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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: P40486
• Protein Description: RecName: Full=Protein SHQ1; AltName: Full=Small nucleolar RNAs of the box H/ACA family quantitative accumulation protein 1;
• Gene Information: Name=SHQ1; OrderedLocusNames=YIL104C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the SHQ1 family. .
• Key Domains: CS_dom. (IPR007052); HSP20-like_chaperone. (IPR008978); Shq1. (IPR039742); SHQ1-like_CS. (IPR048696); Shq1_C. (IPR007009)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SHQ1" 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 'SHQ1' 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 SHQ1 (gene ID: SHQ1, UniProt: P40486) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P40486
• Protein Description: RecName: Full=Protein SHQ1; AltName: Full=Small nucleolar RNAs of the box H/ACA family quantitative accumulation protein 1;
• Gene Information: Name=SHQ1; OrderedLocusNames=YIL104C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the SHQ1 family. .
• Key Domains: CS_dom. (IPR007052); HSP20-like_chaperone. (IPR008978); Shq1. (IPR039742); SHQ1-like_CS. (IPR048696); Shq1_C. (IPR007009)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SHQ1" 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 'SHQ1' 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 SHQ1 (gene ID: SHQ1, UniProt: P40486) 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: Functional Annotation of SHQ1 (YIL104C; UniProt P40486) in Saccharomyces cerevisiae (S288c)

1. Target verification (gene/protein identity)

The research target is yeast SHQ1/Shq1p encoded by YIL104C (UniProt P40486) in Saccharomyces cerevisiae S288c, described in primary literature as a conserved H/ACA RNP assembly factor that binds the yeast dyskerin homolog Cbf5p and acts as an assembly chaperone. The mechanistic descriptions and domain architecture reported in yeast studies match UniProt domain annotations: an N‑terminal CS (CHORD-and-Sgt1/HSP20-like cochaperone-like) domain and a C‑terminal Shq1-specific domain that functions as an RNA mimic/placeholder on Cbf5p. (godin2009theboxhaca pages 1-2, massenet2017assemblyandtrafficking pages 7-10, godin2009theboxhaca pages 2-4)

2. Key concepts and definitions (current understanding)

2.1 H/ACA snoRNPs and pseudouridylation context

Box H/ACA snoRNPs are essential ribonucleoprotein machines that guide conversion of uridine to pseudouridine in target RNAs (notably rRNA), a process central to ribosome biogenesis and multiple RNA processing pathways. In eukaryotes, the mature H/ACA snoRNP core includes the pseudouridine synthase Cbf5p/dyskerin plus core proteins Nop10p, Nhp2p, and Gar1p. In addition to these core proteins, assembly factors coordinate correct RNP formation and prevent non-productive interactions during biogenesis. (godin2009theboxhaca pages 1-2, massenet2017assemblyandtrafficking pages 7-10)

2.2 SHQ1 as an assembly factor / chaperone (definition)

Yeast Shq1p is defined experimentally as an essential assembly factor for eukaryotic H/ACA RNPs, including particles involved in ribosome biogenesis and telomere biology. Mechanistically, it is best described as a dedicated chaperone for Cbf5p that binds Cbf5p early and prevents inappropriate RNA binding and/or aggregation prior to formation of the mature H/ACA snoRNP. (li2011structureofthe pages 1-2, walbott2011thehacarnp pages 1-2, massenet2017assemblyandtrafficking pages 7-10)

2.3 “RNA mimic/placeholder” mechanism (definition)

Structural studies show that the C-terminal portion of Shq1p contacts the RNA-binding surface of Cbf5p (notably the PUA domain region) in a way that mimics guide RNA binding, thereby acting as an RNA placeholder. This explains how SHQ1 can protect Cbf5p from non-specific RNA interactions before assembly with authentic H/ACA RNA and other core proteins. (walbott2011thehacarnp pages 1-2, li2011structureofthe pages 5-7, walbott2011thehacarnp media 3caa9278)

