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Journal articles on the topic 'Microproteins'

Author: Grafiati

Published: 11 March 2023

Last updated: 25 May 2024

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1

Bhati, Kaushal Kumar, Valdeko Kruusvee, Daniel Straub, Anil Kumar Nalini Chandran, Ki-Hong Jung, and Stephan Wenkel. "Global Analysis of Cereal microProteins Suggests Diverse Roles in Crop Development and Environmental Adaptation." G3: Genes|Genomes|Genetics 10, no. 10 (August 6, 2020): 3709–17. http://dx.doi.org/10.1534/g3.120.400794.

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MicroProteins are a class of small single-domain proteins that post-translationally regulate larger multidomain proteins from which they evolved or which they relate to. They disrupt the normal function of their targets by forming microProtein-target heterodimers through compatible protein-protein interaction (PPI) domains. Recent studies confirm the significance of microProteins in the fine-tuning of plant developmental processes such as shoot apical meristem maintenance and flowering time regulation. While there are a number of well-characterized microProteins in Arabidopsis thaliana, studies from more complex plant genomes are still missing. We have previously developed miPFinder, a software for identifying microProteins from annotated genomes. Here we present an improved version where we have updated the algorithm to increase its accuracy and speed, and used it to analyze five cereal crop genomes – wheat, rice, barley, maize and sorghum. We found 20,064 potential microProteins from a total of 258,029 proteins in these five organisms, of which approximately 2000 are high-confidence, i.e., likely to function as actual microProteins. Gene ontology analysis of these 2000 microProtein candidates revealed their roles in stress, light and growth responses, hormone signaling and transcriptional regulation. Using a recently developed rice gene co-expression database, we analyzed 347 potential rice microProteins that are also conserved in other cereal crops and found over 50 of these rice microProteins to be co-regulated with their identified interaction partners. Overall, our study reveals a rich source of biotechnologically interesting small proteins that regulate fundamental plant processes such a growth and stress response that could be utilized in crop bioengineering.

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2

Martinez, Marion, Marta Hergueta, Pilar Ximénez de Embún, Ana Dueso, David Torrents, Teresa Macarulla, Javier Muñoz, Héctor Peinado, and María Abad. "Abstract C074: Mining the secreted microproteome for novel regulators of PDAC progression." Cancer Research 82, no. 22_Supplement (November 15, 2022): C074. http://dx.doi.org/10.1158/1538-7445.panca22-c074.

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Abstract Recent work has unveiled a hidden microproteome composed by thousands of small proteins named microproteins: they are functional short proteins coded by genomic regions previously considered non-coding, and which had been completely ignored, mainly due to their small size (<100 aminoacids). To date, only a small part of the thousands of microproteins present in our cells have been characterized, and they are key players in fundamental processes such as DNA repair, mRNA splicing or cell metabolism. In cancer, they have been shown to regulate most tumor hallmarks, and present a huge potential for the clinic as diagnostic and prognostic biomarkers as well as therapeutic targets. Interestingly, their small size makes them ideal candidates to be shed in tumor-derived exosomes. PDAC-shed exosomes have been shown to prepare the pre-metastatic niche in the liver, and their presence in the bloodstream can be used as a surrogate marker of metastasis. Herein, we have mined the PDAC exosome-secreted microproteome for novel regulators of tumor progression and metastasis. Using proteogenomics in PDAC patient-derived explants, we have identified 439 microproteins secreted in exosomes by pancreatic tumors. We have selected a set of top microprotein candidates for further characterization by in silico analyses (e.g. phylogenetic conservation, predicted protein stability and localisation, mRNA expression in PDAC, etc). We have confirmed their exosome secretion in PDAC cell lines, and preliminary characterisation of these top candidates has shown that they extrinsically promote PDAC cell growth and invasion in vitro. Together, this work advances our knowledge on the underexplored field of secreted microproteins and provides pioneering evidence of their role in tumor cell communication in PDAC. It may further be a source of novel therapeutic targets and PDAC biomarkers for liquid biopsy in the clinic. Citation Format: Marion Martinez, Marta Hergueta, Pilar Ximénez de Embún, Ana Dueso, David Torrents, Teresa Macarulla, Javier Muñoz, Héctor Peinado, María Abad. Mining the secreted microproteome for novel regulators of PDAC progression [abstract]. In: Proceedings of the AACR Special Conference on Pancreatic Cancer; 2022 Sep 13-16; Boston, MA. Philadelphia (PA): AACR; Cancer Res 2022;82(22 Suppl):Abstract nr C074.

