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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is correctly identified as NUDF, the LIS1-family cytoplasmic-dynein regulator encoded by nudF (ORF AN6197) in Aspergillus nidulans, historically also called Emericella nidulans. Tandem mass spectrometry directly identified affinity-purified NUDF as AN6197.1, while organism-specific literature consistently identifies the nudF product as a homolog of human LIS1 with approximately 42% sequence identity. This matches the supplied UniProt description and its LisH/LIS1/WD-repeat domain annotation. The synonym pac1 must be interpreted cautiously because Pac1 is commonly used for the LIS1 ortholog of budding yeast; findings about yeast Pac1 are not automatically evidence about Q00664. (helmstaedt2008thenuclearmigration pages 7-8, efimov2000thelis1relatednudf pages 1-2)
NUDF is not an enzyme, transporter, or dynein motor subunit. It is a soluble, noncatalytic regulatory/adaptor-like protein that binds cytoplasmic dynein and associated regulatory proteins, promotes formation of a cargo-ready activated motor complex, and is required chiefly at the initiation of minus-end-directed transport. Its best-established physiological outputs are the distribution of nuclei, early endosomes, and peroxisomes along polarized fungal hyphae. (egan2012lis1isan pages 7-8, egan2012lis1isan pages 8-9, egan2012lis1isan pages 1-2, helmstaedt2008thenuclearmigration pages 1-2)
The N-terminal LisH motif supports homodimerization, whereas the C-terminal WD40-repeat region forms the interaction-rich β-propeller typical of LIS1-family dynein regulators. NUDF’s WD40 region binds NUDC; the protein also contacts the dynein motor region and associates with NUDE and BNFA. Thus, its architecture is consistent with a multivalent regulator that couples dynein conformational control to assembly and localization rather than catalyzing a chemical reaction. No substrate, catalytic reaction, or intrinsic ATPase activity is established for NUDF; ATP hydrolysis is performed by the dynein heavy-chain AAA+ motor. (helmstaedt2008thenuclearmigration pages 1-2, qiu2021dyneinactivationin pages 1-4)
The most precise direct functional interpretation comes from live-cell studies of three dynein cargo classes. Deleting nudF/Lis1 strongly reduced the frequency of dynein and cargo movements, whereas movements that still initiated proceeded at approximately normal speeds. NUDF was not detectably retained on moving cargo, although dynein and dynactin were. These observations identify NUDF principally as a transient transport-initiation factor, rather than a component needed continuously for motor stepping. (egan2012lis1isan pages 8-9, egan2012lis1isan pages 1-2)
Dynein still accumulates in microtubule-plus-end comets in the absence of NUDF, but it fails to associate efficiently with endosomes and peroxisomes concentrated near hyphal tips. Therefore, kinesin-dependent delivery of dynein to plus ends precedes a distinct NUDF-dependent step that creates a cargo-binding or assembly-competent motor. (egan2012lis1isan pages 7-8)
In polarized hyphae, dynein, dynactin, and NUDF concentrate near microtubule plus ends at the growing tip. Cargo engagement followed by dynein activation drives movement toward microtubule minus ends, which are associated with spindle-pole bodies and septal organizing sites. NUDF is therefore positioned at the transition between plus-end motor accumulation and retrograde cargo transport. (egan2012lis1isan pages 7-8, qiu2021dyneinactivationin pages 1-4)
For early endosomes, the activating adaptor HookA and its FHF complex connect dynein–dynactin to cargo; FhipA contributes the endosome-facing connection. In vivo, overexpressed C-terminally truncated HookA drives dynein/dynactin activation and relocation, and this response requires NUDF/LIS1. (qiu2021dyneinactivationin pages 1-4)
Dynein mutational analysis ties this function to the motor’s AAA3/AAA4 region. Preventing AAA3 ATP hydrolysis bypassed the normal requirement for NUDF or HookA and sent dynein toward minus ends even though early endosomes remained near plus ends. Conversely, preventing AAA3 ATP binding caused abnormal persistence of the dynein–NUDF association after activation. The strongest organism-specific model is therefore that the dynein AAA3 nucleotide cycle coordinates NUDF binding/release, motor activation, and cargo engagement. NUDF regulates this cycle but does not itself hydrolyze ATP. (qiu2021dyneinactivationin pages 1-4)
GFP-NUDF forms motile, comet-like structures coincident with microtubule ends, particularly plus ends near hyphal tips. This localization overlaps with dynein and is consistent with a role in preparing plus-end-accumulated dynein for cargo capture and retrograde movement. (efimov2003rolesofnude pages 1-2, efimov2000thelis1relatednudf pages 6-6)
NUDF also localizes to mitotic nuclear poles/spindle-pole bodies (SPBs). NUDF–NUDC interaction was localized to SPBs by colocalization with MIPA/γ-tubulin, and NUDF recruits BNFA there. NUDF can remain positioned at spindle poles when dynein or microtubules are disrupted, suggesting an SPB anchoring or recruitment function in addition to its plus-end transport role. (helmstaedt2008thenuclearmigration pages 7-8, helmstaedt2008thenuclearmigration pages 9-10)
Accordingly, the most defensible localization annotation is: cytoplasmic microtubule plus ends and spindle-pole bodies/mitotic nuclear poles, with transient association with dynein before cargo movement. NUDF is not supported as a secreted, membrane-spanning, or organelle-lumen protein.
