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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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MOH1 (systematic name YBL049W; also referred to as YBL0518) encodes a small protein in Saccharomyces cerevisiae (strain ATCC 204508 / S288c) that is classified as a member of the Yippee protein family. The UniProt accession for this protein is P38191, and it is annotated as "Pro-Apoptotic protein MOH1" and "Protein yippee-like MOH1" (UniProt, ECO:0000303|PubMed:28173693). MOH1 contains a Yippee domain (InterPro: IPR034751, IPR004910, IPR039058; Pfam: PF03226), placing it in the broader Yippee/Mis18/Cereblon superfamily of zinc-binding proteins.
MOH1 belongs to the Yippee protein family, whose members share a highly conserved structural fold termed the β-tent fold. This fold consists of two four-stranded antiparallel β-meanders that pack at approximately right angles and coordinate a zinc ion at their apex (lupas2015thethalidomidebindingdomain pages 1-2). A β-hairpin inserted into the first β-meander extends across the bottom of the structure toward the second β-meander, forming a characteristic cradle-shaped binding site that is topologically conserved across all members of the fold (lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 9-10). The fold exhibits internal pseudosymmetry, suggesting it may have arisen through duplication of a subdomain-sized fragment (lupas2015thethalidomidebindingdomain pages 1-2).
Zinc coordination in yippee domain proteins is mediated by conserved C-X-X-C motifs located in specific loops of the structure (subramanian2016centromerelocalizationand pages 1-2). Structural studies on the closely related Mis18 protein have shown that the Yippee-like domain consists of two perpendicular antiparallel β-sheets (one three-stranded and one six-stranded) held together by a single Zn²⁺ ion coordinated through these C-X-X-C zinc-binding motifs (subramanian2016centromerelocalizationand pages 1-2). The binding pocket features conserved aromatic residues (including tyrosines, phenylalanines, and tryptophans) that form an aromatic cage implicated in protein–protein or protein–nucleic acid interactions (lupas2015thethalidomidebindingdomain pages 5-6).
The Yippee domain is evolutionarily related to several other well-characterized protein families. Lupas et al. (2015) demonstrated that the CULT domain of cereblon (the thalidomide-binding E3 ubiquitin ligase component), Mis18 (a centromere maintenance factor), and Drosophila Yippee are all members of the same β-tent fold superfamily, appearing roughly equidistant from each other in sequence space (lupas2015thethalidomidebindingdomain pages 1-2, lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 3-5). The β-tent fold also encompasses methionine sulfoxide reductase B (MsrB), the RIG-I helicase regulatory domain, and glutathione-dependent formaldehyde-activating enzyme (lupas2015thethalidomidebindingdomain pages 2-3). The fold serves primarily as a structural platform for mounting a functional binding site; the specific residues in the cradle-shaped groove determine the individual protein's binding partners and biological function (lupas2015thethalidomidebindingdomain pages 8-9).
The following table compares MOH1 with its yippee-family relatives across organisms:
| Protein name | Organism | Key function | Domain type | Zinc binding | Oligomerization | Key references from gathered evidence |
|---|---|---|---|---|---|---|
| MOH1 (YBL049W) | Saccharomyces cerevisiae | Stationary-phase-essential protein; supports long-term survival in quiescence/stationary phase; annotated in UniProt as pro-apoptotic, but direct mechanism was not retrievable from the available primary paper set | Yippee family domain / Yippee-Mis18-like β-tent fold (inferred from family assignment) | Predicted yes by family homology, but not directly shown for yeast MOH1 in retrieved papers | Not directly demonstrated in retrieved MOH1 papers | (martinez2004genomicanalysisof pages 7-8, martinez2004genomicanalysisof pages 8-9, martinez2004genomicanalysisof pages 9-10, lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 1-2) |
| Yippee | Drosophila melanogaster | Conserved eukaryotic protein of previously unknown/poorly defined molecular function; serves as the founding member of the Yippee family and structural reference for the fold | Yippee domain; β-tent fold with cradle-shaped binding site | Yes; family members typically coordinate Zn via conserved CXXC motifs/structural site | Family shows propensity for dimerization/oligomerization, though direct oligomeric state for Drosophila Yippee was not the focus of retrieved evidence | (lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 1-2, lupas2015thethalidomidebindingdomain pages 9-10) |
