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Article ; Online: Overexpression of JNK-associated leucine zipper protein induces chromosomal instability through interaction with dynein light intermediate chain 1.

Suzuki, Ryusuke / Kanemaki, Masato T / Suzuki, Takeshi / Yoshioka, Katsuji

Genes to cells : devoted to molecular & cellular mechanisms

2023 Volume 29, Issue 1, Page(s) 39–51

Abstract: The c-Jun N-terminal kinase-associated leucine zipper protein (JLP), a scaffold protein of mitogen-activated protein kinase signaling pathways, is a multifunctional protein involved in a variety of cellular processes. It has been reported that JLP is ... ...

Abstract	The c-Jun N-terminal kinase-associated leucine zipper protein (JLP), a scaffold protein of mitogen-activated protein kinase signaling pathways, is a multifunctional protein involved in a variety of cellular processes. It has been reported that JLP is overexpressed in various types of cancer and is expected to be a potential therapeutic target. However, whether and how JLP overexpression affects non-transformed cells remain unknown. Here, we aimed to investigate the effect of JLP overexpression on chromosomal stability in human non-transformed cells and the mechanisms involved. We found that aneuploidy was induced in JLP-overexpressed cells. Moreover, we established JLP-inducible cell lines and observed an increased frequency of chromosome missegregation, reduced time from nuclear envelope breakdown to anaphase onset, and decreased levels of the spindle assembly checkpoint (SAC) components at the prometaphase kinetochore in cells overexpressing the wild-type JLP. In contrast, we observed that a point mutant JLP lacking the ability to interact with dynein light intermediate chain 1 (DLIC1) failed to induce chromosomal instability. Our results suggest that overexpression of the wild-type JLP facilitates premature SAC silencing through interaction with DLIC1, leading to aneuploidy. This study provides a novel insight into the mechanism through which JLP overexpression is associated with cancer development and progression.
MeSH term(s)	Humans ; Adaptor Proteins, Signal Transducing/metabolism ; Leucine Zippers ; Dyneins/genetics ; Dyneins/metabolism ; Neoplasms/metabolism ; Chromosomal Instability ; Aneuploidy ; Mitosis
Chemical Substances	Adaptor Proteins, Signal Transducing ; Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2023-11-14
Publishing country	England
Document type	Journal Article
ZDB-ID	1330000-3
ISSN	1365-2443 ; 1356-9597
ISSN (online)	1365-2443
ISSN	1356-9597
DOI	10.1111/gtc.13083
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Article ; Online: Redundant roles of extra-cellular signal-regulated kinase (ERK) 1 and 2 in the G1-S transition and etoposide-induced G2/M checkpoint in HCT116 cells.

Erdenebaatar, Purev / Gunarta, I Ketut / Suzuki, Ryusuke / Odongoo, Ravdandorj / Fujii, Toshihiro / Fukunaga, Rikiro / Kanemaki, Masato T / Yoshioka, Katsuji

Drug discoveries & therapeutics

2023 Volume 17, Issue 1, Page(s) 10–17

Abstract: The extracellular signal-regulated kinase (ERK) 1 and 2 intracellular signaling pathways play key roles in a variety of cellular processes, such as proliferation and differentiation. Dysregulation of ERK1/2 signaling has been implicated in many diseases, ...

Abstract	The extracellular signal-regulated kinase (ERK) 1 and 2 intracellular signaling pathways play key roles in a variety of cellular processes, such as proliferation and differentiation. Dysregulation of ERK1/2 signaling has been implicated in many diseases, including cancer. Although ERK1/2 signaling pathways have been extensively studied, controversy remains as to whether ERK1 and ERK2 have specific or redundant functions. In this study, we examined the functional roles of ERK1 and ERK2 in cell proliferation and cell cycle progression using an auxin-inducible degron system combined with gene knockout technology. We found that ERK1/2 double depletion, but not ERK1 or ERK2 depletion, substantially inhibited the proliferation of HCT116 cells during G1-S transition. We further demonstrated that ERK1/2-double-depleted cells were much more tolerant to etoposide-induced G2/M arrest than ERK1 or ERK2 single-knockout cells. Together, these results strongly suggest the functional redundancy of ERK1 and ERK2 in both the G1-S transition under physiological conditions and the DNA damage-induced G2/M checkpoint. Our findings substantially advance understanding of the ERK1/2 pathways, which could have strong implications for future pharmacological developments.
MeSH term(s)	Humans ; Extracellular Signal-Regulated MAP Kinases ; Etoposide ; HCT116 Cells ; Apoptosis ; G2 Phase Cell Cycle Checkpoints ; Cell Line, Tumor ; Phosphorylation
Chemical Substances	Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; Etoposide (6PLQ3CP4P3)
Language	English
Publishing date	2023-01-14
Publishing country	Japan
Document type	Journal Article
ZDB-ID	2568828-5
ISSN	1881-784X ; 1881-784X
ISSN (online)	1881-784X
ISSN	1881-784X
DOI	10.5582/ddt.2022.01120
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Article ; Online: NF-κB activation is an early event of changes in gene regulation for acquiring drug resistance in human adenocarcinoma PC-9 cells.