The founding phenotype is defective nuclear distribution/migration. In elongated multinucleate hyphae, loss or impairment of NUDF prevents normal dynein-dependent dispersal of nuclei, causing nuclei to remain concentrated near the germinating spore. Secondary colony phenotypes include reduced growth, excessive branching, and defective conidiation; these broad outcomes are best interpreted as consequences of disrupted intracellular organization rather than separate biochemical functions. (helmstaedt2008thenuclearmigration pages 1-2, efimov2000thelis1relatednudf pages 1-2)
NUDF also controls dynein-dependent distribution of early endosomes and peroxisomes. Loss of NUDF causes these cargos to accumulate abnormally near hyphal tips, while dynein remains present at plus ends but associates poorly with cargo. Occasional endosome movements persist, and their velocities are not dramatically reduced; the dominant quantitative distinction is fewer initiation events rather than slower runs. (egan2012lis1isan pages 7-8, egan2012lis1isan pages 8-9, egan2012lis1isan pages 1-2)
The evidence therefore supports annotation to:
A direct role in microtubule polymerization is less certain. Dynein-pathway mutants can alter microtubule dynamics, but the best-resolved function of NUDF is regulation of dynein activation and cargo loading rather than acting as a core microtubule assembly factor. (efimov2003rolesofnude pages 1-2)
The following table separates direct A. nidulans evidence from cross-species mechanistic context.
| Topic | Conclusion | Evidence type/system | Confidence | Key source/date/DOI |
|---|---|---|---|---|
| Identity | NUDF is the A. nidulans AN6197.1 gene product; primary literature identifies it as the fungal LIS1 homolog. This supports the supplied Q00664–nudF–AN6197 mapping. | Direct tandem-MS identification of affinity-purified NUDF; organism-specific genetics and sequence comparison | High | Helmstaedt et al., June 2008, 10.1128/EC.00071-07; Efimov & Morris, August 2000, 10.1083/jcb.150.3.681 (helmstaedt2008thenuclearmigration pages 7-8, efimov2000thelis1relatednudf pages 1-2) |
| LIS1 family and architecture | NUDF is a roughly 50-kDa LIS1-family dimer with an N-terminal LisH dimerization motif, adjacent coiled-coil region, and C-terminal WD40 β-propeller; it shares 42% sequence identity with human LIS1. | Direct/primary A. nidulans protein characterization plus comparative sequence analysis | High | Helmstaedt et al., June 2008, 10.1128/EC.00071-07; Efimov & Morris, August 2000, 10.1083/jcb.150.3.681 (helmstaedt2008thenuclearmigration pages 1-2, efimov2000thelis1relatednudf pages 1-2) |
| Primary molecular function | NUDF is not an enzyme or motor; it is a noncatalytic regulator that promotes formation of a cargo-ready/activated cytoplasmic-dynein state and is required principally for initiation of retrograde transport. Loss reduces event frequency much more than movement speed, and NUDF is absent from already moving cargo. | Direct live-cell imaging and nudF/Lis1 deletion experiments in A. nidulans | High | Egan et al., June 2012, 10.1083/jcb.201112101 (egan2012lis1isan pages 7-8, egan2012lis1isan pages 8-9, egan2012lis1isan pages 1-2) |
| Microtubule-plus-end localization | GFP-NUDF forms motile comet-like structures at microtubule ends. Dynein can still reach plus ends without NUDF, but fails to associate efficiently with organelle cargo, separating plus-end targeting from NUDF-dependent transport initiation. | Direct fluorescence imaging in A. nidulans | High | Efimov, March 2003, 10.1091/mbc.e02-06-0359; Egan et al., June 2012, 10.1083/jcb.201112101 (efimov2003rolesofnude pages 1-2, egan2012lis1isan pages 7-8) |