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3

Kumagai, Hiroshi, Brendan Miller, Su-Jeong Kim, Naphada Leelaprachakul, Naoki Kikuchi, Kelvin Yen, and Pinchas Cohen. "Novel Insights into Mitochondrial DNA: Mitochondrial Microproteins and mtDNA Variants Modulate Athletic Performance and Age-Related Diseases." Genes 14, no. 2 (January 21, 2023): 286. http://dx.doi.org/10.3390/genes14020286.

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Sports genetics research began in the late 1990s and over 200 variants have been reported as athletic performance- and sports injuries-related genetic polymorphisms. Genetic polymorphisms in the α-actinin-3 (ACTN3) and angiotensin-converting enzyme (ACE) genes are well-established for athletic performance, while collagen-, inflammation-, and estrogen-related genetic polymorphisms are reported as genetic markers for sports injuries. Although the Human Genome Project was completed in the early 2000s, recent studies have discovered previously unannotated microproteins encoded in small open reading frames. Mitochondrial microproteins (also called mitochondrial-derived peptides) are encoded in the mtDNA, and ten mitochondrial microproteins, such as humanin, MOTS-c (mitochondrial ORF of the 12S rRNA type-c), SHLPs 1–6 (small humanin-like peptides 1 to 6), SHMOOSE (Small Human Mitochondrial ORF Over SErine tRNA), and Gau (gene antisense ubiquitous in mtDNAs) have been identified to date. Some of those microproteins have crucial roles in human biology by regulating mitochondrial function, and those, including those to be discovered in the future, could contribute to a better understanding of human biology. This review describes a basic concept of mitochondrial microproteins and discusses recent findings about the potential roles of mitochondrial microproteins in athletic performance as well as age-related diseases.

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4

Celia Henry Arnaud, special to C&EN. "Microproteins, macro impact." C&EN Global Enterprise 101, no. 19 (June 12, 2023): 13–15. http://dx.doi.org/10.1021/cen-10119-feature1.

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5

Chen, Jin, Andreas-David Brunner, J. Zachery Cogan, James K. Nuñez, Alexander P. Fields, Britt Adamson, Daniel N. Itzhak, et al. "Pervasive functional translation of noncanonical human open reading frames." Science 367, no. 6482 (March 5, 2020): 1140–46. http://dx.doi.org/10.1126/science.aay0262.

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Ribosome profiling has revealed pervasive but largely uncharacterized translation outside of canonical coding sequences (CDSs). In this work, we exploit a systematic CRISPR-based screening strategy to identify hundreds of noncanonical CDSs that are essential for cellular growth and whose disruption elicits specific, robust transcriptomic and phenotypic changes in human cells. Functional characterization of the encoded microproteins reveals distinct cellular localizations, specific protein binding partners, and hundreds of microproteins that are presented by the human leukocyte antigen system. We find multiple microproteins encoded in upstream open reading frames, which form stable complexes with the main, canonical protein encoded on the same messenger RNA, thereby revealing the use of functional bicistronic operons in mammals. Together, our results point to a family of functional human microproteins that play critical and diverse cellular roles.

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6

de Klein, Niek, Enrico Magnani, Michael Banf, and Seung Yon Rhee. "microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors." International Journal of Genomics 2015 (2015): 1–4. http://dx.doi.org/10.1155/2015/734147.

