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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P38861
• Protein Description: RecName: Full=60S ribosomal export protein NMD3; AltName: Full=Nonsense-mediated mRNA decay protein 3;
• Gene Information: Name=NMD3; OrderedLocusNames=YHR170W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the NMD3 family. .
• Key Domains: Nmd3. (IPR039768); Nmd3_N. (IPR007064); NMD3_OB. (IPR048898); NMD_SH3. (IPR048899); NMD3 (PF04981)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "NMD3" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'NMD3' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene NMD3 (gene ID: NMD3, UniProt: P38861) in yeast.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P38861
• Protein Description: RecName: Full=60S ribosomal export protein NMD3; AltName: Full=Nonsense-mediated mRNA decay protein 3;
• Gene Information: Name=NMD3; OrderedLocusNames=YHR170W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the NMD3 family. .
• Key Domains: Nmd3. (IPR039768); Nmd3_N. (IPR007064); NMD3_OB. (IPR048898); NMD_SH3. (IPR048899); NMD3 (PF04981)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "NMD3" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'NMD3' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene NMD3 (gene ID: NMD3, UniProt: P38861) in yeast.

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.

Research report: NMD3 (YHR170W; UniProt P38861) in Saccharomyces cerevisiae

0. Target verification (gene/protein identity)

The literature summarized here refers to Saccharomyces cerevisiae Nmd3p (gene NMD3, ORF YHR170W), a conserved 60S ribosomal subunit export adaptor. This matches the UniProt description (P38861) of “60S ribosomal export protein NMD3” and the defining mechanistic features (Nmd3 family; nucleocytoplasmic shuttling; Crm1/Xpo1-dependent export; late pre-60S binding; release by Lsg1 and Rpl10/uL16) (gadal2001nuclearexportof pages 1-2, johnson2002nuclearexportof pages 2-3, malyutin2017nmd3isa pages 1-2).

1. Key concepts and definitions (current understanding)

1.1. What Nmd3 is (definition)

Nmd3p is an essential, conserved, shuttling adaptor protein required for nuclear export of nascent 60S ribosomal subunits. In yeast, it binds pre-60S particles and provides a leucine-rich nuclear export signal (NES) that recruits the export receptor Crm1/Xpo1 (gadal2001nuclearexportof pages 1-2, johnson2002nuclearexportof pages 2-3).

Although the gene symbol historically suggested a connection to nonsense-mediated decay, mechanistic work in yeast and reviews emphasize that its primary, essential function is ribosome large-subunit export and late maturation, not RNA decay catalysis (johnson2002nuclearexportof pages 2-3, gadal2001nuclearexportof pages 1-2).

1.2. Where Nmd3 acts in the 60S biogenesis pathway

Ribosome biogenesis in eukaryotes proceeds from nucleolus → nucleoplasm → cytoplasm; export of the large subunit through the nuclear pore complex (NPC) is a key transition. Nmd3 is best described as a late-acting “export competence” factor: it binds to large subunits and licenses Crm1-mediated export (johnson2002nuclearexportof pages 2-3, johnson2002nuclearexportof pages 1-2).

Reviews further frame Nmd3 as part of a quality control logic—binding preferentially to “mature/correctly folded” 60S particles and helping exclude immature ones from export (johnson2002nuclearexportof pages 1-2).

1.3. Export adaptor vs export receptor

• Crm1/Xpo1 is the karyopherin-type export receptor that recognizes NES-bearing cargos in a RanGTP-dependent manner.
• Nmd3 is a cargo-specific adaptor: it binds pre-60S and provides the NES in trans so Crm1 can engage the 60S particle (johnson2002nuclearexportof pages 2-3, gadal2001nuclearexportof pages 1-2).

2. Core functional annotation of yeast Nmd3p (mechanism and evidence)

2.1. Essentiality and role in 60S export

Genetic and cell biological evidence in yeast shows that impaired Nmd3 function causes nuclear accumulation of large-subunit reporters (export block). Gadal et al. used an in vivo export assay (Rpl25–GFP) and showed that thermosensitive nmd3 mutants impair 60S export, consistent with Nmd3 as an essential factor required for large-subunit export (gadal2001nuclearexportof pages 1-2).

