On the public citation graph
Architecture of the Mto1/2 microtubule nucleation complex
0 signed · 84 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0061(199807)14:10<943::aid-yea292>3.0.co;2-yopenalex-snapshot
Heterologous modules for efficient and versatile PCR-based gene targeting inSchizosaccharomyces pombe
inferredcites →https://doi.org/10.1002/0471140864.ps0520s51openalex-snapshot
MultiBac: Multigene Baculovirus‐Based Eukaryotic Protein Complex Production
inferredcites →https://doi.org/10.1002/anie.201709559openalex-snapshot
Cross‐Linking/Mass Spectrometry for Studying Protein Structures and Protein–Protein Interactions: Where Are We Now and Where Should We Go from Here?
inferredcites →https://doi.org/10.1002/prot.21124openalex-snapshot
High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl‐CoA ligand
inferredcites →https://doi.org/10.1002/yea.1291openalex-snapshot
Three novel antibiotic marker cassettes for gene disruption and marker switching inSchizosaccharomyces pombe
inferredcites →https://doi.org/10.1002/yea.1293openalex-snapshot
Additional vectors for PCR-based gene tagging inSaccharomyces cerevisiae andSchizosaccharomyces pombe using nourseothricin resistance
inferredcites →https://doi.org/10.1002/yea.1404openalex-snapshot
Cytoplasmic microtubule organization in fission yeast
inferredcites →https://doi.org/10.1006/jmbi.1998.2439openalex-snapshot
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
inferredcites →https://doi.org/10.1006/jmbi.2001.4749openalex-snapshot
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein
inferredcites →https://doi.org/10.1007/s10969-008-9047-6openalex-snapshot
Towards eukaryotic structural complexomics
inferredcites →https://doi.org/10.1016/j.ab.2005.05.015openalex-snapshot
Construction of a set Gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli
inferredcites →https://doi.org/10.1016/j.ceb.2016.09.003openalex-snapshot
Microtubule-organizing centers: from the centrosome to non-centrosomal sites
inferredcites →https://doi.org/10.1016/j.cell.2017.05.030openalex-snapshot
Structural Basis for Mitotic Centrosome Assembly in Flies
inferredcites →https://doi.org/10.1016/j.cub.2004.03.042openalex-snapshot
Microtubule Nucleation at Non-Spindle Pole Body Microtubule-Organizing Centers Requires Fission Yeast Centrosomin-Related Protein mod20p
inferredcites →https://doi.org/10.1016/j.cub.2010.08.035openalex-snapshot
A Catalytic Role for Mod5 in the Formation of the Tea1 Cell Polarity Landmark
inferredcites →https://doi.org/10.1016/j.cub.2010.10.006openalex-snapshot
Fission Yeast Mto1 Regulates Diversity of Cytoplasmic Microtubule Organizing Centers
inferredcites →https://doi.org/10.1016/j.cub.2014.03.006openalex-snapshot
Activation of the γ-Tubulin Complex by the Mto1/2 Complex
inferredcites →https://doi.org/10.1016/j.cub.2019.05.058openalex-snapshot
Reconstitution of Microtubule Nucleation In Vitro Reveals Novel Roles for Mzt1
inferredcites →https://doi.org/10.1016/j.devcel.2014.02.013openalex-snapshot
The Centrosome-Specific Phosphorylation of Cnn by Polo/Plk1 Drives Cnn Scaffold Assembly and Centrosome Maturation
inferredcites →https://doi.org/10.1016/j.jmb.2007.05.022openalex-snapshot
Inference of Macromolecular Assemblies from Crystalline State
inferredcites →https://doi.org/10.1016/j.jsb.2010.02.010openalex-snapshot
New baculovirus expression tools for recombinant protein complex production
inferredcites →https://doi.org/10.1016/j.tcb.2014.12.002openalex-snapshot
Targeting of γ-tubulin complexes to microtubule organizing centers: conservation and divergence
inferredcites →https://doi.org/10.1016/j.tcb.2017.10.005openalex-snapshot
Microtubule-Organizing Centers: Towards a Minimal Parts List
inferredcites →https://doi.org/10.1016/j.tibs.2015.10.008openalex-snapshot
Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines
inferredcites →https://doi.org/10.1016/s0014-5793(99)01122-9openalex-snapshot
Strong hydrophobic nature of cysteine residues in proteins
inferredcites →https://doi.org/10.1016/s0091-679x(10)97009-xopenalex-snapshot
New and Old Reagents for Fluorescent Protein Tagging of Microtubules in Fission Yeast
inferredcites →https://doi.org/10.1016/s0960-9822(01)00017-3openalex-snapshot