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An emerging concept in transcriptional regulation is that a class of truncated transcription factors (TFs), called microProteins (miPs), engages in protein-protein interactions with TF complexes and provides feedback controls. A handful of miP examples have been described in the literature but the extent of their prevalence is unclear. Here we present an algorithm that predicts miPs and their target TFs from a sequenced genome. The algorithm is called miP prediction program (miP3), which is implemented in Python. The software will help shed light on the prevalence, biological roles, and evolution of miPs. Moreover, miP3 can be used to predict other types of miP-like proteins that may have evolved from other functional classes such as kinases and receptors. The program is freely available and can be applied to any sequenced genome.

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7

Rodrigues, Vandasue L., Ulla Dolde, Bin Sun, Anko Blaakmeer, Daniel Straub, Tenai Eguen, Esther Botterweg-Paredes, et al. "A microProtein repressor complex in the shoot meristem controls the transition to flowering." Plant Physiology 187, no. 1 (May 20, 2021): 187–202. http://dx.doi.org/10.1093/plphys/kiab235.

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Abstract MicroProteins are potent post-translational regulators. In Arabidopsis (Arabidopsis thaliana), the miP1a/b microProteins delay floral transition by forming a complex with CONSTANS (CO) and the co-repressor protein TOPLESS. To better understand the function of the miP1a microProtein in floral repression, we performed a genetic suppressor screen to identify suppressors of miP1a (sum) function. One mutant, sum1, exhibited strong suppression of the miP1a-induced late-flowering phenotype. Mapping of sum1 identified another allele of the gene encoding the histone H3K4 demethylase JUMONJI14 (JMJ14), which is required for miP1a function. Plants carrying mutations in JMJ14 exhibit an early flowering phenotype that is largely dependent on CO activity, supporting an additional role for CO in the repressive complex. We further investigated whether miP1a function involves chromatin modification, performed whole-genome methylome sequencing studies with plants ectopically expressing miP1a, and identified differentially methylated regions (DMRs). Among these DMRs is the promoter of FLOWERING LOCUS T (FT), the prime target of miP1a that is ectopically methylated in a JMJ14-dependent manner. Moreover, when aberrantly expressed at the shoot apex, CO induces early flowering, but only when JMJ14 is mutated. Detailed analysis of the genetic interaction among CO, JMJ14, miP1a/b, and TPL revealed a potential role for CO as a repressor of flowering in the shoot apical meristem (SAM). Altogether, our results suggest that a repressor complex operates in the SAM, likely to maintain it in an undifferentiated state until leaf-derived florigen signals induce SAM conversion into a floral meristem.

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8

Eguen, Tenai, Daniel Straub, Moritz Graeff, and Stephan Wenkel. "MicroProteins: small size – big impact." Trends in Plant Science 20, no. 8 (August 2015): 477–82. http://dx.doi.org/10.1016/j.tplants.2015.05.011.

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9

Hong, Shin-Young, Bin Sun, Daniel Straub, Anko Blaakmeer, Lorenzo Mineri, Jonas Koch, Henrik Brinch-Pedersen, et al. "Heterologous microProtein expression identifies LITTLE NINJA, a dominant regulator of jasmonic acid signaling." Proceedings of the National Academy of Sciences 117, no. 42 (October 8, 2020): 26197–205. http://dx.doi.org/10.1073/pnas.2005198117.

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MicroProteins are small, often single-domain proteins that are sequence-related to larger, often multidomain proteins. Here, we used a combination of comparative genomics and heterologous synthetic misexpression to isolate functional cereal microProtein regulators. Our approach identified LITTLE NINJA (LNJ), a microProtein that acts as a modulator of jasmonic acid (JA) signaling. Ectopic expression ofLNJinArabidopsisresulted in stunted plants that resembled the decupleJAZ(jazD) mutant. In fact, comparing the transcriptomes of transgenicLNJoverexpressor plants andjazDrevealed a large overlap of deregulated genes, suggesting that ectopicLNJexpression altered JA signaling. Transgenic Brachypodium plants with elevatedLNJexpression levels showed deregulation of JA signaling as well and displayed reduced growth and enhanced production of side shoots (tiller). This tillering effect was transferable between grass species, and overexpression ofLNJin barley and rice caused similar traits. We used a clustered regularly interspaced short palindromic repeats (CRISPR) approach and created a LNJ-like protein inArabidopsisby deleting parts of the coding sentence of theAFP2gene that encodes a NINJA-domain protein. Theseafp2-crisprmutants were also stunted in size and resembledjazD. Thus, similar genome-engineering approaches can be exploited as a future tool to create LNJ proteins and produce cereals with altered architectures.