| YPEL1-5 (general human Yippee-like family) | Homo sapiens | Conserved regulatory proteins linked to apoptosis/senescence, development, and tumor suppression; family members provide the main orthology-based functional context for MOH1 | Yippee-like domain | Predicted/expected by family homology; direct zinc biochemistry not retrieved for all YPEL paralogs | Not established in the retrieved family-wide evidence | (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3, blancosanchez2020yippeelike3 pages 1-2, lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 1-2) |
| YPEL3 | Homo sapiens / vertebrate models | p53-inducible tumor suppressor; promotes senescence, suppresses EMT/metastasis, and is required for glial development/myelination in zebrafish | Yippee-like domain | Inferred from family homology; direct zinc-binding assay not retrieved in the YPEL3 paper | Not established in retrieved YPEL3 developmental paper | (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3, blancosanchez2020yippeelike3 pages 26-27, blancosanchez2020yippeelike3 pages 1-2) |
| Mis18 | Fission yeast and humans | Centromere maintenance factor; recruits/organizes machinery for CENP-A deposition and centromere identity maintenance | Yippee-like domain plus C-terminal α-helical region | Yes; Zn²⁺ coordinated through CXXC motifs in the Yippee-like domain | Yes; homodimerization/heterodimerization and higher-order oligomerization are central to function | (subramanian2016centromerelocalizationand pages 1-2, subramanian2016centromerelocalizationand pages 8-9, thamkachy2024structuralbasisfor pages 3-4, thamkachy2024structuralbasisfor pages 1-3, subramanian2016centromerelocalizationand pages 10-11) |
| Cereblon CULT domain | Animals and bacteria (domain family context) | Ligand-binding domain of cereblon; defines the CULT family and provides a key evolutionary/structural link to Yippee and Mis18 | CULT domain; β-tent fold | Yes in core structural models via conserved cysteine motifs, though some related β-tent proteins can lose the zinc site | Not the primary functional feature emphasized in retrieved evidence | (lupas2015thethalidomidebindingdomain pages 1-2, lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 8-9, lupas2015thethalidomidebindingdomain pages 3-5, lupas2015thethalidomidebindingdomain pages 2-3, lupas2015thethalidomidebindingdomain pages 6-8) |
| FAM72A-D | Homo sapiens | DNA maintenance/replication stress-associated factors; accumulate on chromatin during replication and genotoxic stress; FAM72B binds UNG and RPA and can suppress BER during class-switch recombination | MIS18/Yippee domain identified by structural annotation | Predicted by Yippee/MIS18 family assignment; direct zinc biochemistry was not detailed in retrieved FAM72 evidence | Yes; homo- and heterodimerization/multimerization reported for FAM72 family | (schou2024exploringthestructural pages 10-11) |
| SPIDR-associated Yippee/MIS18 domain annotation | Homo sapiens | Recent structural annotation places Yippee/MIS18-like domains in additional DNA maintenance proteins, expanding the family’s relevance beyond centromeres | MIS18/Yippee-like domain annotation | Predicted by domain assignment | Not established in the retrieved summary evidence | (schou2024exploringthestructural pages 10-11) |
Table: This table compares yeast MOH1 with structurally or functionally related Yippee-family proteins and domains across fungi, animals, and DNA maintenance systems. It is useful for inferring MOH1 function when direct biochemical characterization is limited.
The best-documented function of MOH1 in S. cerevisiae comes from a genome-wide analysis of stationary phase gene expression and viability by Martinez et al. (2004). MOH1 was identified as one of 127 stationary-phase-expressed genes whose transcripts reproducibly accumulate in cells during quiescence. More importantly, deletion of MOH1 resulted in approximately 10-fold loss of viability after 9 days of growth at 37°C, classifying it as a stationary-phase-essential (SP-essential) gene (martinez2004genomicanalysisof pages 7-8, martinez2004genomicanalysisof pages 8-9). This phenotype was specific: MOH1 was among nine SP-essential genes that were not required for growth on nonfermentable carbon sources, distinguishing it from the majority of SP-essential genes that encode mitochondrial or respiratory chain components (martinez2004genomicanalysisof pages 9-10). This indicates that MOH1's role in stationary-phase survival is not simply a consequence of respiratory deficiency but rather involves a specific function in maintaining cell viability during quiescence.
Martinez et al. (2004) described Moh1p as a "myristolated protein of unknown function" and noted that its sequence is related to Snf7p (an ESCRT-III component) according to SGD annotations available at the time (martinez2004genomicanalysisof pages 9-10). The study also established that SP-expressed and SP-essential genes, including MOH1, are more broadly conserved across the three major phylogenetic domains (Eukarya, Bacteria, Archaea) than yeast genes in general (martinez2004genomicanalysisof pages 8-9).