| Spindle-pole localization | NUDF localizes to mitotic nuclear poles/SPBs and participates in an SPB-associated complex. Its SPB positioning can persist without dynein or microtubules, consistent with a recruitment or anchoring function. | GFP/BiFC imaging and γ-tubulin/MIPA colocalization in A. nidulans | High | Helmstaedt et al., June 2008, 10.1128/EC.00071-07 (helmstaedt2008thenuclearmigration pages 7-8, helmstaedt2008thenuclearmigration pages 9-10) |
| NUDE interaction | NUDF binds the conserved NUDE coiled-coil (residues 25–183); interaction was supported by yeast two-hybrid analysis and coprecipitation from A. nidulans. NUDF overexpression suppresses nudE defects. | Direct physical and genetic interaction assays | High | Efimov & Morris, August 2000, 10.1083/jcb.150.3.681; Efimov, March 2003, 10.1091/mbc.e02-06-0359 (efimov2000thelis1relatednudf pages 1-2, efimov2000thelis1relatednudf pages 6-6, efimov2000thelis1relatednudf pages 5-6, efimov2003rolesofnude pages 15-16) |
| NUDC and BNFA interactions | NUDF’s WD40 domain binds NUDC at SPBs. BNFA copurifies and interacts with NUDF, and its SPB recruitment requires NUDF; BNFA itself is dispensable for growth and nuclear migration. | Yeast two-hybrid, BiFC, tandem-affinity purification/MS, and dependency imaging in A. nidulans | High | Helmstaedt et al., June 2008, 10.1128/EC.00071-07 (helmstaedt2008thenuclearmigration pages 1-2, helmstaedt2008thenuclearmigration pages 7-8, helmstaedt2008thenuclearmigration pages 9-10) |
| Dynein interaction | NUDF associates genetically and physically with the dynein heavy chain NUDA, including its motor/AAA region; suppressor mutations in dynein’s stem and AAA4 regions reinforce a direct regulatory relationship. | Two-hybrid/in-vitro binding, allele-specific genetics, and suppressor genetics in A. nidulans | High | Efimov, March 2003, 10.1091/mbc.e02-06-0359; Zhuang et al., March 2007, 10.1534/genetics.106.069013 (efimov2003rolesofnude pages 1-2, efimov2003rolesofnude pages 15-16, egan2012lis1isan pages 11-12) |
| Nuclear and organelle phenotypes | nudF loss disrupts nuclear distribution and causes nuclei to accumulate near the spore remnant; it also impairs distribution of early endosomes and peroxisomes. Associated colony-level effects include slow growth, excessive branching, and defective conidiation. | Deletion/conditional-mutant phenotypes and live-cell cargo imaging in A. nidulans | High for distribution defects; moderate for linking broad morphology directly to the molecular step | Egan et al., June 2012, 10.1083/jcb.201112101; Helmstaedt et al., June 2008, 10.1128/EC.00071-07 (egan2012lis1isan pages 7-8, egan2012lis1isan pages 8-9, egan2012lis1isan pages 1-2, helmstaedt2008thenuclearmigration pages 1-2) |
| HookA/AAA3 mechanism | In the early-endosome pathway, HookA and the FHF complex connect dynein–dynactin to cargo. HookA-driven dynein activation requires NUDF/LIS1. Preventing AAA3 ATP hydrolysis bypasses the need for NUDF or HookA, whereas preventing AAA3 ATP binding blocks normal NUDF dissociation, showing that dynein’s AAA3 nucleotide cycle coordinates activation, cargo binding, and transient NUDF association. | Direct genetic, localization, and in-vivo activation assays in A. nidulans | High | Qiu et al., 2021, 10.1016/j.cub.2021.08.059 (qiu2021dyneinactivationin pages 1-4) |
| 2024 assembly mechanism—non-direct context | Mammalian cryo-EM indicates that LIS1’s WD40 domain binds dynein at the AAA3–AAA4/stalk region while its N-terminal region contacts dynactin p150, constraining dynein–dynactin into an assembly-competent configuration. This is a strong mechanistic model for conserved LIS1-family action but was not tested on A. nidulans NUDF. | Mammalian reconstituted dynein–dynactin–adaptor complex; cryo-EM and pull-down assays | High for mammalian LIS1; inferential for NUDF | Singh et al., March 2024, 10.1126/science.adk8544 (singh2024molecularmechanismof pages 6-8) |