3. Molecular function and mechanism (yeast-specific evidence)

3.1 Primary molecular function: Cbf5 chaperoning during pre-snoRNP assembly

Multiple independent yeast studies converge on a model in which Shq1p binds Cbf5p directly and functions as an assembly chaperone rather than as a stable component of mature H/ACA snoRNPs. In vitro and in vivo evidence supports that SHQ1’s interaction is transient, consistent with a pre-assembly role. (godin2009theboxhaca pages 1-2, godin2009theboxhaca pages 8-9)

3.2 Domain organization and mechanistic roles

Two-domain architecture: Yeast Shq1p is composed of two structurally independent domains. The N-terminal domain adopts a CS fold (Chord-and-Sgt1) reminiscent of Hsp90 co-chaperones; the C-terminal domain provides key client interaction and chaperone-like activity. (godin2009theboxhaca pages 1-2, godin2009theboxhaca pages 2-4)

Chaperone-like activity: Shq1p exhibits intrinsic chaperone activity, primarily residing in the C-terminal domain but enhanced by the presence of the N-terminal domain when both are present in cis. (godin2009theboxhaca pages 1-2, godin2009theboxhaca pages 7-8)

3.3 Structural basis for binding: “clamp” on Cbf5 and overlap with H/ACA RNA binding

An EMBO Journal study determined structures of the Shq1-specific domain and a complex with Cbf5–Nop10–Gar1, showing that Shq1 makes primary contacts with the PUA domain and the Cbf5 C-terminal extension, and that the binding surface overlaps with the H/ACA RNA interface—supporting the “placeholder” hypothesis. (li2011structureofthe pages 1-2, li2011structureofthe pages 5-7)

A complementary Genes & Development structure specifically supports the RNA-mimicry mechanism: the Shq1 C-terminal domain occupies RNA-binding sites on Cbf5, and comparison to guide RNA-bound archaeal complexes suggests structural mimicry of RNA elements (including portions corresponding to guide RNA features). (walbott2011thehacarnp pages 1-2, walbott2011thehacarnp media 3caa9278)

4. Interaction partners and pathway placement

4.1 Direct binding partner: Cbf5p (yeast dyskerin)

Yeast Shq1p binds Cbf5p directly; the interaction is strongest with full-length Shq1p and is mediated largely by the C-terminal domain (with the N-terminal domain contributing synergistically). (godin2009theboxhaca pages 1-2, godin2009theboxhaca pages 2-4)

4.2 Relationship to other H/ACA proteins and assembly factor Naf1

Biochemical evidence indicates that Nop10, Nhp2, Gar1, and the assembly factor Naf1 do not disrupt the Shq1–Cbf5 interaction in vitro, consistent with a model where SHQ1 can bind Cbf5 independently in an early assembly intermediate. (li2011structureofthe pages 5-7)

However, review synthesis highlights that experimental results across systems have suggested potentially different assembly orders: in some experiments an RNA-free complex containing SHQ1, NAF1, NHP2, NOP10, and DKC1/Cbf5 can be reconstituted, while other experiments suggest SHQ1 binding may exclude recruitment of certain factors, implying SHQ1 must be released before or during later assembly steps. (massenet2017assemblyandtrafficking pages 7-10)

4.3 H/ACA RNA competes with SHQ1: handoff model

H/ACA RNAs can compete SHQ1 off Cbf5 by binding an overlapping site on the Cbf5 PUA domain, and this displacement can be RNA-specific and enhanced by Nhp2, supporting a regulated handoff from an SHQ1-bound Cbf5 complex to an RNA-containing pre-snoRNP. (li2011structureofthe pages 5-7)

5. Subcellular localization (where SHQ1 acts)

Primary evidence indicates that Naf1 and Shq1 localize to the nucleoplasm and are excluded from nucleoli and Cajal bodies, supporting a role in early assembly before mature particle localization to sites of rRNA modification. A review further classifies SHQ1 (with NAF1) as a nucleocytoplasmic shuttling factor, consistent with an early, pre-snoRNP assembly role rather than functioning within mature nucleolar H/ACA snoRNPs. (li2011structureofthe pages 1-2, massenet2017assemblyandtrafficking pages 7-10)