The UniProt annotation of MOH1 as a "Pro-Apoptotic protein" derives from the characterization reported in PubMed:28173693. While this primary publication was not directly retrievable in our literature searches, multiple lines of evidence support this functional assignment:
Human homologues induce apoptosis: Martinez et al. (2004) specifically noted that "the human homologues of MOH1 and NGR1 are known to induce apoptosis" (martinez2004genomicanalysisof pages 9-10). Of the 32 SP-essential genes identified, 23 have human homologues, and at least 13 of these are involved in apoptosis or are associated with human diseases including cancer.
YPEL family as apoptosis-associated proteins: The closest human orthologs of MOH1 are the YPEL (Yippee-like) protein family members (YPEL1–YPEL5). YPEL3, the best-characterized member, was originally identified as a senescence factor involved in the apoptotic phase of myeloid cell development and functions as a tumor suppressor (blancosanchez2020yippeelike3 pages 2-3). Under genotoxic stress, YPEL3 is an inducible target of p53. Overexpression of YPEL3 causes cell cycle arrest, suppresses epithelial-mesenchymal transition, and can be repressed by estrogen in ER+ mammary tumor cells (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 26-27). YPEL protein family members more broadly have been characterized as apoptosis-associated proteins that suppress proliferation of myeloid cells (blancosanchez2020yippeelike3 pages 25-26).
MOH1 in fungal stress and cell death pathways: The MOH1 gene in Candida albicans has been reported to interact genetically with the molecular chaperone Hsp90, and its expression is induced by various stress conditions (singhbabak2012globalanalysisof pages 4-5). A recent study by Wang et al. (2025) directly investigated MOH1 in Candida albicans in the context of ROS-dependent apoptosis in genotoxic stress response, though this paper was not fully accessible for our analysis.
In Candida glabrata, MOH1 was identified as one of four genes that acquired non-synonymous mutations during clinical evolution of echinocandin resistance. Whole-genome sequencing of serial clinical isolates revealed a MOH1 mutation (Y5H, resulting from a TAC→CAC codon change at position 5) that accompanied an early modest increase in echinocandin resistance (singhbabak2012globalanalysisof pages 4-5, singhbabak2012globalanalysisof pages 17-18). However, when the specific MOH1-T13C(Y5H) allele was cloned into a susceptible laboratory strain, it did not confer any increase in echinocandin resistance, suggesting that MOH1 changes may not directly drive resistance but could instead create a genetic background in which the primary FKS2 resistance mutation is less detrimental to fitness (singhbabak2012globalanalysisof pages 6-8). This finding positions MOH1 as a stress-responsive gene in fungal pathogens without a direct role in drug resistance per se.
According to UniProt annotations, MOH1 localizes to the cytoplasm. The dynamic subcellular localization of related yippee-family proteins provides additional context: YPEL3 in vertebrate cells shows dynamic localization during the cell cycle, residing in the nucleus, perinuclear structures, and near centrosomes during mitosis (blancosanchez2020yippeelike3 pages 2-3). This pattern suggests that yippee-family proteins, including potentially MOH1, may function as mobile regulatory factors rather than enzymes with fixed organellar localization.
The most extensively structurally characterized yippee-domain protein is Mis18, which functions in centromere maintenance by recruiting the CENP-A chaperone HJURP for centromeric histone deposition. The yippee-like domain of Mis18 mediates homo- and hetero-oligomerization that is essential for its centromere localization and function (subramanian2016centromerelocalizationand pages 8-9, subramanian2016centromerelocalizationand pages 1-2). In the human Mis18 complex, Mis18α and Mis18β contain yippee domains that form homodimers (Mis18α/Mis18α) or heterodimers (Mis18α/Mis18β), and their C-terminal helices form a 2:1 heterotrimer, assembling into a hetero-octameric complex (4 Mis18α, 2 Mis18β, 2 Mis18BP1) (thamkachy2024structuralbasisfor pages 3-4, thamkachy2024structuralbasisfor pages 1-3). This complex architecture is cell-cycle regulated and essential for centromere identity maintenance.