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10

Wu, Qingqing, Kunyan Kuang, Mohan Lyu, Yan Zhao, Yue Li, Jing Li, Ying Pan, Hui Shi, and Shangwei Zhong. "Allosteric deactivation of PIFs and EIN3 by microproteins in light control of plant development." Proceedings of the National Academy of Sciences 117, no. 31 (July 21, 2020): 18858–68. http://dx.doi.org/10.1073/pnas.2002313117.

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Buried seedlings undergo dramatic developmental transitions when they emerge from soil into sunlight. As central transcription factors suppressing light responses, PHYTOCHROME-INTERACTING FACTORs (PIFs) and ETHYLENE-INSENSITIVE 3 (EIN3) actively function in darkness and must be promptly repressed upon light to initiate deetiolation. Microproteins are evolutionarily conserved small single-domain proteins that act as posttranslational regulators in eukaryotes. Although hundreds to thousands of microproteins are predicted to exist in plants, their target molecules, biological roles, and mechanisms of action remain largely unknown. Here, we show that two microproteins, miP1a and miP1b (miP1a/b), are robustly stimulated in the dark-to-light transition.miP1a/bare primarily expressed in cotyledons and hypocotyl, exhibiting tissue-specific patterns similar to those ofPIFs andEIN3. We demonstrate that PIFs and EIN3 assemble functional oligomers by self-interaction, while miP1a/b directly interact with and disrupt the oligomerization of PIFs and EIN3 by forming nonfunctional protein complexes. As a result, the DNA binding capacity and transcriptional activity of PIFs and EIN3 are predominantly suppressed. These biochemical findings are further supported by genetic evidence. miP1a/b positively regulate photomorphogenic development, and constitutively expressingmiP1a/brescues the delayed apical hook unfolding and cotyledon development of plants overexpressingPIFs andEIN3. Our study reveals that microproteins provide a temporal and negative control of the master transcription factors' oligomerization to achieve timely developmental transitions upon environmental changes.

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11

Bonilauri, Bernardo, Fabiola Barbieri Holetz, and Bruno Dallagiovanna. "Long Non-Coding RNAs Associated with Ribosomes in Human Adipose-Derived Stem Cells: From RNAs to Microproteins." Biomolecules 11, no. 11 (November 11, 2021): 1673. http://dx.doi.org/10.3390/biom11111673.

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Ribosome profiling reveals the translational dynamics of mRNAs by capturing a ribosomal footprint snapshot. Growing evidence shows that several long non-coding RNAs (lncRNAs) contain small open reading frames (smORFs) that are translated into functional peptides. The difficulty in identifying bona-fide translated smORFs is a constant challenge in experimental and bioinformatics fields due to their unconventional characteristics. This motivated us to isolate human adipose-derived stem cells (hASC) from adipose tissue and perform a ribosome profiling followed by bioinformatics analysis of transcriptome, translatome, and ribosome-protected fragments of lncRNAs. Here, we demonstrated that 222 lncRNAs were associated with the translational machinery in hASC, including the already demonstrated lncRNAs coding microproteins. The ribosomal occupancy of some transcripts was consistent with the translation of smORFs. In conclusion, we were able to identify a subset of 15 lncRNAs containing 35 smORFs that likely encode functional microproteins, including four previously demonstrated smORF-derived microproteins, suggesting a possible dual role of these lncRNAs in hASC self-renewal.

