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  1. Artikel ; Online: N-Terminal Arginylation Pull-down Analysis Using the R-Catcher Tool.

    Seo, Taewook / Han, Goeun / Cha-Molstad, Hyunjoo

    Methods in molecular biology (Clifton, N.J.)

    2023  Band 2620, Seite(n) 219–228

    Abstract: Protein arginylation is a unique and under-explored posttranslational modification, which governs many biological functions and the fate of affected proteins. Since ATE1 was discovered in 1963, a central tenet of protein arginylation is that arginylated ... ...

    Abstract Protein arginylation is a unique and under-explored posttranslational modification, which governs many biological functions and the fate of affected proteins. Since ATE1 was discovered in 1963, a central tenet of protein arginylation is that arginylated proteins are destined for proteolysis. However, recent studies have shown that protein arginylation controls not only the half-life of a protein but also various signaling pathways. Here, we introduce a novel molecular tool to elucidate protein arginylation. This new tool, termed R-catcher, is derived from the ZZ domain of p62/sequestosome-1, an N-recognin of the N-degron pathway. The ZZ domain, which has been shown to strongly bind N-terminal arginine, has been modified at specific residues to increase specificity and affinity for N-terminal arginine. R-catcher is a powerful analysis tool allowing researchers to capture the cellular arginylation patterns under various stimuli and conditions, thereby identifying potential therapeutic targets in numerous diseases.
    Mesh-Begriff(e) Aminoacyltransferases/chemistry ; Protein Processing, Post-Translational ; Proteolysis ; Proteins/metabolism ; Arginine/metabolism
    Chemische Substanzen Aminoacyltransferases (EC 2.3.2.-) ; Proteins ; Arginine (94ZLA3W45F)
    Sprache Englisch
    Erscheinungsdatum 2023-04-03
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2942-0_24
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Signaling Pathways Regulated by UBR Box-Containing E3 Ligases.

    Kim, Jung Gi / Shin, Ho-Chul / Seo, Taewook / Nawale, Laxman / Han, Goeun / Kim, Bo Yeon / Kim, Seung Jun / Cha-Molstad, Hyunjoo

    International journal of molecular sciences

    2021  Band 22, Heft 15

    Abstract: UBR box E3 ligases, also called N-recognins, are integral components of the N-degron pathway. Representative N-recognins include UBR1, UBR2, UBR4, and UBR5, and they bind destabilizing N-terminal residues, termed N-degrons. Understanding the molecular ... ...

    Abstract UBR box E3 ligases, also called N-recognins, are integral components of the N-degron pathway. Representative N-recognins include UBR1, UBR2, UBR4, and UBR5, and they bind destabilizing N-terminal residues, termed N-degrons. Understanding the molecular bases of their substrate recognition and the biological impact of the clearance of their substrates on cellular signaling pathways can provide valuable insights into the regulation of these pathways. This review provides an overview of the current knowledge of the binding mechanism of UBR box N-recognin/N-degron interactions and their roles in signaling pathways linked to G-protein-coupled receptors, apoptosis, mitochondrial quality control, inflammation, and DNA damage. The targeting of these UBR box N-recognins can provide potential therapies to treat diseases such as cancer and neurodegenerative diseases.
    Mesh-Begriff(e) Animals ; Apoptosis ; DNA Damage ; Humans ; Inflammation/metabolism ; Inflammation/pathology ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction ; Ubiquitin-Protein Ligases/metabolism
    Chemische Substanzen Receptors, G-Protein-Coupled ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Sprache Englisch
    Erscheinungsdatum 2021-08-03
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22158323
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  3. Artikel ; Online: Amino-terminal arginylation as a degradation signal for selective autophagy.

    Cha-Molstad, Hyunjoo / Kwon, Yong Tae / Kim, Bo Yeon

    BMB reports

    2015  Band 48, Heft 9, Seite(n) 487–488

    Abstract: The ubiquitin-proteasome system and the autophagy lysosome system are the two major protein degradation machineries in eukaryotic cells. These two systems coordinate the removal of unwanted intracellular materials, but the mechanism by which they achieve ...