Schou et al. (2024) recently identified Yippee/MIS18-like domains in the FAM72A-D protein family through systematic structural annotation of DNA maintenance proteins. FAM72 proteins accumulate on chromatin during DNA replication and in response to genotoxic insults. FAM72B binds UNG (uracil-DNA glycosylase) and RPA subunits involved in DNA repair, and can suppress base excision repair during class-switch recombination in B cells (schou2024exploringthestructural pages 10-11). This expands the functional repertoire of the yippee domain family beyond centromere biology into active DNA damage response and repair pathways, and suggests that MOH1's β-tent fold may similarly function as a protein–protein interaction platform in stress-related processes.
| Gene / ORF | UniProt accession | Organism | Protein description | Protein family | Domain architecture | Subcellular localization | Key functions / current interpretation | Human orthologs / family context | Key phenotypes from deletion or mutation studies |
|---|---|---|---|---|---|---|---|---|---|
| MOH1 / YBL049W | P38191 | Saccharomyces cerevisiae strain S288c | Pro-apoptotic protein MOH1; protein yippee-like MOH1 (UniProt identity provided in prompt) | Yippee family; evolutionarily related to Mis18 and cereblon/CULT-domain proteins (lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 1-2, subramanian2016centromerelocalizationand pages 1-2) | Predicted Yippee/Mis18/Cereblon-like β-tent fold with zinc-binding CXXC-type motifs and a cradle-shaped binding pocket, based on family-level structural studies; Yippee domains often mediate oligomerization and binding functions (lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 1-2, lupas2015thethalidomidebindingdomain pages 9-10, subramanian2016centromerelocalizationand pages 1-2, lupas2015thethalidomidebindingdomain pages 3-5, lupas2015thethalidomidebindingdomain pages 6-8) | Cytoplasm (from UniProt identity provided in prompt); direct localization evidence from retrieved primary literature was limited | Best-supported direct yeast function is required for long-term stationary-phase survival/quiescence maintenance; MOH1 was identified as a stationary-phase-essential gene. More generally, its family context suggests a small conserved regulatory/adaptor protein rather than an enzyme or transporter. The “pro-apoptotic” annotation is consistent with later characterization and with apoptosis-associated functions of YPEL family orthologs, but mechanism-level evidence in S. cerevisiae was limited in retrievable papers (martinez2004genomicanalysisof pages 8-9, martinez2004genomicanalysisof pages 9-10, blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3) | Human YPEL family proteins (YPEL1–YPEL5) are the closest family counterparts. YPEL3 is a p53-inducible, tumor-suppressive, apoptosis/senescence-associated yippee-like protein; family members are evolutionarily conserved and linked to development and stress responses (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3, blancosanchez2020yippeelike3 pages 1-2, OpenTargets Search: -YPEL1,YPEL2,YPEL3,YPEL4,YPEL5) | In S. cerevisiae, moh1Δ showed about 10-fold loss of viability after 16 days in stationary phase at 37°C, identifying MOH1 as a stationary-phase-essential gene; notably, it was among SP-essential genes not required for growth on nonfermentable carbon sources, suggesting a specific role in persistence/quiescence rather than generic respiratory deficiency (martinez2004genomicanalysisof pages 7-8, martinez2004genomicanalysisof pages 8-9, martinez2004genomicanalysisof pages 9-10) |
| Additional comparative evidence relevant to MOH1 interpretation | — | Fungal / metazoan comparators | In Candida glabrata, a MOH1 Y5H variant arose during echinocandin-resistance evolution but did not confer resistance when tested, implying MOH1 may be stress-responsive without being a primary resistance determinant (singhbabak2012globalanalysisof pages 4-5, singhbabak2012globalanalysisof pages 6-8) | Conserved yippee-like proteins in fungi and animals | Related Yippee domains in Mis18 form zinc-stabilized β-sheet structures and mediate homo-/hetero-oligomerization required for centromere function; FAM72 yippee/Mis18 domains were recently implicated in DNA maintenance and replication-stress biology, illustrating broader functional versatility of the fold (subramanian2016centromerelocalizationand pages 8-9, thamkachy2024structuralbasisfor pages 3-4, schou2024exploringthestructural pages 10-11, subramanian2016centromerelocalizationand pages 1-2, thamkachy2024structuralbasisfor pages 1-3) | YPEL3 localization in vertebrates is dynamic across nucleus, perinuclear structures, and near centrosomes during mitosis, underscoring that family members can act as mobile regulatory proteins rather than fixed metabolic enzymes (blancosanchez2020yippeelike3 pages 2-3) | Together, current evidence supports MOH1 as a small conserved yippee-family regulatory protein involved in stress survival and likely cell-death-related signaling, but its precise biochemical activity in budding yeast remains unresolved in the retrievable literature (martinez2004genomicanalysisof pages 8-9, martinez2004genomicanalysisof pages 9-10, lupas2015thethalidomidebindingdomain pages 5-6, lupas2015thethalidomidebindingdomain pages 8-9) | YPEL proteins provide the strongest orthology-based functional clues for apoptosis/senescence; Open Targets also links some YPEL genes to human disease phenotypes, though these associations are indirect for yeast MOH1 (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3, OpenTargets Search: -YPEL1,YPEL2,YPEL3,YPEL4,YPEL5) | Comparative evidence strengthens the interpretation of MOH1 as stress- and survival-related, but does not yet define a substrate, catalytic activity, or dedicated signaling pathway in S. cerevisiae (singhbabak2012globalanalysisof pages 4-5, singhbabak2012globalanalysisof pages 6-8, schou2024exploringthestructural pages 10-11) |
Table: This table summarizes the identity, family assignment, inferred structure, localization, function, orthology, and phenotypes of yeast MOH1/YBL049W using the gathered evidence. It is useful as a compact reference for functional annotation, especially where direct biochemical characterization remains limited.