| 2024 force regulation—non-direct context | Yeast single-molecule and optical-trapping experiments show that Lis1 slows dynein through AAA-ring binding, prolongs stalls, and reduces force-dependent detachment asymmetry without changing force generation; stalk-site mutations partly restore detachment behavior. These results are not direct A. nidulans NUDF evidence. | Yeast-derived dynein biophysics; single-molecule imaging and optical trapping | High for yeast Lis1; inferential for NUDF | Kusakci et al., 2024, 10.1038/s41589-023-01464-6 (kusakci2024lis1slowsforceinduced pages 1-3, kusakci2024lis1slowsforceinduced pages 22-23) |
Table: Evidence hierarchy separating direct Aspergillus nidulans findings from comparative mammalian and yeast LIS1 mechanisms. It summarizes identity, architecture, localization, interactions, transport function, phenotypes, and confidence for Q00664/NUDF.
No direct 2023–2024 study of Q00664/AN6197 was identified in the retrieved literature. The major recent advances instead concern conserved LIS1 mechanisms in mammalian and yeast systems and should be used to refine—but not replace—the organism-specific annotation.
A March 2024 Science cryo-EM study of a mammalian dynein–dynactin–adaptor assembly found that LIS1’s WD40 domain contacts dynein near the AAA3–AAA4/stalk region while LIS1 also helps dock dynactin’s p150 arm. The resulting model is that LIS1 constrains dynein and dynactin in an assembly-competent geometry, facilitating adaptor binding before LIS1 is released. The reported IC–light-chain tower region was resolved at approximately 9 Å, and pull-down assays supported stoichiometric ternary-complex assembly. This provides a structural explanation consistent with the older A. nidulans observation that NUDF is required before cargo movement, but direct conservation of every interface in NUDF remains to be tested. Published March 2024; DOI: https://doi.org/10.1126/science.adk8544. (singh2024molecularmechanismof pages 6-8)
A 2024 Nature Chemical Biology study using yeast-derived dynein, single-molecule imaging, and optical trapping showed that Lis1 slows motor movement through AAA-ring binding, prolongs stalls, and reduces the usual asymmetry of force-induced microtubule detachment without changing force generation. Mutations at stalk-binding sites partly restored detachment behavior but not velocity, indicating separable ring- and stalk-mediated effects. These experiments used up to 300 or 900 nM Lis1 depending on the dynein construct and 2 mM ATP. They provide useful biophysical context but are not direct measurements of A. nidulans NUDF. DOI: https://doi.org/10.1038/s41589-023-01464-6. (kusakci2024lis1slowsforceinduced pages 1-3, kusakci2024lis1slowsforceinduced pages 22-23)
Together, recent structural and biophysical work strengthens the expert consensus that LIS1-family proteins are transient conformational and assembly regulators of dynein, not permanent cargo adaptors and not catalytic motors. The A. nidulans initiation-factor model remains compatible with this framework. (egan2012lis1isan pages 7-8, singh2024molecularmechanismof pages 6-8, kusakci2024lis1slowsforceinduced pages 1-3)
There is no established industrial, diagnostic, clinical, or therapeutic implementation directed specifically at A. nidulans nudF. Its principal application is as an experimentally tractable model system for dissecting conserved dynein regulation in long, polarized cells. The separation of plus-end motor delivery, cargo attachment, activation, and processive movement in fungal hyphae has enabled live-cell genetic tests that are difficult to perform in mammalian neurons.