6. Phenotypes and essentiality (functional importance in yeast)

Yeast SHQ1 is essential for viability, and mutations in Shq1 that disrupt interaction with Cbf5 lead to growth defects, especially at elevated temperatures. (li2011structureofthe pages 1-2, li2011structureofthe pages 5-7)

Functional disruption/depletion of SHQ1 is associated with unstable accumulation of H/ACA snoRNAs and rRNA processing defects, consistent with failure of H/ACA snoRNP biogenesis. (walbott2011thehacarnp pages 1-2, godin2009theboxhaca pages 1-2)

7. Quantitative data and key statistics from experimental studies

7.1 Structural biology (resolution/quality metrics)

Walbott et al., 2011 (Genes & Development; published Nov 2011):
- Crystal structure of yeast Shq1pC at 1.5 Å (native) and 1.6 Å (SeMet SAD). (walbott2011thehacarnp pages 8-9, walbott2011thehacarnp pages 2-3)
- Structure of Shq1pC/Cbf5pΔcat complex refined to 2.8 Å. (walbott2011thehacarnp pages 8-9, walbott2011thehacarnp pages 2-3)

Li et al., 2011 (EMBO Journal; published Dec 2011):
- SHQ1-specific domain crystal datasets include 1.6 Å (native) and 2.1 Å (Se-derivative) and a multi-protein complex refined to 3.06 Å. (li2011structureofthe pages 8-10)

Godin et al., 2009 (Journal of Molecular Biology; published Jul 2009):
- NMR structure statistics for the N-terminal CS domain: 4521 NOEs used, resulting in 20 refined structures with average backbone/heavy-atom RMSDs 0.25 Å / 0.71 Å over the structured region; deposited as PDB 2K8V (with comparison to a related crystal structure 3EUD). (godin2009theboxhaca pages 2-4)

7.2 Quantified binding/interaction effects

In pull-down quantifications using truncation variants of dyskerin/NAP57 constructs, truncation NAP57 31–387 reduced binding to full-length SHQ1 by ~28% and to the SHQ1 C-terminal domain by ~34% (averages of three experiments ± SEM). (walbott2011thehacarnp pages 8-9)

In yeast Cbf5 mutant binding assays, deletion of the Cbf5 C-terminal extension substantially reduced SHQ1 binding, with experimental sensitivity sufficient to detect an approximately ~4-fold reduction in binding in the reported assays. (li2011structureofthe pages 5-7)

7.3 Experimental design statistics relevant to reproducibility

Li et al. provide explicit molar amounts for pull-down assembly assays (e.g., 120 pmol Cbf5 complex mixed with 480 pmol Shq1, i.e., 4-fold molar excess) and detailed crystallographic model validation (e.g., 98.4% Ramachandran favored for the SSD model). (li2011structureofthe pages 8-10)

8. Recent developments (2023–2024) and how they inform yeast SHQ1 annotation

Direct 2023–2024 yeast SHQ1 mechanistic papers were not identified in the retrieved set; recent work is predominantly in human SHQ1, but it strongly supports conserved SHQ1 function and highlights conserved residues and interaction networks that can be interpreted in the yeast system by homology.

8.1 Human genetics reinforces conserved essential mechanism

A 2023 report identified a homozygous SHQ1 p.I278T variant (c.833T>C) in unrelated families, located in a highly conserved region, with modeling suggesting destabilization of the C-terminal domain core. The paper explicitly ties SHQ1 function to protecting Cbf5/dyskerin complexes from nonspecific RNA binding/aggregation prior to H/ACA RNA assembly, aligning with yeast structural models. (alhargan2023shq1associatedneurodevelopmentaldisorder pages 2-4, alhargan2023shq1associatedneurodevelopmentaldisorder pages 1-2)

8.2 2024 variant and interactome analyses highlight conserved assembly partners

A 2024 study reported compound heterozygous variants including a recurrent frameshift p.Asp277Serfs*27 and a novel missense p.Tyr386Ser, and highlighted interactors that overlap strongly with the known H/ACA assembly network (GAR1, NAF1, DKC1, NOP10, NHP2, and also RUVBL1/2—R2TP-related AAA+ ATPases). These analyses further support SHQ1’s conserved placement at the start of H/ACA snoRNP assembly and its functional linkage to ribosome biogenesis and RNA processing. (gowda2024insilicocharacterization pages 1-2, gowda2024insilicocharacterization pages 2-3)