Fukuoka, Masashi / Yoshioka, Katsuji / Hohjoh, Hirohiko

PloS one

2018 Volume 13, Issue 8, Page(s) e0201796

Abstract: Gefitinib and erlotinib are epidermal growth factor receptor-tyrosine kinase inhibitors (EGFR-TKIs). Although EGFR-TKIs are effective as anti-cancer drugs, cancer cells sometimes gain tolerance to the drugs. Previous studies suggested that the fibroblast ...

Abstract	Gefitinib and erlotinib are epidermal growth factor receptor-tyrosine kinase inhibitors (EGFR-TKIs). Although EGFR-TKIs are effective as anti-cancer drugs, cancer cells sometimes gain tolerance to the drugs. Previous studies suggested that the fibroblast growth factor receptor (FGFR)-signaling pathway could serve as compensation for the EGFR-signaling pathway inhibited by EGFR-TKIs. Our study further suggested that FGF2, a FGFR ligand, leaked out from naïve cells killed by gefitinib could initiate the FGFR-signaling pathway in surviving cells; i.e., altruistic survival may occur in naïve cells immediately after EGFR-TKI treatment. Altruistic survival may be temporal, and cells need to change their gene regulation toward gaining resistance to EGFR-TKIs. Changes in such gene regulation after EGFR-TKI treatment are poorly understood. In this study, we examined early events of such gene regulation changes in human adenocarcinoma PC-9 cells that are capable of changing their nature from susceptibility to resistance to EFGR-TKIs. Our study indicated that activation of nuclear factor-kappa B (NF-κB) occurred in the cells immediately after EGFR-TKI treatment and also by gene silencing against oncogenic EGFR; and, MG132 treatment for inhibiting NF-κB activation affected cell viability. Taken together, our findings (including the previous study) suggest that altruistic survival and NF-κB activation might be vital for initiating the acquisition of EGFR-TKI resistance.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/metabolism ; Cell Line, Tumor ; Cell Survival/drug effects ; Cell Survival/physiology ; Drug Resistance, Neoplasm/physiology ; Epidermal Growth Factor/antagonists & inhibitors ; ErbB Receptors/antagonists & inhibitors ; ErbB Receptors/genetics ; ErbB Receptors/metabolism ; Fibroblast Growth Factor 2/metabolism ; Gene Expression Regulation, Neoplastic/drug effects ; Gene Expression Regulation, Neoplastic/physiology ; Gene Silencing ; Humans ; NF-kappa B/metabolism ; Protein Kinase Inhibitors/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA Interference ; Time Factors
Chemical Substances	Antineoplastic Agents ; NF-kappa B ; Protein Kinase Inhibitors ; Fibroblast Growth Factor 2 (103107-01-3) ; Epidermal Growth Factor (62229-50-9) ; EGFR protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2018-08-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0201796
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Article ; Online: Functional role of c-Jun NH

Suzuki, Ryusuke / Gunarta, I Ketut / Boldbaatar, Jambaldorj / Erdenebaatar, Purev / Odongoo, Ravdandorj / Yoshioka, Katsuji

Drug discoveries & therapeutics

2020 Volume 14, Issue 1, Page(s) 35–41

Abstract: Lysosomes are involved in many cellular functions, and in turn lysosomal dysfunction underlies a variety of diseases, including cancer and neurodegenerative diseases. Lysosomes are distributed broadly in the cytoplasm and can move throughout the cell in ... ...

Abstract	Lysosomes are involved in many cellular functions, and in turn lysosomal dysfunction underlies a variety of diseases, including cancer and neurodegenerative diseases. Lysosomes are distributed broadly in the cytoplasm and can move throughout the cell in kinesin- and dynein-dependent manners. Although many mechanisms of lysosomal transport have been reported, how lysosomal transport is regulated has yet to be fully elucidated. In this study we analyzed c-Jun NH
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Autophagy ; Dynactin Complex/metabolism ; Humans ; Kinesin/metabolism ; Lysosomes/metabolism ; Mitogen-Activated Protein Kinase 9/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; DCTN1 protein, human ; Dynactin Complex ; SPAG9 protein, human ; Mitogen-Activated Protein Kinase 9 (EC 2.7.1.24) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2020-02-05
Publishing country	Japan
Document type	Journal Article
ISSN	1881-784X
ISSN (online)	1881-784X
DOI	10.5582/ddt.2020.01001
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Article: Scaffold proteins in mammalian MAP kinase cascades.

Yoshioka, Katsuji

Journal of biochemistry

2004 Volume 135, Issue 6, Page(s) 657–661

Abstract: The mitogen-activated protein kinase (MAPK) signaling pathway, which is conserved from yeast to humans, is activated in response to a variety of extra- and intracellular stimuli, and plays key roles in multiple cellular processes, including proliferation, ...