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12

Feller, Stephan. "Microproteins (miPs) – the next big thing." Cell Communication and Signaling 10, no. 1 (2012): 42. http://dx.doi.org/10.1186/1478-811x-10-42.

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13

Staudt, Annica‐Carolin, and Stephan Wenkel. "Regulation of protein function by ‘microProteins’." EMBO reports 12, no. 1 (December 10, 2010): 35–42. http://dx.doi.org/10.1038/embor.2010.196.

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14

Makarewich, Catherine A. "The hidden world of membrane microproteins." Experimental Cell Research 388, no. 2 (March 2020): 111853. http://dx.doi.org/10.1016/j.yexcr.2020.111853.

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15

McLafferty, M. A., R. B. Kent, R. C. Ladner, and W. Markland. "M13 bacteriophage displaying disulfide-constrained microproteins." Gene 128, no. 1 (June 1993): 29–36. http://dx.doi.org/10.1016/0378-1119(93)90149-w.

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16

Lee, Jiwon, Aaron Wacholder, and Anne-Ruxandra Carvunis. "Evolutionary Characterization of the Short Protein SPAAR." Genes 12, no. 12 (November 24, 2021): 1864. http://dx.doi.org/10.3390/genes12121864.

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Microproteins (<100 amino acids) are receiving increasing recognition as important participants in numerous biological processes, but their evolutionary dynamics are poorly understood. SPAAR is a recently discovered microprotein that regulates muscle regeneration and angiogenesis through interactions with conserved signaling pathways. Interestingly, SPAAR does not belong to any known protein family and has known homologs exclusively among placental mammals. This lack of distant homology could be caused by challenges in homology detection of short sequences, or it could indicate a recent de novo emergence from a noncoding sequence. By integrating syntenic alignments and homology searches, we identify SPAAR orthologs in marsupials and monotremes, establishing that SPAAR has existed at least since the emergence of mammals. SPAAR shows substantial primary sequence divergence but retains a conserved protein structure. In primates, we infer two independent evolutionary events leading to the de novo origination of 5′ elongated isoforms of SPAAR from a noncoding sequence and find evidence of adaptive evolution in this extended region. Thus, SPAAR may be of ancient origin, but it appears to be experiencing continual evolutionary innovation in mammals.

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17

Tam, James P., Jiayi Huang, Shining Loo, Yimeng Li, and Antony Kam. "Ginsentide-like Coffeetides Isolated from Coffee Waste Are Cell-Penetrating and Metal-Binding Microproteins." Molecules 28, no. 18 (September 10, 2023): 6556. http://dx.doi.org/10.3390/molecules28186556.

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Coffee processing generates a huge amount of waste that contains many natural products. Here, we report the discovery of a panel of novel cell-penetrating and metal ion-binding microproteins designated coffeetide cC1a–c and cL1–6 from the husk of two popular coffee plants, Coffea canephora and Coffea liberica, respectively. Combining sequence determination and a database search, we show that the prototypic coffeetide cC1a is a 37-residue, eight-cysteine microprotein with a hevein-like cysteine motif, but without a chitin-binding domain. NMR determination of cC1a reveals a compact structure that confers its resistance to heat and proteolytic degradation. Disulfide mapping together with chemical synthesis reveals that cC1a has a ginsentide-like, and not a hevein-like, disulfide connectivity. In addition, transcriptomic analysis showed that the 98-residue micrcoproten-like coffeetide precursor contains a three-domain arrangement, like ginsentide precursors. Molecular modeling, together with experimental validation, revealed a Mg2+ and Fe3+ binding pocket at the N-terminus formed by three glutamic acids. Importantly, cC1a is amphipathic with a continuous stretch of 19 apolar amino acids, which enables its cell penetration to target intracellular proteins, despite being highly negatively charged. Our findings suggest that coffee by-products could provide a source of ginsentide-like bioactive peptides that have the potential to target intracellular proteins.