    Abstract The ubiquitin-proteasome system and the autophagy lysosome system are the two major protein degradation machineries in eukaryotic cells. These two systems coordinate the removal of unwanted intracellular materials, but the mechanism by which they achieve this synchronization is largely unknown. The ubiquitination of substrates serves as a universal degradation signal for both systems. Our study revealed that the amino-terminal Arg, a canonical N-degron in the ubiquitin-proteasome system, also acts as a degradation signal in autophagy. We showed that many ER residents, such as BiP, contain evolutionally conserved arginylation permissive pro-N-degrons, and that certain inducers like dsDNA or proteasome inhibitors cause their translocation into the cytoplasm where they bind misfolded proteins and undergo amino-terminal arginylation by arginyl transferase 1 (ATE1). The amino-terminal Arg of BiP binds p62, which triggers p62 oligomerization and enhances p62-LC3 interaction, thereby stimulating autophagic delivery and degradation of misfolded proteins, promoting cell survival. This study reveals a novel ubiquitin-independent mechanism for the selective autophagy pathway, and provides an insight into how these two major protein degradation pathways communicate in cells to dispose the unwanted proteins.
    Mesh-Begriff(e) Adaptor Proteins, Signal Transducing/metabolism ; Aminoacyltransferases/metabolism ; Arginine/metabolism ; Autophagy/physiology ; Computational Biology ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding ; Protein Processing, Post-Translational ; Proteolysis ; Ubiquitin/metabolism
    Chemische Substanzen Adaptor Proteins, Signal Transducing ; Ubiquitin ; Arginine (94ZLA3W45F) ; Aminoacyltransferases (EC 2.3.2.-) ; arginyltransferase (EC 2.3.2.8) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Sprache Englisch
    Erscheinungsdatum 2015-08-23
    Erscheinungsland Korea (South)
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2410389-5
    ISSN 1976-670X ; 1976-6696
    ISSN (online) 1976-670X
    ISSN 1976-6696
    DOI 10.5483/bmbrep.2015.48.9.176
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Degradation of Polo-like Kinase 1 by the Novel Poly-Arginine N-Degron Pathway PROTAC Regulates Tumor Growth in Nonsmall Cell Lung Cancer.

    Gunasekaran, Pethaiah / Hwang, Yeon Sil / Lee, Gong-Hyeon / Park, Jaehui / Kim, Jung Gi / La, Yeo Kyung / Park, Nam Yeong / Kothandaraman, Rajesh / Yim, Min Su / Choi, Joonhyeok / Kim, Hak Nam / Park, Il Yeong / Lee, Soo Jae / Kim, Mi-Hyun / Cha-Molstad, Hyunjoo / Shin, Song Yub / Ryu, Eun Kyoung / Bang, Jeong Kyu

    Journal of medicinal chemistry

    2023  Band 67, Heft 5, Seite(n) 3307–3320

    Abstract: Polo-like kinase 1 (PLK1), which is crucial in cell cycle regulation, is considered a promising anticancer drug target. Herein, we present the N-degron pathway-based proteolysis targeting chimera (PROTAC) for PLK1 degradation, targeting the Polo-box ... ...

    Abstract Polo-like kinase 1 (PLK1), which is crucial in cell cycle regulation, is considered a promising anticancer drug target. Herein, we present the N-degron pathway-based proteolysis targeting chimera (PROTAC) for PLK1 degradation, targeting the Polo-box domain (PBD). We identified DD-2 as the most potent PROTAC that selectively induces PLK1 degradation in cancer cells, including HeLa and nonsmall cell lung cancer (NSCLC), through the N-degron pathway. DD-2 exhibited significant in vitro anticancer effects, inducing G2/M arrest and apoptosis in HeLa and NSCLC cell lines. DD-2 showed significant tumor growth inhibition in a xenograft mouse model using HeLa and NSCLC cell lines, highlighting its potential in cancer treatment. Furthermore, the combination of DD-2 with tyrosine kinase inhibitor (TKI), osimertinib, effectively suppressed tumor growth in double-mutated H1975 cell lines, emphasizing DD-2's potential in combination cancer therapies. Collectively, this study demonstrates the potential of the N-degron pathway, especially using DD-2, for targeted cancer therapies.
    Mesh-Begriff(e) Humans ; Animals ; Mice ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/pathology ; Cell Cycle Proteins ; Proteolysis Targeting Chimera ; Protein Serine-Threonine Kinases ; Polo-Like Kinase 1 ; Apoptosis ; Degrons ; Cell Line, Tumor ; Lung Neoplasms/drug therapy ; Lung Neoplasms/pathology ; G2 Phase Cell Cycle Checkpoints ; Protein Kinase Inhibitors/pharmacology ; Protein Kinase Inhibitors/therapeutic use
    Chemische Substanzen Cell Cycle Proteins ; Proteolysis Targeting Chimera ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Polo-Like Kinase 1 ; Protein Kinase Inhibitors
    Sprache Englisch
    Erscheinungsdatum 2023-12-17
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.3c01493
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: p62-Induced Cancer-Associated Fibroblast Activation via the Nrf2-ATF6 Pathway Promotes Lung Tumorigenesis.