9. Current applications and real-world implementations

9.1 Yeast SHQ1 as a model for conserved H/ACA RNP assembly and disease mechanisms

Although yeast SHQ1 research is primarily fundamental, structural and mechanistic yeast studies are directly used as a model framework to interpret conserved SHQ1/dyskerin biology, including disease-relevant disruptions of H/ACA RNP assembly. In particular, yeast structural results demonstrating RNA-mimicry/placeholder binding to Cbf5 provide a mechanistic basis for understanding how SHQ1 perturbations could destabilize H/ACA RNP accumulation, consistent with 2023–2024 human SHQ1 neurodevelopmental disorder reports. (li2011structureofthe pages 1-2, alhargan2023shq1associatedneurodevelopmentaldisorder pages 2-4, walbott2011thehacarnp media 3caa9278)

9.2 Broader pathway relevance: telomerase and RNA processing

SHQ1 is described as required for H/ACA RNPs involved in telomere maintenance (via H/ACA motifs in telomerase RNA in eukaryotes) and also linked to pathways such as pre-mRNA splicing through H/ACA RNP function. In yeast, this relevance is indirect but arises from SHQ1’s essential role in producing functional H/ACA RNPs. (walbott2011thehacarnp pages 1-2)

10. Expert synthesis and interpretation (authoritative analysis)

Across the major yeast studies, the most consistent mechanistic interpretation is that SHQ1 is a dedicated, early-acting chaperone for Cbf5/dyskerin, preventing premature RNA association and thereby ensuring correct assembly order and quality control during H/ACA snoRNP biogenesis. Structural overlap between SHQ1 binding and H/ACA RNA binding to the Cbf5 PUA domain provides a concrete molecular basis for this function. (walbott2011thehacarnp pages 1-2, li2011structureofthe pages 5-7, walbott2011thehacarnp media 3caa9278)

The CS-domain similarity to canonical Hsp90 cochaperones has prompted hypotheses of chaperone-network integration, but yeast biochemical tests did not detect direct Hsp90 binding, suggesting SHQ1 is cochaperone-like by fold yet functionally specialized and possibly Hsp90-independent in yeast, while still fitting into a broader chaperone logic (client shielding, regulated release) emphasized in reviews. (godin2009theboxhaca pages 1-2, massenet2017assemblyandtrafficking pages 7-10, godin2009theboxhaca pages 7-8)

Summary table (evidence-linked)

The following table consolidates the core functional annotation elements (molecular function, localization, partners, phenotypes, and quantitative/structural data).

Table: This table summarizes experimentally supported knowledge about Saccharomyces cerevisiae SHQ1/YIL104C, including its molecular role, domains, interactions, localization, pathway placement, and phenotypes. It also notes the most relevant 2023-2024 developments from conserved human SHQ1 studies that inform yeast functional annotation by homology.

Key figure (structural mechanism)

A key structural panel illustrating SHQ1’s RNA-mimicry/placeholder binding to Cbf5 is available from Walbott et al. 2011 (Genes & Development) (Figure 2). (walbott2011thehacarnp media 3caa9278)

References (retrieved sources; with URLs and publication dates)