MOH1 (YBL049W) in S. cerevisiae encodes a small, conserved yippee-family protein whose precise biochemical activity remains to be fully elucidated. The available evidence converges on the following functional interpretation:
MOH1 is not an enzyme, transporter, or structural protein in the classical sense. Rather, it appears to function as a small regulatory or adaptor protein, likely acting through its yippee domain-mediated protein–protein interactions. Its β-tent fold contains a conserved zinc-binding site and a cradle-shaped binding pocket that, in homologous proteins, mediates oligomerization and recruitment of binding partners (lupas2015thethalidomidebindingdomain pages 5-6, subramanian2016centromerelocalizationand pages 1-2).
Its primary biological role is in maintaining cell viability during stationary phase/quiescence, where its deletion causes significant loss of viability under stress conditions (martinez2004genomicanalysisof pages 7-8, martinez2004genomicanalysisof pages 9-10). The pro-apoptotic annotation is consistent with the known functions of its human orthologs (YPEL1-5), which regulate apoptosis, cellular senescence, and cell cycle control (blancosanchez2020yippeelike3 pages 25-26, blancosanchez2020yippeelike3 pages 2-3, martinez2004genomicanalysisof pages 9-10).
The protein localizes to the cytoplasm and its function is likely linked to stress response pathways, potentially involving reactive oxygen species signaling and interactions with the Hsp90 chaperone network (singhbabak2012globalanalysisof pages 4-5). Recent structural and functional work on the broader yippee/Mis18 domain family (2024) has revealed an expanding role for this fold in DNA maintenance and chromatin-associated processes (schou2024exploringthestructural pages 10-11, thamkachy2024structuralbasisfor pages 3-4), which may provide additional avenues for understanding MOH1's specific molecular mechanism in future research.
The precise signaling pathway in which MOH1 functions in S. cerevisiae remains an open question. Its involvement in stationary-phase survival, combined with the apoptotic functions of its orthologs, suggests it may participate in the cellular decision-making process between survival and programmed cell death during nutrient deprivation and stress—a process that is increasingly recognized as having deep evolutionary roots shared between unicellular and multicellular organisms (martinez2004genomicanalysisof pages 8-9, martinez2004genomicanalysisof pages 9-10).
References
(lupas2015thethalidomidebindingdomain pages 1-2): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(lupas2015thethalidomidebindingdomain pages 5-6): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(lupas2015thethalidomidebindingdomain pages 9-10): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(subramanian2016centromerelocalizationand pages 1-2): Lakxmi Subramanian, Bethan Medina‐Pritchard, Rachael Barton, Frances Spiller, Raghavendran Kulasegaran‐Shylini, Guoda Radaviciute, Robin C Allshire, and A Arockia Jeyaprakash. Centromere localization and function of mis18 requires yippee‐like domain‐mediated oligomerization. EMBO reports, 17:496-507, Mar 2016. URL: https://doi.org/10.15252/embr.201541520, doi:10.15252/embr.201541520. This article has 54 citations and is from a highest quality peer-reviewed journal.