Zygotic development without functional mitotic centrosomes
inferredcites →https://doi.org/10.1021/ac026117iopenalex-snapshot
Stop and Go Extraction Tips for Matrix-Assisted Laser Desorption/Ionization, Nanoelectrospray, and LC/MS Sample Pretreatment in Proteomics
inferredcites →https://doi.org/10.1021/acs.analchem.6b03745openalex-snapshot
Quirks of Error Estimation in Cross-Linking/Mass Spectrometry
inferredcites →https://doi.org/10.1021/acs.jproteome.8b00600openalex-snapshot
In-Search Assignment of Monoisotopic Peaks Improves the Identification of Cross-Linked Peptides
inferredcites →https://doi.org/10.1038/35014051openalex-snapshot
A new function for the γ -tubulin ring complex as a microtubule minus-end cap
inferredcites →https://doi.org/10.1038/362219a0openalex-snapshot
Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
inferredcites →https://doi.org/10.1038/378578a0openalex-snapshot
Nucleation of microtubule assembly by a γ-tubulin-containing ring complex
inferredcites →https://doi.org/10.1038/emboj.2009.331openalex-snapshot
Fission yeast Pcp1 links polo kinase‐mediated mitotic entry to γ‐tubulin‐dependent spindle formation
inferredcites →https://doi.org/10.1038/nature09207openalex-snapshot
Microtubule nucleating γ-TuSC assembles structures with 13-fold microtubule-like symmetry
inferredcites →https://doi.org/10.1038/ncb3220openalex-snapshot
Microtubule nucleation at the centrosome and beyond
inferredcites →https://doi.org/10.1038/ncomms8929openalex-snapshot
Mto2 multisite phosphorylation inactivates non-spindle microtubule nucleation complexes during mitosis
inferredcites →https://doi.org/10.1038/nrm.2017.75openalex-snapshot
Microtubule nucleation: beyond the template
inferredcites →https://doi.org/10.1038/nrm3209openalex-snapshot
Microtubule nucleation by γ-tubulin complexes
inferredcites →https://doi.org/10.1038/nsmb.2953openalex-snapshot
Ring closure activates yeast γTuRC for species-specific microtubule nucleation
inferredcites →https://doi.org/10.1038/s41594-018-0147-0openalex-snapshot
Cross-linking mass spectrometry: methods and applications in structural, molecular and systems biology
inferredcites →https://doi.org/10.1039/a701327bopenalex-snapshot
Thermodynamics and kinetics of dissociation of ligand-induced dimers of vancomycin antibiotics
inferredcites →https://doi.org/10.1042/ebc20180028openalex-snapshot
Microtubule nucleation by γ-tubulin complexes and beyond
inferredcites →https://doi.org/10.1074/jbc.m111.298984openalex-snapshot
Diversity in the C3b Convertase Contact Residues and Tertiary Structures of the Staphylococcal Complement Inhibitor (SCIN) Protein Family
inferredcites →https://doi.org/10.1074/mcp.m700274-mcp200openalex-snapshot
Structural Analysis of Multiprotein Complexes by Cross-linking, Mass Spectrometry, and Database Searching
inferredcites →https://doi.org/10.1083/jcb.144.4.721openalex-snapshot
Characterization of Two Related Drosophila γ-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules
inferredcites →https://doi.org/10.1083/jcb.200410119openalex-snapshot
Efficient formation of bipolar microtubule bundles requires microtubule-bound γ-tubulin complexes
inferredcites →https://doi.org/10.1083/jcb.200511071openalex-snapshot
Drosophila melanogaster γ-TuRC is dispensable for targeting γ-tubulin to the centrosome and microtubule nucleation
inferredcites →https://doi.org/10.1083/jcb.201007030openalex-snapshot
CDK5RAP2 stimulates microtubule nucleation by the γ-tubulin ring complex
inferredcites →https://doi.org/10.1091/mbc.02-01-0603openalex-snapshot
A Fourth Component of the Fission Yeast γ-Tubulin Complex, Alp16, Is Required for Cytoplasmic Microtubule Integrity and Becomes Indispensable When γ-Tubulin Function Is Compromised
inferredcites →https://doi.org/10.1091/mbc.e03-10-0728openalex-snapshot
Identification and Characterization of Two Novel Proteins Affecting Fission Yeast γ-tubulin Complex Function
inferredcites →https://doi.org/10.1091/mbc.e04-11-1003openalex-snapshot
Fission Yeast mto2p Regulates Microtubule Nucleation by the Centrosomin-related Protein mto1p
inferredcites →https://doi.org/10.1091/mbc.e04-12-1043openalex-snapshot