1. Godin KS, Walbott H, Leulliot N, van Tilbeurgh H, Varani G. The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme. Journal of Molecular Biology. 2009-07. https://doi.org/10.1016/j.jmb.2009.04.076 (godin2009theboxhaca pages 1-2, godin2009theboxhaca pages 2-4, godin2009theboxhaca pages 19-22)
2. Walbott H, Machado-Pinilla R, Liger D, et al. The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic. Genes & Development. 2011-11. https://doi.org/10.1101/gad.176834.111 (walbott2011thehacarnp pages 1-2, walbott2011thehacarnp media 3caa9278, walbott2011thehacarnp pages 8-9, walbott2011thehacarnp pages 2-3)
3. Li S, Duan J, Li D, Ma S, Ye K. Structure of the Shq1–Cbf5–Nop10–Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita. The EMBO Journal. 2011-12. https://doi.org/10.1038/emboj.2011.427 (li2011structureofthe pages 1-2, li2011structureofthe pages 5-7, li2011structureofthe pages 8-10, li2011structureofthe pages 7-8)
4. Massenet S, Bertrand E, Verheggen C. Assembly and trafficking of box C/D and H/ACA snoRNPs. RNA Biology. 2017-12. https://doi.org/10.1080/15476286.2016.1243646 (massenet2017assemblyandtrafficking pages 7-10)
5. AlHargan A, AlMuhaizea MA, Almass R, et al. SHQ1-associated neurodevelopmental disorder: Report of the first homozygous variant in unrelated patients and review of the literature. Human Genome Variation. 2023-02. https://doi.org/10.1038/s41439-023-00234-z (alhargan2023shq1associatedneurodevelopmentaldisorder pages 2-4, alhargan2023shq1associatedneurodevelopmentaldisorder pages 1-2)
6. Gowda VK, Srinivasan VM, Srivastava S, et al. In silico characterization and identification of compound heterozygous variants in H/ACA Ribonucleoprotein Assembly Factor (SHQ1) from Indian population. Journal of Family Medicine and Primary Care. 2024-01. https://doi.org/10.4103/jfmpc.jfmpc_979_23 (gowda2024insilicocharacterization pages 1-2, gowda2024insilicocharacterization pages 2-3)

References

1. (godin2009theboxhaca pages 1-2): Katherine S. Godin, Hélène Walbott, Nicolas Leulliot, Herman van Tilbeurgh, and Gabriele Varani. The box h/aca snornp assembly factor shq1p is a chaperone protein homologous to hsp90 cochaperones that binds to the cbf5p enzyme. Journal of molecular biology, 390 2:231-44, Jul 2009. URL: https://doi.org/10.1016/j.jmb.2009.04.076, doi:10.1016/j.jmb.2009.04.076. This article has 26 citations and is from a domain leading peer-reviewed journal.

2. (massenet2017assemblyandtrafficking pages 7-10): Séverine Massenet, Edouard Bertrand, and Céline Verheggen. Assembly and trafficking of box c/d and h/aca snornps. RNA Biology, 14:680-692, Dec 2017. URL: https://doi.org/10.1080/15476286.2016.1243646, doi:10.1080/15476286.2016.1243646. This article has 239 citations and is from a peer-reviewed journal.

3. (godin2009theboxhaca pages 2-4): Katherine S. Godin, Hélène Walbott, Nicolas Leulliot, Herman van Tilbeurgh, and Gabriele Varani. The box h/aca snornp assembly factor shq1p is a chaperone protein homologous to hsp90 cochaperones that binds to the cbf5p enzyme. Journal of molecular biology, 390 2:231-44, Jul 2009. URL: https://doi.org/10.1016/j.jmb.2009.04.076, doi:10.1016/j.jmb.2009.04.076. This article has 26 citations and is from a domain leading peer-reviewed journal.

4. (li2011structureofthe pages 1-2): Shuang Li, Jingqi Duan, Dandan Li, Shoucai Ma, and Keqiong Ye. Structure of the shq1–cbf5–nop10–gar1 complex and implications for h/aca rnp biogenesis and dyskeratosis congenita. The EMBO Journal, 30:5010-5020, Dec 2011. URL: https://doi.org/10.1038/emboj.2011.427, doi:10.1038/emboj.2011.427. This article has 64 citations.

5. (walbott2011thehacarnp pages 1-2): Hélène Walbott, Rosario Machado-Pinilla, Dominique Liger, Magali Blaud, Stéphane Réty, Petar N. Grozdanov, Kate Godin, Herman van Tilbeurgh, Gabriele Varani, U. Thomas Meier, and Nicolas Leulliot. The h/aca rnp assembly factor shq1 functions as an rna mimic. Genes & Development, 25:2398-2408, Nov 2011. URL: https://doi.org/10.1101/gad.176834.111, doi:10.1101/gad.176834.111. This article has 79 citations and is from a highest quality peer-reviewed journal.