The broader relevance comes from conservation with human LIS1, whose dosage is essential for neuronal migration and whose haploinsufficiency causes lissencephaly. That relationship makes fungal NUDF valuable for identifying conserved dynein interfaces and regulatory steps; it does not mean that Q00664 itself is a human disease gene or a validated drug target. NUDF shares approximately 42% identity with human LIS1, and its interaction with fungal NUDE parallels LIS1–NDE-family regulation, supporting evolutionary conservation while leaving organism-specific details intact. (efimov2000thelis1relatednudf pages 1-2, efimov2000thelis1relatednudf pages 5-6)
Primary molecular function: LIS1-family, noncatalytic cytoplasmic-dynein regulator that binds the dynein motor and associated regulatory proteins to promote an activation- and cargo-loading-competent motor state at microtubule plus ends and spindle-pole bodies.
Principal biological process: Initiation of dynein-driven minus-end transport required for nuclear distribution and for early-endosome and peroxisome positioning in polarized hyphae.
Localization: Cytoplasmic microtubule plus-end comets; spindle-pole bodies/mitotic nuclear poles; transiently associated with pre-transport dynein complexes.
Structure: LIS1-family homodimer with N-terminal LisH/coiled-coil architecture and a C-terminal WD40 β-propeller; the domain organization supports dimerization and multivalent protein binding. (helmstaedt2008thenuclearmigration pages 1-2)
Not supported: Enzymatic activity, a small-molecule substrate, transmembrane transport, secretion, or continuous residence on moving cargo.
The direct A. nidulans literature is mechanistically strong but mostly predates 2023. Several useful observations are qualitative, and the retrieved sources do not supply a comprehensive modern numerical dataset for NUDF abundance, binding affinity, run frequency, or complete loss-of-function effect sizes. The 2024 structural and force measurements were obtained with mammalian or yeast machinery; they support conserved hypotheses but should not be entered as experimentally demonstrated Q00664-specific properties without direct validation.
References
(helmstaedt2008thenuclearmigration pages 7-8): Kerstin Helmstaedt, Karen Laubinger, Katja Voßkuhl, Özgür Bayram, Silke Busch, Michael Hoppert, Oliver Valerius, Stephan Seiler, and Gerhard H. Braus. The nuclear migration protein nudf/lis1 forms a complex with nudc and bnfa at spindle pole bodies. Eukaryotic Cell, 7:1041-1052, Jun 2008. URL: https://doi.org/10.1128/ec.00071-07, doi:10.1128/ec.00071-07. This article has 31 citations and is from a peer-reviewed journal.
(efimov2000thelis1relatednudf pages 1-2): Vladimir P. Efimov and N. Ronald Morris. The lis1-related nudf protein of aspergillus nidulans interacts with the coiled-coil domain of the nude/ro11 protein. The Journal of Cell Biology, 150:681-688, Aug 2000. URL: https://doi.org/10.1083/jcb.150.3.681, doi:10.1083/jcb.150.3.681. This article has 223 citations.
(egan2012lis1isan pages 7-8): Martin J. Egan, Kaeling Tan, and Samara L. Reck-Peterson. Lis1 is an initiation factor for dynein-driven organelle transport. The Journal of Cell Biology, 197:971-982, Jun 2012. URL: https://doi.org/10.1083/jcb.201112101, doi:10.1083/jcb.201112101. This article has 222 citations.
(egan2012lis1isan pages 8-9): Martin J. Egan, Kaeling Tan, and Samara L. Reck-Peterson. Lis1 is an initiation factor for dynein-driven organelle transport. The Journal of Cell Biology, 197:971-982, Jun 2012. URL: https://doi.org/10.1083/jcb.201112101, doi:10.1083/jcb.201112101. This article has 222 citations.
(egan2012lis1isan pages 1-2): Martin J. Egan, Kaeling Tan, and Samara L. Reck-Peterson. Lis1 is an initiation factor for dynein-driven organelle transport. The Journal of Cell Biology, 197:971-982, Jun 2012. URL: https://doi.org/10.1083/jcb.201112101, doi:10.1083/jcb.201112101. This article has 222 citations.
(helmstaedt2008thenuclearmigration pages 1-2): Kerstin Helmstaedt, Karen Laubinger, Katja Voßkuhl, Özgür Bayram, Silke Busch, Michael Hoppert, Oliver Valerius, Stephan Seiler, and Gerhard H. Braus. The nuclear migration protein nudf/lis1 forms a complex with nudc and bnfa at spindle pole bodies. Eukaryotic Cell, 7:1041-1052, Jun 2008. URL: https://doi.org/10.1128/ec.00071-07, doi:10.1128/ec.00071-07. This article has 31 citations and is from a peer-reviewed journal.