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18

Sedlov, I. A., and I. A. Fesenko. "Methods for Interactome Analysis of Microproteins Encoded by Small Open Reading Frames." Биоорганическая химия 49, no. 4 (July 1, 2023): 333–47. http://dx.doi.org/10.31857/s0132342323040395.

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Recent studies have shown that small open reading frames (sORFs, 100 codons) can encode peptides or microproteins that perform important functions in prokaryotic and eukaryotic cells. It has been established that sORF translation products are involved in the regulation of many processes, for example, they modulate the activity of the mitochondrial respiratory chain or the functions of muscle cells in mammals. However, the identification and subsequent functional analysis of peptides or microproteins encoded by sORFs is a non-trivial task and requires the use of special approaches. One of the critical steps in functional analysis is identification of protein partners of the peptide under study. This review considers the features of the interactome analysis of short protein molecules and describes the approaches currently used for studies in the field.

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19

Bhati, Kaushal Kumar, Ulla Dolde, and Stephan Wenkel. "MicroProteins: Expanding functions and novel modes of regulation." Molecular Plant 14, no. 5 (May 2021): 705–7. http://dx.doi.org/10.1016/j.molp.2021.01.006.

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20

Wu, Qingqing, Shangwei Zhong, and Hui Shi. "MicroProteins: Dynamic and accurate regulation of protein activity." Journal of Integrative Plant Biology 64, no. 4 (February 28, 2022): 812–20. http://dx.doi.org/10.1111/jipb.13229.

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21

Jiang, Meiqian, Huiqiang Lou, and Wenya Hou. "Microproteins: from behind the scenes to the spotlight." Genome Instability & Disease 2, no. 4 (May 16, 2021): 225–39. http://dx.doi.org/10.1007/s42764-021-00040-3.

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22

Eguen, Tenai, Jorge Gomez Ariza, Vittoria Brambilla, Bin Sun, Kaushal Kumar Bhati, Fabio Fornara, and Stephan Wenkel. "Control of flowering in rice through synthetic microProteins." Journal of Integrative Plant Biology 62, no. 6 (October 16, 2019): 730–36. http://dx.doi.org/10.1111/jipb.12865.

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23

Zlotorynski, Eytan. "The functions of short ORFs and their microproteins." Nature Reviews Molecular Cell Biology 21, no. 5 (March 24, 2020): 252–53. http://dx.doi.org/10.1038/s41580-020-0239-7.

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24

Liang, Chao, Shan Zhang, David Robinson, Matthew Vander Ploeg, Rebecca Wilson, Jiemin Nah, Dale Taylor, et al. "Mitochondrial microproteins link metabolic cues to respiratory chain biogenesis." Cell Reports 40, no. 7 (August 2022): 111204. http://dx.doi.org/10.1016/j.celrep.2022.111204.

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Bonilauri, Bernardo, and Bruno Dallagiovanna. "Microproteins in skeletal muscle: hidden keys in muscle physiology." Journal of Cachexia, Sarcopenia and Muscle 13, no. 1 (November 30, 2021): 100–113. http://dx.doi.org/10.1002/jcsm.12866.

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26

Straub, Daniel, and Stephan Wenkel. "Cross-Species Genome-Wide Identification of Evolutionary Conserved MicroProteins." Genome Biology and Evolution 9, no. 3 (March 2017): 777–89. http://dx.doi.org/10.1093/gbe/evx041.

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Thongyoo, Panumart, Agnes M. Jaulent, Edward W. Tate, and Robin J. Leatherbarrow. "Immobilized Protease-Assisted Synthesis of Engineered Cysteine-Knot Microproteins." ChemBioChem 8, no. 10 (July 9, 2007): 1107–9. http://dx.doi.org/10.1002/cbic.200700187.

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Chothani, Sonia, Lena Ho, Sebastian Schafer, and Owen Rackham. "Discovering microproteins: making the most of ribosome profiling data." RNA Biology 20, no. 1 (November 27, 2023): 943–54. http://dx.doi.org/10.1080/15476286.2023.2279845.