    Kang, Ji In / Kim, Dong Hyun / Sung, Ki Woon / Shim, Sang Mi / Cha-Molstad, Hyunjoo / Soung, Nak Kyun / Lee, Kyung Ho / Hwang, Joonsung / Lee, Hee Gu / Kwon, Yong Tae / Kim, Bo Yeon

    Cancers

    2021  Band 13, Heft 4

    Abstract: Cancer-associated fibroblasts (CAFs) are important in tumor progression. The autophagy adaptor protein, p62/SQSTM1/Sequestosome-1, is up-regulated in tumors, but down-regulated in CAFs in the early stages of lung adenocarcinoma. We investigated whether ... ...

    Abstract Cancer-associated fibroblasts (CAFs) are important in tumor progression. The autophagy adaptor protein, p62/SQSTM1/Sequestosome-1, is up-regulated in tumors, but down-regulated in CAFs in the early stages of lung adenocarcinoma. We investigated whether p62-induced autophagy might control CAF activation. Under CAF-inducing conditions, like hypoxia or cancer cell co-cultures, p62 ablation or autophagy inhibition with hydroxychloroquine (HCQ) impaired CAF activation and reduced transforming growth factor beta (TGFβ) production, which impeded tumor growth. During CAF activation, p62-induced autophagy up-regulated the expression of the anti-oxidant signaling protein, nuclear factor erythroid 2-related factor 2 (Nrf2), and the ER-stress response regulator, activating transcription factor 6 (ATF6). Genetically or pharmacologically inhibiting the Nrf2-ATF6 pathway totally blocked CAF activation and tumor progression. These results demonstrate that p62 is a key modulator of primary lung adenocarcinoma progression. Thus, targeting the p62-Nrf2 autophagy signaling pathway might be a novel, stroma-focused, cancer prevention and/or treatment strategy.
    Sprache Englisch
    Erscheinungsdatum 2021-02-18
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers13040864
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Phosphorylation of β-catenin Ser60 by polo-like kinase 1 drives the completion of cytokinesis.

    Yu, Ji Eun / Kim, Sun-Ok / Hwang, Jeong-Ah / Hong, Jin Tae / Hwang, Joonsung / Soung, Nak-Kyun / Cha-Molstad, Hyunjoo / Kwon, Yong Tae / Kim, Bo Yeon / Lee, Kyung Ho

    EMBO reports

    2021  Band 22, Heft 12, Seite(n) e51503

    Abstract: β-Catenin is a multifunctional protein and participates in numerous processes required for embryonic development, cell proliferation, and homeostasis through various molecular interactions and signaling pathways. To date, however, there is no direct ... ...