2.2. Nmd3 binding site on the 60S subunit (structural/biochemical evidence)

A cryo-EM reconstruction of MBP-Nmd3 bound to the 60S subunit showed Nmd3 density on the intersubunit/joining face near 25S rRNA helices H38, H69, and H95, and Nmd3 binding is blocked when 60S is engaged in 80S ribosomes (consistent with a joining-face site) (sengupta2010characterizationofthe pages 1-2). The binding appears saturable at ~1:1 Nmd3:60S stoichiometry, even at 81-fold excess of Nmd3, and Nmd3 binds 60S but not 80S (sengupta2010characterizationofthe pages 1-2).

Visual evidence: A representative cryo-EM figure labeling helices H38/H69/H95 and showing the Nmd3 density on the 60S joining face is available from Sengupta et al. (sengupta2010characterizationofthe media 9c1f3f22).

2.3. Key interaction partners and their roles

Crm1/Xpo1 (export receptor)

Nmd3’s essential export function is mediated by Crm1/Xpo1, recruited through Nmd3’s C-terminal leucine-rich NES; the Crm1 dependence is a core feature of the pathway (gadal2001nuclearexportof pages 1-2, johnson2002nuclearexportof pages 2-3).

Rpl10/uL16 and Lsg1 (cytoplasmic recycling / maturation checkpoint)

After export to the cytoplasm, Nmd3 must be removed so the 60S can become translation competent. The release of Nmd3 from cytoplasmic 60S requires the ribosomal protein Rpl10/uL16 and the conserved cytoplasmic GTPase Lsg1 (hedges2005releaseofthe pages 1-2). Hedges et al. showed that defects in LSG1 or RPL10 impair Nmd3 recycling and 60S export, and that NMD3 overexpression or weakened Nmd3–60S binding alleles can suppress these defects—supporting a model where failure to recycle/release Nmd3 is a bottleneck (hedges2005releaseofthe pages 1-2).

High-resolution structures and biochemical reconstitution later clarified mechanistic details: Nmd3 occupies functional centers of the subunit (including E-site/P-site vicinity), and Nmd3–Lsg1 interactions remodel parts of the ribosome (including helix 69), consistent with a GTPase activation/coupling role for Lsg1 in Nmd3 eviction (malyutin2017nmd3isa pages 1-2).

Tif6/eIF6 (anti-association factor in late cytoplasmic maturation)

Cryo-EM of late cytoplasmic particles shows Nmd3 co-binding with Tif6/eIF6 and Lsg1; Nmd3 extends toward functionally important regions and contacts/relates to Tif6 positioning, consistent with coordinated late cytoplasmic maturation steps that must occur before subunit joining and translation (malyutin2017nmd3isa pages 1-2).

2.4. Domain architecture and shuttling signals (NLS/NES)

Reviews describe Nmd3 as having a conserved N-terminal domain (~40 kDa) and a eukaryote-specific C-terminal extension that contains both a basic NLS and leucine-rich NES required for nucleocytoplasmic shuttling (johnson2002nuclearexportof pages 2-3). The C-terminal NES is necessary for export: removal of the NES causes nuclear retention of the adaptor and 60S particles, while addition of a heterologous NES can restore export (johnson2002nuclearexportof pages 2-3).

A yeast-focused mechanistic synthesis (thesis excerpt) reports mapping of a C-terminal NLS (aa 399–419) and NES (aa 496–505); a canonical leucine-rich NES sequence is also described (LLDELDEMTL) (west2006nmd3pthenuclear pages 172-176).

2.5. Molecular mechanism from high-resolution cryo-EM (late cytoplasmic maturation)

Malyutin et al. reported that Nmd3 is a structural mimic of eIF5A and that its binding includes insertion into the ribosomal E site and stabilization/closure of the L1 stalk; other Nmd3 regions occupy/approach the P site and connect to Tif6-associated regions (malyutin2017nmd3isa pages 1-2). They reported cryo-EM structures of relevant complexes at 3.1 Å (60S–Nmd3) and 3.3 Å (60S–Nmd3–Lsg1–Tif6), helping explain how late cytoplasmic remodeling and factor release are coupled (malyutin2017nmd3isa pages 1-2).

3. Recent developments (prioritizing 2023–2024)

3.1. 2023: rRNA modification checkpoint upstream of Nmd3 export competence

Two 2023 studies provided strong evidence that a single rRNA 2′-O-methylation at Gm2922 gates late 60S biogenesis and nuclear export competence by controlling Nog2 behavior.