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Dolde, Ulla, Vandasue Rodrigues, Daniel Straub, Kaushal Kumar Bhati, Sukwon Choi, Seong Wook Yang, and Stephan Wenkel. "Synthetic MicroProteins: Versatile Tools for Posttranslational Regulation of Target Proteins." Plant Physiology 176, no. 4 (January 30, 2018): 3136–45. http://dx.doi.org/10.1104/pp.17.01743.

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Gautam, Himanshi, Ashish Sharma, and Prabodh Kumar Trivedi. "Plant microProteins and miPEPs: Small molecules with much bigger roles." Plant Science 326 (January 2023): 111519. http://dx.doi.org/10.1016/j.plantsci.2022.111519.

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Vakirlis, Nikolaos, Zoe Vance, Kate M. Duggan, and Aoife McLysaght. "De novo birth of functional microproteins in the human lineage." Cell Reports 41, no. 12 (December 2022): 111808. http://dx.doi.org/10.1016/j.celrep.2022.111808.

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Li, Bing, Zheng Zhang, and Cuihong Wan. "Identification of Microproteins in Hep3B Cells at Different Cell Cycle Stages." Journal of Proteome Research 21, no. 4 (February 24, 2022): 1052–60. http://dx.doi.org/10.1021/acs.jproteome.1c00926.

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Ma, Jiao, Alan Saghatelian, and Maxim Nikolaievich Shokhirev. "The influence of transcript assembly on the proteogenomics discovery of microproteins." PLOS ONE 13, no. 3 (March 27, 2018): e0194518. http://dx.doi.org/10.1371/journal.pone.0194518.

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BS, Harshitha, Karthik Kumar Manjunath, and Bhargavi HA. "Mysterious microproteins as a novel tool for crop improvement: A review." Pharma Innovation 12, no. 1 (January 1, 2023): 2317–22. http://dx.doi.org/10.22271/tpi.2023.v12.i1z.18331.

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Wang, Zhiwei, Ni Pan, Jiahao Yan, Jian Wan, and Cuihong Wan. "Systematic Identification of Microproteins during the Development of Drosophila melanogaster." Journal of Proteome Research 21, no. 4 (March 1, 2022): 1114–23. http://dx.doi.org/10.1021/acs.jproteome.2c00004.

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Nagel, Raimund. "MicroProteins as the First Step toward a Master Key for Posttranslational Regulation." Plant Physiology 176, no. 4 (April 2018): 2588–89. http://dx.doi.org/10.1104/pp.18.00159.

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Lafranchi, Lorenzo, Dörte Schlesinger, Kyle J. Kimler, and Simon J. Elsässer. "Universal Single-Residue Terminal Labels for Fluorescent Live Cell Imaging of Microproteins." Journal of the American Chemical Society 142, no. 47 (November 11, 2020): 20080–87. http://dx.doi.org/10.1021/jacs.0c09574.

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Bhati, Kaushal Kumar, Anko Blaakmeer, Esther Botterweg Paredes, Ulla Dolde, Tenai Eguen, Shin-Young Hong, Vandasue Rodrigues, Daniel Straub, Bin Sun, and Stephan Wenkel. "Approaches to identify and characterize microProteins and their potential uses in biotechnology." Cellular and Molecular Life Sciences 75, no. 14 (April 18, 2018): 2529–36. http://dx.doi.org/10.1007/s00018-018-2818-8.

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Magnani, Enrico, Niek de Klein, Hye-In Nam, Jung-Gun Kim, Kimberly Pham, Elisa Fiume, Mary Beth Mudgett, and Seung Yon Rhee. "A Comprehensive Analysis of MicroProteins Reveals Their Potentially Widespread Mechanism of Transcriptional Regulation." Plant Physiology 165, no. 1 (March 10, 2014): 149–59. http://dx.doi.org/10.1104/pp.114.235903.