6. (li2011structureofthe pages 5-7): Shuang Li, Jingqi Duan, Dandan Li, Shoucai Ma, and Keqiong Ye. Structure of the shq1–cbf5–nop10–gar1 complex and implications for h/aca rnp biogenesis and dyskeratosis congenita. The EMBO Journal, 30:5010-5020, Dec 2011. URL: https://doi.org/10.1038/emboj.2011.427, doi:10.1038/emboj.2011.427. This article has 64 citations.

7. (walbott2011thehacarnp media 3caa9278): Hélène Walbott, Rosario Machado-Pinilla, Dominique Liger, Magali Blaud, Stéphane Réty, Petar N. Grozdanov, Kate Godin, Herman van Tilbeurgh, Gabriele Varani, U. Thomas Meier, and Nicolas Leulliot. The h/aca rnp assembly factor shq1 functions as an rna mimic. Genes & Development, 25:2398-2408, Nov 2011. URL: https://doi.org/10.1101/gad.176834.111, doi:10.1101/gad.176834.111. This article has 79 citations and is from a highest quality peer-reviewed journal.

8. (godin2009theboxhaca pages 8-9): Katherine S. Godin, Hélène Walbott, Nicolas Leulliot, Herman van Tilbeurgh, and Gabriele Varani. The box h/aca snornp assembly factor shq1p is a chaperone protein homologous to hsp90 cochaperones that binds to the cbf5p enzyme. Journal of molecular biology, 390 2:231-44, Jul 2009. URL: https://doi.org/10.1016/j.jmb.2009.04.076, doi:10.1016/j.jmb.2009.04.076. This article has 26 citations and is from a domain leading peer-reviewed journal.

9. (godin2009theboxhaca pages 7-8): Katherine S. Godin, Hélène Walbott, Nicolas Leulliot, Herman van Tilbeurgh, and Gabriele Varani. The box h/aca snornp assembly factor shq1p is a chaperone protein homologous to hsp90 cochaperones that binds to the cbf5p enzyme. Journal of molecular biology, 390 2:231-44, Jul 2009. URL: https://doi.org/10.1016/j.jmb.2009.04.076, doi:10.1016/j.jmb.2009.04.076. This article has 26 citations and is from a domain leading peer-reviewed journal.

10. (walbott2011thehacarnp pages 8-9): Hélène Walbott, Rosario Machado-Pinilla, Dominique Liger, Magali Blaud, Stéphane Réty, Petar N. Grozdanov, Kate Godin, Herman van Tilbeurgh, Gabriele Varani, U. Thomas Meier, and Nicolas Leulliot. The h/aca rnp assembly factor shq1 functions as an rna mimic. Genes & Development, 25:2398-2408, Nov 2011. URL: https://doi.org/10.1101/gad.176834.111, doi:10.1101/gad.176834.111. This article has 79 citations and is from a highest quality peer-reviewed journal.

11. (walbott2011thehacarnp pages 2-3): Hélène Walbott, Rosario Machado-Pinilla, Dominique Liger, Magali Blaud, Stéphane Réty, Petar N. Grozdanov, Kate Godin, Herman van Tilbeurgh, Gabriele Varani, U. Thomas Meier, and Nicolas Leulliot. The h/aca rnp assembly factor shq1 functions as an rna mimic. Genes & Development, 25:2398-2408, Nov 2011. URL: https://doi.org/10.1101/gad.176834.111, doi:10.1101/gad.176834.111. This article has 79 citations and is from a highest quality peer-reviewed journal.

12. (li2011structureofthe pages 8-10): Shuang Li, Jingqi Duan, Dandan Li, Shoucai Ma, and Keqiong Ye. Structure of the shq1–cbf5–nop10–gar1 complex and implications for h/aca rnp biogenesis and dyskeratosis congenita. The EMBO Journal, 30:5010-5020, Dec 2011. URL: https://doi.org/10.1038/emboj.2011.427, doi:10.1038/emboj.2011.427. This article has 64 citations.