(lupas2015thethalidomidebindingdomain pages 3-5): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(lupas2015thethalidomidebindingdomain pages 2-3): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(lupas2015thethalidomidebindingdomain pages 8-9): Andrei N. Lupas, Hongbo Zhu, and Mateusz Korycinski. The thalidomide-binding domain of cereblon defines the cult domain family and is a new member of the β-tent fold. PLoS Computational Biology, 11:e1004023, Jan 2015. URL: https://doi.org/10.1371/journal.pcbi.1004023, doi:10.1371/journal.pcbi.1004023. This article has 61 citations and is from a highest quality peer-reviewed journal.
(martinez2004genomicanalysisof pages 7-8): M. Juanita Martinez, Sushmita Roy, Amanda B. Archuletta, Peter D. Wentzell, Sonia Santa Anna-Arriola, Angelina L. Rodriguez, Anthony D. Aragon, Gabriel A. Quiñones, Chris Allen, and Margaret Werner-Washburne. Genomic analysis of stationary-phase and exit in saccharomyces cerevisiae: gene expression and identification of novel essential genes. Molecular biology of the cell, 15 12:5295-305, Dec 2004. URL: https://doi.org/10.1091/mbc.e03-11-0856, doi:10.1091/mbc.e03-11-0856. This article has 190 citations and is from a domain leading peer-reviewed journal.
(martinez2004genomicanalysisof pages 8-9): M. Juanita Martinez, Sushmita Roy, Amanda B. Archuletta, Peter D. Wentzell, Sonia Santa Anna-Arriola, Angelina L. Rodriguez, Anthony D. Aragon, Gabriel A. Quiñones, Chris Allen, and Margaret Werner-Washburne. Genomic analysis of stationary-phase and exit in saccharomyces cerevisiae: gene expression and identification of novel essential genes. Molecular biology of the cell, 15 12:5295-305, Dec 2004. URL: https://doi.org/10.1091/mbc.e03-11-0856, doi:10.1091/mbc.e03-11-0856. This article has 190 citations and is from a domain leading peer-reviewed journal.
(martinez2004genomicanalysisof pages 9-10): M. Juanita Martinez, Sushmita Roy, Amanda B. Archuletta, Peter D. Wentzell, Sonia Santa Anna-Arriola, Angelina L. Rodriguez, Anthony D. Aragon, Gabriel A. Quiñones, Chris Allen, and Margaret Werner-Washburne. Genomic analysis of stationary-phase and exit in saccharomyces cerevisiae: gene expression and identification of novel essential genes. Molecular biology of the cell, 15 12:5295-305, Dec 2004. URL: https://doi.org/10.1091/mbc.e03-11-0856, doi:10.1091/mbc.e03-11-0856. This article has 190 citations and is from a domain leading peer-reviewed journal.
(blancosanchez2020yippeelike3 pages 25-26): Bernardo Blanco-Sánchez, Aurélie Clément, Sara J. Stednitz, Jennifer Kyle, Judy L. Peirce, Marcie McFadden, Jeremy Wegner, Jennifer B. Phillips, Ellen Macnamara, Yan Huang, David R. Adams, Camilo Toro, William A. Gahl, May Christine V. Malicdan, Cynthia J. Tifft, Erika M. Zink, Kent J. Bloodsworth, Kelly G. Stratton, David M. Koeller, Thomas O. Metz, Philip Washbourne, and Monte Westerfield. Yippee like 3 (ypel3) is a novel gene required for myelinating and perineurial glia development. PLOS Genetics, 16:e1008841, Jun 2020. URL: https://doi.org/10.1371/journal.pgen.1008841, doi:10.1371/journal.pgen.1008841. This article has 28 citations and is from a domain leading peer-reviewed journal.
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(blancosanchez2020yippeelike3 pages 1-2): Bernardo Blanco-Sánchez, Aurélie Clément, Sara J. Stednitz, Jennifer Kyle, Judy L. Peirce, Marcie McFadden, Jeremy Wegner, Jennifer B. Phillips, Ellen Macnamara, Yan Huang, David R. Adams, Camilo Toro, William A. Gahl, May Christine V. Malicdan, Cynthia J. Tifft, Erika M. Zink, Kent J. Bloodsworth, Kelly G. Stratton, David M. Koeller, Thomas O. Metz, Philip Washbourne, and Monte Westerfield. Yippee like 3 (ypel3) is a novel gene required for myelinating and perineurial glia development. PLOS Genetics, 16:e1008841, Jun 2020. URL: https://doi.org/10.1371/journal.pgen.1008841, doi:10.1371/journal.pgen.1008841. This article has 28 citations and is from a domain leading peer-reviewed journal.
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