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Cao, Xiongwen, Alexandra Khitun, Zhenkun Na, Daniel G. Dumitrescu, Marcelina Kubica, Elizabeth Olatunji, and Sarah A. Slavoff. "Comparative Proteomic Profiling of Unannotated Microproteins and Alternative Proteins in Human Cell Lines." Journal of Proteome Research 19, no. 8 (May 24, 2020): 3418–26. http://dx.doi.org/10.1021/acs.jproteome.0c00254.

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Tataranni, G., G. Zavagli, R. Farinelli, F. Malacarne, O. Fiocchi, L. Nunzi, P. Scaramuzzo, and R. Scorrano. "Usefulness of the Assessment of Urinary Enzymes and Microproteins in Monitoring Ciclosporin Nephrotoxicity." Nephron 60, no. 3 (1992): 314–18. http://dx.doi.org/10.1159/000186771.

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He, Cuitong, Chenxi Jia, Yao Zhang, and Ping Xu. "Enrichment-Based Proteogenomics Identifies Microproteins, Missing Proteins, and Novel smORFs in Saccharomyces cerevisiae." Journal of Proteome Research 17, no. 7 (June 13, 2018): 2335–44. http://dx.doi.org/10.1021/acs.jproteome.8b00032.

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Le Nguyen, D., A. Heitz, L. Chiche, B. Castro, R. A. Boigegrain, A. Favel, and M. A. Coletti-Previero. "Molecular recognition between serine proteases and new bioactive microproteins with a knotted structure." Biochimie 72, no. 6-7 (June 1990): 431–35. http://dx.doi.org/10.1016/0300-9084(90)90067-q.

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Sedlov, I. A., and I. A. Fesenko. "Methods for Analysis of Interactome of Microproteins Encoded by Short Open Reading Frames." Russian Journal of Bioorganic Chemistry 49, no. 4 (August 2023): 717–30. http://dx.doi.org/10.1134/s1068162023040179.

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Ahmad, Zaki. "A big role for microProteins in preventing premature floral transition in the shoot meristem." Plant Physiology 187, no. 1 (September 1, 2021): 12–13. http://dx.doi.org/10.1093/plphys/kiab320.

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Carraro, M., W. Mancini, M. Artero, F. Stacul, M. Grotto, M. Cova, and L. Faccini. "Dose effect of nitrendipine on urinary enzymes and microproteins following non-ionic radiocontrast administration." Nephrology Dialysis Transplantation 11, no. 3 (March 1, 1996): 444–48. http://dx.doi.org/10.1093/oxfordjournals.ndt.a027309.

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Carraro, M., W. Mancini, M. Artero, F. Stacul, M. Grotto, M. Cova, and L. Faccini. "Dose effect of nitrendipine on urinary enzymes and microproteins following non-ionic radiocontrast administration." Nephrology Dialysis Transplantation 11, no. 3 (March 1996): 444–48. http://dx.doi.org/10.1093/ndt/11.3.444.

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Shcherbatko, Anatoly, Andrea Rossi, Davide Foletti, Guoyun Zhu, Oren Bogin, Meritxell Galindo Casas, Mathias Rickert, et al. "Engineering Highly Potent and Selective Microproteins against Nav1.7 Sodium Channel for Treatment of Pain." Journal of Biological Chemistry 291, no. 27 (April 22, 2016): 13974–86. http://dx.doi.org/10.1074/jbc.m116.725978.

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Burghard, Rainer, Ralf Pallacks, Nader Gordjani, Jekabs U. Leititis, Bernhard J. Hackel�er, and Matthias Brandis. "Microproteins in amniotic fluid as an index of changes in fetal renal function during development." Pediatric Nephrology 1, no. 4 (1987): 574–80. http://dx.doi.org/10.1007/bf00853591.

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Werle, Martin, Thierry Schmitz, Hong-Lei Huang, Alexander Wentzel, Harald Kolmar, and Andreas Bernkop-Schnürch. "The potential of cystine-knot microproteins as novel pharmacophoric scaffolds in oral peptide drug delivery." Journal of Drug Targeting 14, no. 3 (January 2006): 137–46. http://dx.doi.org/10.1080/10611860600648254.

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