KIN-G negatively regulates centrin arm biogenesis in Trypanosoma brucei
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