• Yelland et al. (publication date: Dec 2023) showed that methylation of a single nucleotide in the large subunit catalytic center “gates ribosome assembly” and is needed for efficient nuclear export; they used massively parallel mutational scanning of Nog2 to identify bypass substitutions and used cryo-EM to visualize methylation-dependent structural engagement (yelland2023asingle2′omethylation pages 1-2). Because Nmd3 is loaded late in nuclear maturation, such checkpoints are directly relevant to the timing/availability of Nmd3 recruitment and subsequent export.
• Sekulski et al. (publication date: May 2023) showed that loss of Spb1-dependent methylation leads to premature Nog2 activation and impaired recruitment/binding dynamics of Nog2 to nucleoplasmic intermediates, proposing a kinetic checkpoint near the nucleolar/nucleoplasmic boundary (sekulski2023rrnamethylationby pages 1-2).

These studies do not primarily re-characterize Nmd3 directly, but they reshape the current understanding of what makes a pre-60S particle “export-ready” for downstream export factors such as Nmd3.

3.2. 2023: quantitative live-cell export kinetics support cooperative CRM1 transport (conserved logic)

Junod et al. (publication date: Aug 2023) quantified pre-ribosome export dynamics by high-speed single-molecule microscopy in live mammalian cells. They report:
- ~two-thirds of NPC interactions lead to successful export.
- CRM1 inhibition reduces export efficiency 11–17-fold.
- CRM1 recognition of pre-60S is mediated by an NES on Nmd3, and they propose cooperative CRM1 usage to chaperone large cargo through the NPC (junod2023dynamicsofnuclear pages 1-3).

While this work is not in yeast, it provides an experimentally grounded quantitative framework for the conserved Nmd3–CRM1 axis.

3.3. 2024: conserved late-maturation factor biology around LSG1/NMD3

A 2024 study focused on human LSG1 reported that LSG1 is required for eviction/recycling of NMD3 in the cytoplasm, probing conserved biology of the LSG1–NMD3 stage of 60S maturation (junod2023dynamicsofnuclear pages 1-3). Although not yeast, it is relevant to interpreting yeast pathway conservation.

4. Current applications and real-world implementations

4.1. Experimental readouts for 60S export and export competence

Nmd3 is embedded in widely used experimental logic for ribosome export:
- Rpl25–GFP nuclear accumulation is used as a 60S export assay; nmd3 mutants cause nuclear retention of this reporter (gadal2001nuclearexportof pages 1-2).
- Structural studies use purified pre-60S/60S complexes containing Nmd3 to define late maturation states and factor occupancy, demonstrating that Nmd3 provides a tractable handle for isolating/export-competence states (sengupta2010characterizationofthe pages 1-2).

4.2. Generalizable nuclear export principles

Nmd3 is often cited as a canonical example of a cargo adaptor (providing an NES) enabling a general export receptor (Crm1) to transport a large RNP (60S) (johnson2002nuclearexportof pages 2-3). This makes Nmd3 a reference point in models of NPC transport specificity and large-cargo export.

5. Statistics and quantitative data points (from primary studies)

Key quantitative/structural datapoints available in the reviewed evidence include:
- Stoichiometry: Nmd3 binds 60S at a maximum ~1:1 stoichiometry, even at 81-fold excess Nmd3; binds 60S but not 80S (sengupta2010characterizationofthe pages 1-2).
- Cryo-EM resolution: 60S–Nmd3 at 3.1 Å and 60S–Nmd3–Lsg1–Tif6 at 3.3 Å (malyutin2017nmd3isa pages 1-2).
- Export efficiency (conserved, mammalian): ~two-thirds NPC interactions successful; CRM1 inhibition decreases efficiency 11–17-fold (junod2023dynamicsofnuclear pages 1-3).

6. Consolidated evidence table

Table: This table compiles the main mechanistic and structural evidence supporting the role of yeast Nmd3/YHR170W as the essential 60S ribosomal export adaptor. It also highlights 2023 studies that refine the timing and checkpoints upstream or downstream of Nmd3-mediated export.

7. Limitations and scope notes

• Many of the most quantitative export-dynamics measurements are currently available from mammalian imaging work (junod2023dynamicsofnuclear pages 1-3). Yeast-specific quantitative NPC transit statistics were not extracted from the available texts in this run.
• A 2006 thesis excerpt is used for some NLS/NES mapping details (west2006nmd3pthenuclear pages 172-176); core pathway conclusions are corroborated by peer-reviewed primary and review literature (gadal2001nuclearexportof pages 1-2, johnson2002nuclearexportof pages 2-3, hedges2005releaseofthe pages 1-2, sengupta2010characterizationofthe pages 1-2, malyutin2017nmd3isa pages 1-2).