13. (alhargan2023shq1associatedneurodevelopmentaldisorder pages 2-4): Aljouhra AlHargan, Mohammed A. AlMuhaizea, Rawan Almass, Ali H. Alwadei, Maha Daghestani, Stefan T. Arold, and Namik Kaya. Shq1-associated neurodevelopmental disorder: report of the first homozygous variant in unrelated patients and review of the literature. Human Genome Variation, Feb 2023. URL: https://doi.org/10.1038/s41439-023-00234-z, doi:10.1038/s41439-023-00234-z. This article has 10 citations.

14. (alhargan2023shq1associatedneurodevelopmentaldisorder pages 1-2): Aljouhra AlHargan, Mohammed A. AlMuhaizea, Rawan Almass, Ali H. Alwadei, Maha Daghestani, Stefan T. Arold, and Namik Kaya. Shq1-associated neurodevelopmental disorder: report of the first homozygous variant in unrelated patients and review of the literature. Human Genome Variation, Feb 2023. URL: https://doi.org/10.1038/s41439-023-00234-z, doi:10.1038/s41439-023-00234-z. This article has 10 citations.

15. (gowda2024insilicocharacterization pages 1-2): Vykuntaraju K. Gowda, Varunvenkat M. Srinivasan, Sudhanshu Srivastava, Noor Ghali, Uddhav Kinhal, Asha Shamnur, and Anshika Srivastava. In silico characterization and identification of compound heterozygous variants in h/aca ribonucleoprotein assembly factor (shq1) from indian population. Journal of Family Medicine and Primary Care, 13:208-220, Jan 2024. URL: https://doi.org/10.4103/jfmpc.jfmpc_979_23, doi:10.4103/jfmpc.jfmpc_979_23. This article has 0 citations and is from a peer-reviewed journal.

16. (gowda2024insilicocharacterization pages 2-3): Vykuntaraju K. Gowda, Varunvenkat M. Srinivasan, Sudhanshu Srivastava, Noor Ghali, Uddhav Kinhal, Asha Shamnur, and Anshika Srivastava. In silico characterization and identification of compound heterozygous variants in h/aca ribonucleoprotein assembly factor (shq1) from indian population. Journal of Family Medicine and Primary Care, 13:208-220, Jan 2024. URL: https://doi.org/10.4103/jfmpc.jfmpc_979_23, doi:10.4103/jfmpc.jfmpc_979_23. This article has 0 citations and is from a peer-reviewed journal.

17. (godin2009theboxhaca pages 19-22): Katherine S. Godin, Hélène Walbott, Nicolas Leulliot, Herman van Tilbeurgh, and Gabriele Varani. The box h/aca snornp assembly factor shq1p is a chaperone protein homologous to hsp90 cochaperones that binds to the cbf5p enzyme. Journal of molecular biology, 390 2:231-44, Jul 2009. URL: https://doi.org/10.1016/j.jmb.2009.04.076, doi:10.1016/j.jmb.2009.04.076. This article has 26 citations and is from a domain leading peer-reviewed journal.

18. (li2011structureofthe pages 7-8): Shuang Li, Jingqi Duan, Dandan Li, Shoucai Ma, and Keqiong Ye. Structure of the shq1–cbf5–nop10–gar1 complex and implications for h/aca rnp biogenesis and dyskeratosis congenita. The EMBO Journal, 30:5010-5020, Dec 2011. URL: https://doi.org/10.1038/emboj.2011.427, doi:10.1038/emboj.2011.427. This article has 64 citations.

Citations

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2. massenet2017assemblyandtrafficking pages 7-10
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4. godin2009theboxhaca pages 2-4
5. walbott2011thehacarnp pages 8-9
6. walbott2011thehacarnp pages 1-2
7. godin2009theboxhaca pages 1-2
8. li2011structureofthe pages 1-2
9. godin2009theboxhaca pages 8-9
10. godin2009theboxhaca pages 7-8
11. walbott2011thehacarnp pages 2-3
12. gowda2024insilicocharacterization pages 1-2
13. gowda2024insilicocharacterization pages 2-3
14. godin2009theboxhaca pages 19-22
15. li2011structureofthe pages 7-8
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17. https://doi.org/10.1101/gad.176834.111;
18. https://doi.org/10.1038/emboj.2011.427;
19. https://doi.org/10.1080/15476286.2016.1243646
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