    Abstract β-Catenin is a multifunctional protein and participates in numerous processes required for embryonic development, cell proliferation, and homeostasis through various molecular interactions and signaling pathways. To date, however, there is no direct evidence that β-catenin contributes to cytokinesis. Here, we identify a novel p-S60 epitope on β-catenin generated by Plk1 kinase activity, which can be found at the actomyosin contractile ring of early telophase cells and at the midbody of late telophase cells. Depletion of β-catenin leads to cytokinesis-defective phenotypes, which eventually result in apoptotic cell death. In addition, phosphorylation of β-catenin Ser60 by Plk1 is essential for the recruitment of Ect2 to the midbody, activation of RhoA, and interaction between β-catenin, Plk1, and Ect2. Time-lapse image analysis confirmed the importance of β-catenin phospho-Ser60 in furrow ingression and the completion of cytokinesis. Taken together, we propose that phosphorylation of β-catenin Ser60 by Plk1 in cooperation with Ect2 is essential for the completion of cytokinesis. These findings may provide fundamental knowledge for the research of cytokinesis failure-derived human diseases.
    Mesh-Begriff(e) Actomyosin/metabolism ; Cell Cycle Proteins/metabolism ; Cytokinesis ; HeLa Cells ; Humans ; Phosphorylation ; Protein Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Spindle Apparatus/metabolism ; beta Catenin/metabolism ; Polo-Like Kinase 1
    Chemische Substanzen Cell Cycle Proteins ; ECT2 protein, human ; Proto-Oncogene Proteins ; beta Catenin ; Actomyosin (9013-26-7) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Sprache Englisch
    Erscheinungsdatum 2021-09-29
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.202051503
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Correction to: R-catcher, a potent molecular tool to unveil the arginylome.

    Seo, Taewook / Kim, Jihyo / Shin, Ho-Chul / Kim, Jung Gi / Ju, Shinyeong / Nawale, Laxman / Han, Goeun / Lee, Hye Seon / Bang, Geul / Kim, Jin Young / Bang, Jeong Kyu / Lee, Kyung Ho / Soung, Nak-Kyun / Hwang, Joonsung / Lee, Cheolju / Kim, Seung Jun / Kim, Bo Yeon / Cha-Molstad, Hyunjoo

    Cellular and molecular life sciences : CMLS

    2021  Band 78, Heft 21-22, Seite(n) 7085–7086

    Sprache Englisch
    Erscheinungsdatum 2021-09-27
    Erscheinungsland Switzerland
    Dokumenttyp Published Erratum
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-021-03915-6
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  8. Artikel ; Online: Signaling Pathways Regulated by UBR Box-Containing E3 Ligases

    Jung Gi Kim / Ho-Chul Shin / Taewook Seo / Laxman Nawale / Goeun Han / Bo Yeon Kim / Seung Jun Kim / Hyunjoo Cha-Molstad

    International Journal of Molecular Sciences, Vol 22, Iss 8323, p

    2021  Band 8323

    Abstract: UBR box E3 ligases, also called N-recognins, are integral components of the N-degron pathway. Representative N-recognins include UBR1, UBR2, UBR4, and UBR5, and they bind destabilizing N-terminal residues, termed N-degrons. Understanding the molecular ... ...

    Abstract UBR box E3 ligases, also called N-recognins, are integral components of the N-degron pathway. Representative N-recognins include UBR1, UBR2, UBR4, and UBR5, and they bind destabilizing N-terminal residues, termed N-degrons. Understanding the molecular bases of their substrate recognition and the biological impact of the clearance of their substrates on cellular signaling pathways can provide valuable insights into the regulation of these pathways. This review provides an overview of the current knowledge of the binding mechanism of UBR box N-recognin/N-degron interactions and their roles in signaling pathways linked to G-protein-coupled receptors, apoptosis, mitochondrial quality control, inflammation, and DNA damage. The targeting of these UBR box N-recognins can provide potential therapies to treat diseases such as cancer and neurodegenerative diseases.
    Schlagwörter UBR Box E3 ligases ; N-recognin ; Arg/N-degron pathway ; N-degron ; G-protein signaling ; apoptosis ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Thema/Rubrik (Code) 570
    Sprache Englisch
    Erscheinungsdatum 2021-08-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  9. Artikel ; Online: Wnt3a Stimulation Promotes Primary Ciliogenesis through β-Catenin Phosphorylation-Induced Reorganization of Centriolar Satellites.

    Kyun, Mi-Lang / Kim, Sun-Ok / Lee, Hee Gu / Hwang, Jeong-Ah / Hwang, Joonsung / Soung, Nak-Kyun / Cha-Molstad, Hyunjoo / Lee, Sangku / Kwon, Yong Tae / Kim, Bo Yeon / Lee, Kyung Ho

    Cell reports

    2020  Band 30, Heft 5, Seite(n) 1447–1462.e5

    Abstract: Primary cilium is an antenna-like microtubule-based cellular sensing structure. Abnormal regulation of the dynamic assembly and disassembly cycle of primary cilia is closely related to ciliopathy and cancer. The Wnt signaling pathway plays a major role ... ...