Key cited sources (with publication dates and URLs)

• Gadal O. et al. 2001-05. Molecular and Cellular Biology. “Nuclear export of 60S ribosomal subunits depends on Xpo1p and requires… Nmd3p…” https://doi.org/10.1128/mcb.21.10.3405-3415.2001 (gadal2001nuclearexportof pages 1-2)
• Johnson A.W. et al. 2002-11. Trends in Biochemical Sciences. “Nuclear export of ribosomal subunits.” https://doi.org/10.1016/S0968-0004(02)02208-9 (johnson2002nuclearexportof pages 2-3)
• Hedges J. et al. 2005-02. The EMBO Journal. “Release of the export adapter, Nmd3p, from the 60S… requires Rpl10p and… Lsg1p.” https://doi.org/10.1038/sj.emboj.7600547 (hedges2005releaseofthe pages 1-2)
• Sengupta J. et al. 2010-06. The Journal of Cell Biology. “Characterization of the nuclear export adaptor protein Nmd3…” https://doi.org/10.1083/jcb.201001124 (sengupta2010characterizationofthe pages 1-2)
• Malyutin A.G. et al. 2017-02. The EMBO Journal. “Nmd3 is a structural mimic of eIF5A, and activates… Lsg1…” https://doi.org/10.15252/embj.201696012 (malyutin2017nmd3isa pages 1-2)
• Sekulski K. et al. 2023-05. Nature Communications. “rRNA methylation by Spb1 regulates the GTPase activity of Nog2…” https://doi.org/10.1038/s41467-023-36867-5 (sekulski2023rrnamethylationby pages 1-2)
• Yelland J.N. et al. 2023-12 (journal issue date shown; DOI indicates 2022 online publication). Nature Structural & Molecular Biology. “A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome.” https://doi.org/10.1038/s41594-022-00891-8 (yelland2023asingle2′omethylation pages 1-2)
• Junod S.L. et al. 2023-08. iScience. “Dynamics of nuclear export of pre-ribosomal subunits revealed by high-speed single-molecule microscopy…” https://doi.org/10.1016/j.isci.2023.107445 (junod2023dynamicsofnuclear pages 1-3)

References

1. (gadal2001nuclearexportof pages 1-2): Olivier Gadal, Daniela Strauß, Jacques Kessl, Bernard Trumpower, David Tollervey, and Ed Hurt. Nuclear export of 60s ribosomal subunits depends on xpo1p and requires a nuclear export sequence-containing factor, nmd3p, that associates with the large subunit protein rpl10p. Molecular and Cellular Biology, 21:3405-3415, May 2001. URL: https://doi.org/10.1128/mcb.21.10.3405-3415.2001, doi:10.1128/mcb.21.10.3405-3415.2001. This article has 403 citations and is from a domain leading peer-reviewed journal.

2. (johnson2002nuclearexportof pages 2-3): Arlen W Johnson, Elsebet Lund, and James Dahlberg. Nuclear export of ribosomal subunits. Trends in biochemical sciences, 27 11:580-5, Nov 2002. URL: https://doi.org/10.1016/s0968-0004(02)02208-9, doi:10.1016/s0968-0004(02)02208-9. This article has 211 citations and is from a domain leading peer-reviewed journal.

3. (malyutin2017nmd3isa pages 1-2): Andrey G Malyutin, Sharmishtha Musalgaonkar, Stephanie Patchett, Joachim Frank, and Arlen W Johnson. Nmd3 is a structural mimic of eif5a, and activates the cpgtpase lsg1 during 60s ribosome biogenesis. The EMBO Journal, 36:854-868, Feb 2017. URL: https://doi.org/10.15252/embj.201696012, doi:10.15252/embj.201696012. This article has 89 citations.

4. (johnson2002nuclearexportof pages 1-2): Arlen W Johnson, Elsebet Lund, and James Dahlberg. Nuclear export of ribosomal subunits. Trends in biochemical sciences, 27 11:580-5, Nov 2002. URL: https://doi.org/10.1016/s0968-0004(02)02208-9, doi:10.1016/s0968-0004(02)02208-9. This article has 211 citations and is from a domain leading peer-reviewed journal.

5. (sengupta2010characterizationofthe pages 1-2): Jayati Sengupta, Cyril Bussiere, Jesper Pallesen, Matthew West, Arlen W. Johnson, and Joachim Frank. Characterization of the nuclear export adaptor protein nmd3 in association with the 60s ribosomal subunit. The Journal of Cell Biology, 189:1079-1086, Jun 2010. URL: https://doi.org/10.1083/jcb.201001124, doi:10.1083/jcb.201001124. This article has 92 citations.