Mto2p, a Novel Fission Yeast Protein Required for Cytoplasmic Microtubule Organization and Anchoring of the Cytokinetic Actin Ring
inferredcites →https://doi.org/10.1091/mbc.e05-11-1009openalex-snapshot
Noncore Components of the Fission Yeast γ-Tubulin Complex
inferredcites →https://doi.org/10.1091/mbc.e07-05-0474openalex-snapshot
Proper Recruitment of γ-Tubulin and D-TACC/Msps to EmbryonicDrosophilaCentrosomes Requires Centrosomin Motif 1
inferredcites →https://doi.org/10.1091/mbc.e11-09-0800openalex-snapshot
Roles of putative Rho-GEF Gef2 in division-site positioning and contractile-ring function in fission yeast cytokinesis
inferredcites →https://doi.org/10.1093/bioinformatics/btn323openalex-snapshot
ProteoWizard: open source software for rapid proteomics tools development
inferredcites →https://doi.org/10.1093/emboj/16.23.6985openalex-snapshot
Spc98p and Spc97p of the yeast γ‐tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p
inferredcites →https://doi.org/10.1093/nar/gky1106openalex-snapshot
The PRIDE database and related tools and resources in 2019: improving support for quantification data
inferredcites →https://doi.org/10.1098/rsob.170266openalex-snapshot
Assembly and regulation of γ-tubulin complexes
inferredcites →https://doi.org/10.1101/pdb.top079764openalex-snapshot
Growth and the Environment of Schizosaccharomyces pombe
inferredcites →https://doi.org/10.1101/pdb.top079772openalex-snapshot
Genetic Analysis of Schizosaccharomyces pombe
inferredcites →https://doi.org/10.1107/s0021889807021206openalex-snapshot
Phaser crystallographic software
inferredcites →https://doi.org/10.1107/s0021889809045701openalex-snapshot
xia2 : an expert system for macromolecular crystallography data reduction
inferredcites →https://doi.org/10.1107/s0907444904026460openalex-snapshot
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
inferredcites →https://doi.org/10.1107/s0907444909042073openalex-snapshot
MolProbity : all-atom structure validation for macromolecular crystallography
inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot
Features and development of Coot
inferredcites →https://doi.org/10.1107/s0907444910045749openalex-snapshot
Overview of the CCP 4 suite and current developments
inferredcites →https://doi.org/10.1107/s0907444911001314openalex-snapshot
REFMAC 5 for the refinement of macromolecular crystal structures
inferredcites →https://doi.org/10.1107/s2059798317004193openalex-snapshot
The first plant acyl-CoA-binding protein structures: the close homologues OsACBP1 and OsACBP2 from rice
inferredcites →https://doi.org/10.1115/1.1451234openalex-snapshot
Mechanics of Motor Proteins and the Cytoskeleton
inferredcites →https://doi.org/10.1126/science.1113230openalex-snapshot
Counting Cytokinesis Proteins Globally and Locally in Fission Yeast
inferredcites →https://doi.org/10.1146/annurev-biophys-070816-033928openalex-snapshot
Geometric Principles for Designing Highly Symmetric Self-Assembling Protein Nanomaterials
inferredcites →https://doi.org/10.1146/annurev-cellbio-100616-060615openalex-snapshot
Microtubule-Organizing Centers
inferredcites →https://doi.org/10.1242/jcs.038414openalex-snapshot
Two distinct regions of Mto1 are required for normal microtubule nucleation and efficient association with the γ-tubulin complex in vivo
inferredcites →https://doi.org/10.1242/jcs.059196openalex-snapshot
In vivo analysis of the functions of γ-tubulin-complex proteins
inferredcites →https://doi.org/10.1242/jcs.083741openalex-snapshot
Microtubule stabilization in vivo by nucleation-incompetent γ-tubulin complex
inferredcites →https://doi.org/10.1242/jcs.195321openalex-snapshot
MZT1 regulates microtubule nucleation by linking γTuRC assembly to adapter-mediated targeting and activation
inferredcites →https://doi.org/10.1371/journal.pone.0097683openalex-snapshot
Extending the Schizosaccharomyces pombe Molecular Genetic Toolbox
inferredcites →https://doi.org/10.1371/journal.pone.0190530openalex-snapshot
The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles
inferredcites →https://doi.org/10.15252/msb.20198994openalex-snapshot
An integrated workflow for crosslinking mass spectrometry
inferredcites →https://doi.org/10.7554/elife.33465openalex-snapshot
Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.