    Abstract Primary cilium is an antenna-like microtubule-based cellular sensing structure. Abnormal regulation of the dynamic assembly and disassembly cycle of primary cilia is closely related to ciliopathy and cancer. The Wnt signaling pathway plays a major role in embryonic development and tissue homeostasis, and defects in Wnt signaling are associated with a variety of human diseases, including cancer. In this study, we provide direct evidence of Wnt3a-induced primary ciliogenesis, which includes a continuous pathway showing that the stimulation of Wnt3a, a canonical Wnt ligand, promotes the generation of β-catenin p-S47 epitope by CK1δ, and these events lead to the reorganization of centriolar satellites resulting in primary ciliogenesis. We have also confirmed the application of our findings in MCF-7/ADR cells, a multidrug-resistant tumor cell model. Thus, our data provide a Wnt3a-induced primary ciliogenesis pathway and may provide a clue on how to overcome multidrug resistance in cancer treatment.
    Mesh-Begriff(e) Amino Acid Sequence ; Animals ; Casein Kinases/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Cilia/metabolism ; Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; Epitopes/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Ligands ; MCF-7 Cells ; Mice ; Organogenesis ; Phosphorylation ; Phosphoserine/metabolism ; Wnt3A Protein/chemistry ; Wnt3A Protein/metabolism ; beta Catenin/metabolism
    Chemische Substanzen Epitopes ; Ligands ; Wnt3A Protein ; beta Catenin ; Phosphoserine (17885-08-4) ; Casein Kinases (EC 2.7.11.1)
    Sprache Englisch
    Erscheinungsdatum 2020-02-05
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2020.01.019
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: R-catcher, a potent molecular tool to unveil the arginylome.

    Seo, Taewook / Kim, Jihyo / Shin, Ho-Chul / Kim, Jung Gi / Ju, Shinyeong / Nawale, Laxman / Han, Goeun / Lee, Hye Seon / Bang, Geul / Kim, Jin Young / Bang, Jeong Kyu / Lee, Kyung Ho / Soung, Nak-Kyun / Hwang, Joonsung / Lee, Cheolju / Kim, Seung Jun / Kim, Bo Yeon / Cha-Molstad, Hyunjoo

    Cellular and molecular life sciences : CMLS

    2021  Band 78, Heft 7, Seite(n) 3725–3741

    Abstract: Protein arginylation is a critical regulator of a variety of biological processes. The ability to uncover the global arginylation pattern and its associated signaling pathways would enable us to identify novel disease targets. Here, we report the ... ...

    Abstract Protein arginylation is a critical regulator of a variety of biological processes. The ability to uncover the global arginylation pattern and its associated signaling pathways would enable us to identify novel disease targets. Here, we report the development of a tool able to capture the N-terminal arginylome. This tool, termed R-catcher, is based on the ZZ domain of p62, which was previously shown to bind N-terminally arginylated proteins. Mutating the ZZ domain enhanced its binding specificity and affinity for Nt-Arg. R-catcher pulldown coupled to LC-MS/MS led to the identification of 59 known and putative arginylated proteins. Among these were a subgroup of novel ATE1-dependent arginylated ER proteins that are linked to diverse biological pathways, including cellular senescence and vesicle-mediated transport as well as diseases, such as Amyotrophic Lateral Sclerosis and Alzheimer's disease. This study presents the first molecular tool that allows the unbiased identification of arginylated proteins, thereby unlocking the arginylome and provide a new path to disease biomarker discovery.
    Mesh-Begriff(e) Aminoacyltransferases/chemistry ; Aminoacyltransferases/genetics ; Aminoacyltransferases/metabolism ; Arginine/chemistry ; Arginine/genetics ; Arginine/metabolism ; Endoplasmic Reticulum/metabolism ; Genetic Vectors/genetics ; HeLa Cells ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Protein Processing, Post-Translational ; Substrate Specificity
    Chemische Substanzen Membrane Proteins ; Arginine (94ZLA3W45F) ; Aminoacyltransferases (EC 2.3.2.-)
    Sprache Englisch
    Erscheinungsdatum 2021-03-09
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-021-03805-x
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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