6. (sengupta2010characterizationofthe media 9c1f3f22): Jayati Sengupta, Cyril Bussiere, Jesper Pallesen, Matthew West, Arlen W. Johnson, and Joachim Frank. Characterization of the nuclear export adaptor protein nmd3 in association with the 60s ribosomal subunit. The Journal of Cell Biology, 189:1079-1086, Jun 2010. URL: https://doi.org/10.1083/jcb.201001124, doi:10.1083/jcb.201001124. This article has 92 citations.

7. (hedges2005releaseofthe pages 1-2): John Hedges, Matthew West, and Arlen W Johnson. Release of the export adapter, nmd3p, from the 60s ribosomal subunit requires rpl10p and the cytoplasmic gtpase lsg1p. The EMBO Journal, 24:567-579, Feb 2005. URL: https://doi.org/10.1038/sj.emboj.7600547, doi:10.1038/sj.emboj.7600547. This article has 226 citations.

8. (west2006nmd3pthenuclear pages 172-176): MB West. Nmd3p, the nuclear export adapter for the 60s ribosomal subunit: characterization of its recycling mechanism and novel interaction with the nuclear pore …. Unknown journal, 2006.

9. (yelland2023asingle2′omethylation pages 1-2): James N. Yelland, Jack P. K. Bravo, Joshua J. Black, David W. Taylor, and Arlen W. Johnson. A single 2′-o-methylation of ribosomal rna gates assembly of a functional ribosome. Nature Structural & Molecular Biology, 30:91-98, Dec 2023. URL: https://doi.org/10.1038/s41594-022-00891-8, doi:10.1038/s41594-022-00891-8. This article has 42 citations and is from a highest quality peer-reviewed journal.

10. (sekulski2023rrnamethylationby pages 1-2): Kamil Sekulski, Victor Emmanuel Cruz, Christine S. Weirich, and Jan P. Erzberger. Rrna methylation by spb1 regulates the gtpase activity of nog2 during 60s ribosomal subunit assembly. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-36867-5, doi:10.1038/s41467-023-36867-5. This article has 15 citations and is from a highest quality peer-reviewed journal.

11. (junod2023dynamicsofnuclear pages 1-3): Samuel L. Junod, Mark Tingey, Joseph M. Kelich, Alexander Goryaynov, Karl Herbine, and Weidong Yang. Dynamics of nuclear export of pre-ribosomal subunits revealed by high-speed single-molecule microscopy in live cells. iScience, 26:107445, Aug 2023. URL: https://doi.org/10.1016/j.isci.2023.107445, doi:10.1016/j.isci.2023.107445. This article has 9 citations and is from a peer-reviewed journal.

12. (west2006nmd3pthenuclear pages 38-43): MB West. Nmd3p, the nuclear export adapter for the 60s ribosomal subunit: characterization of its recycling mechanism and novel interaction with the nuclear pore …. Unknown journal, 2006.

Citations

1. johnson2002nuclearexportof pages 1-2
2. gadal2001nuclearexportof pages 1-2
3. sengupta2010characterizationofthe pages 1-2
4. hedges2005releaseofthe pages 1-2
5. johnson2002nuclearexportof pages 2-3
6. sekulski2023rrnamethylationby pages 1-2
7. junod2023dynamicsofnuclear pages 1-3
8. https://doi.org/10.1128/mcb.21.10.3405-3415.2001
9. https://doi.org/10.1016/S0968-0004(02
10. https://doi.org/10.1038/sj.emboj.7600547
11. https://doi.org/10.1083/jcb.201001124
12. https://doi.org/10.15252/embj.201696012
13. https://doi.org/10.1038/s41467-023-36867-5
14. https://doi.org/10.1038/s41594-022-00891-8
15. https://doi.org/10.1016/j.isci.2023.107445
16. https://doi.org/10.1128/mcb.21.10.3405-3415.2001,
17. https://doi.org/10.1016/s0968-0004(02
18. https://doi.org/10.15252/embj.201696012,
19. https://doi.org/10.1083/jcb.201001124,
20. https://doi.org/10.1038/sj.emboj.7600547,
21. https://doi.org/10.1038/s41594-022-00891-8,
22. https://doi.org/10.1038/s41467-023-36867-5,
23. https://doi.org/10.1016/j.isci.2023.107445,