(qiu2021dyneinactivationin pages 1-4): Rongde Qiu, Jun Zhang, Jeremy D. Rotty, and Xin Xiang. Dynein activation in vivo is regulated by the nucleotide states of its aaa3 domain. Current Biology, 31:4486-4498.e6, Apr 2021. URL: https://doi.org/10.1101/2021.04.12.439451, doi:10.1101/2021.04.12.439451. This article has 17 citations and is from a highest quality peer-reviewed journal.
(efimov2003rolesofnude pages 1-2): Vladimir P. Efimov. Roles of nude and nudf proteins of aspergillus nidulans: insights from intracellular localization and overexpression effects. Molecular biology of the cell, 14 3:871-88, Mar 2003. URL: https://doi.org/10.1091/mbc.e02-06-0359, doi:10.1091/mbc.e02-06-0359. This article has 76 citations and is from a domain leading peer-reviewed journal.
(efimov2003rolesofnude pages 15-16): Vladimir P. Efimov. Roles of nude and nudf proteins of aspergillus nidulans: insights from intracellular localization and overexpression effects. Molecular biology of the cell, 14 3:871-88, Mar 2003. URL: https://doi.org/10.1091/mbc.e02-06-0359, doi:10.1091/mbc.e02-06-0359. This article has 76 citations and is from a domain leading peer-reviewed journal.
(egan2012lis1isan pages 11-12): Martin J. Egan, Kaeling Tan, and Samara L. Reck-Peterson. Lis1 is an initiation factor for dynein-driven organelle transport. The Journal of Cell Biology, 197:971-982, Jun 2012. URL: https://doi.org/10.1083/jcb.201112101, doi:10.1083/jcb.201112101. This article has 222 citations.
(efimov2000thelis1relatednudf pages 6-6): Vladimir P. Efimov and N. Ronald Morris. The lis1-related nudf protein of aspergillus nidulans interacts with the coiled-coil domain of the nude/ro11 protein. The Journal of Cell Biology, 150:681-688, Aug 2000. URL: https://doi.org/10.1083/jcb.150.3.681, doi:10.1083/jcb.150.3.681. This article has 223 citations.
(efimov2000thelis1relatednudf pages 5-6): Vladimir P. Efimov and N. Ronald Morris. The lis1-related nudf protein of aspergillus nidulans interacts with the coiled-coil domain of the nude/ro11 protein. The Journal of Cell Biology, 150:681-688, Aug 2000. URL: https://doi.org/10.1083/jcb.150.3.681, doi:10.1083/jcb.150.3.681. This article has 223 citations.
(helmstaedt2008thenuclearmigration pages 9-10): Kerstin Helmstaedt, Karen Laubinger, Katja Voßkuhl, Özgür Bayram, Silke Busch, Michael Hoppert, Oliver Valerius, Stephan Seiler, and Gerhard H. Braus. The nuclear migration protein nudf/lis1 forms a complex with nudc and bnfa at spindle pole bodies. Eukaryotic Cell, 7:1041-1052, Jun 2008. URL: https://doi.org/10.1128/ec.00071-07, doi:10.1128/ec.00071-07. This article has 31 citations and is from a peer-reviewed journal.
(singh2024molecularmechanismof pages 6-8): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.
(kusakci2024lis1slowsforceinduced pages 1-3): Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P. Gillies, Samara L. Reck-Peterson, and Ahmet Yildiz. Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nature chemical biology, 20:521-529, Nov 2024. URL: https://doi.org/10.1038/s41589-023-01464-6, doi:10.1038/s41589-023-01464-6. This article has 6 citations and is from a highest quality peer-reviewed journal.
(kusakci2024lis1slowsforceinduced pages 22-23): Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P. Gillies, Samara L. Reck-Peterson, and Ahmet Yildiz. Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nature chemical biology, 20:521-529, Nov 2024. URL: https://doi.org/10.1038/s41589-023-01464-6, doi:10.1038/s41589-023-01464-6. This article has 6 citations and is from a highest quality peer-reviewed journal.