Abstract	The mitogen-activated protein kinase (MAPK) signaling pathway, which is conserved from yeast to humans, is activated in response to a variety of extra- and intracellular stimuli, and plays key roles in multiple cellular processes, including proliferation, differentiation, and apoptosis. The MAPK pathway transmits its signal through the sequential phosphorylation of MAPK kinase kinase to MAPK kinase to MAPK. Specific and efficient activation of the MAPK cascades is crucial for proper cellular responses to stimuli. As shown in yeast, the mammalian MAPK signaling system may also employ scaffold proteins, in part, to organize the MAPK signaling components into functional MAPK modules, thereby enabling the efficient activation of specific MAPK pathways. This review article describes recent advances in the study of potential mammalian scaffold proteins that may help us understand the complex regulation, including the spatial and temporal control, of the mammalian MAPK signaling pathways.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Humans ; MAP Kinase Signaling System/physiology ; Mitogen-Activated Protein Kinases/metabolism ; Nuclear Matrix-Associated Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Nuclear Matrix-Associated Proteins ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2004-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvh079
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Article ; Online: Neighbors' death is required for surviving human adenocarcinoma PC-9 cells in an early stage of gefitinib treatment.

Takahashi, Masaki / Fukuoka, Masashi / Yoshioka, Katsuji / Hohjoh, Hirohiko

Biochemical and biophysical research communications

2016 Volume 479, Issue 2, Page(s) 393–397

Abstract: Acquired drug resistance is a major problem in chemotherapy, and understanding of the mechanism, by which naïve cells defend themselves from drugs when the cells exposed to the drugs for the first time, may provide a solution of the problem. Gefitinib is ...

Abstract	Acquired drug resistance is a major problem in chemotherapy, and understanding of the mechanism, by which naïve cells defend themselves from drugs when the cells exposed to the drugs for the first time, may provide a solution of the problem. Gefitinib is an epidermal growth factor receptor (EGFR)-tyrosine kinase inhibitor, and used as an anticancer drug; however, gefitinib treatment may sometimes lead cancer cells gradually into a gefitinib-tolerance. Here we describe that human adenocarcinoma PC-9 cells even under the presence of gefitinib were able to survive by activating another signaling pathway involving fibroblast growth factor receptor (FGFR) and its signaling molecule, FGF2; and further suggest that the FGF2 for initiating the pathway might be supplied from neighboring cells which were killed by gefitinib, i.e., the survival might be founded on neighbors' sacrifice in an early stage of gefitinib treatment. Our findings suggested that whether cells had a chance to encounter to survival factors such as FGF2 soon after gefitinib treatment might be an important crossroads for the cells for survival and for gaining a gefitinib tolerance.
MeSH term(s)	Adenocarcinoma/pathology ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/pathology ; Cell Death ; Cell Line, Tumor ; Cell Survival ; Dose-Response Relationship, Drug ; Drug Resistance, Neoplasm ; Fibroblast Growth Factor 2/metabolism ; Gene Expression Profiling ; Humans ; Lung Neoplasms/drug therapy ; Lung Neoplasms/pathology ; Quinazolines/pharmacology ; Receptor, Epidermal Growth Factor/metabolism ; Receptors, Fibroblast Growth Factor/metabolism ; Signal Transduction ; Treatment Outcome
Chemical Substances	Quinazolines ; Receptors, Fibroblast Growth Factor ; Fibroblast Growth Factor 2 (103107-01-3) ; Receptor, Epidermal Growth Factor (EC 2.7.10.1) ; gefitinib (S65743JHBS)
Language	English
Publishing date	2016-10-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.09.092
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Zs.A 116: Show issues

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Article ; Online: Protective role of c-Jun NH

Boldbaatar, Jambaldorj / Gunarta, I Ketut / Suzuki, Ryusuke / Erdenebaatar, Purev / Davaakhuu, Gantulga / Hohjoh, Hirohiko / Yoshioka, Katsuji

Biochemical and biophysical research communications

2019 Volume 522, Issue 3, Page(s) 697–703

Abstract: Previous studies have established the antitumor activity of curcumin, a major component of turmeric. Increasing evidence indicates that curcumin induces autophagy, the activation of mitogen-activated protein kinase (MAPK) intracellular signaling pathways, ...

Abstract	Previous studies have established the antitumor activity of curcumin, a major component of turmeric. Increasing evidence indicates that curcumin induces autophagy, the activation of mitogen-activated protein kinase (MAPK) intracellular signaling pathways, and reactive oxygen species (ROS)-mediated cell death. The c-Jun NH
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Antineoplastic Agents/pharmacology ; Autophagy/drug effects ; Cell Death/drug effects ; Cell Line, Tumor ; Curcumin/pharmacology ; Humans ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Reactive Oxygen Species/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antineoplastic Agents ; Reactive Oxygen Species ; SPAG9 protein, human ; Curcumin (IT942ZTH98)
Language	English
Publishing date	2019-11-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.11.154
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Article ; Online: c-Jun NH

Gunarta, I Ketut / Yuliana, Dewi / Erdenebaatar, Purev / Kishi, Yuhei / Boldbaatar, Jambaldorj / Suzuki, Ryusuke / Odongoo, Ravdandorj / Davaakhuu, Gantulga / Hohjoh, Hirohiko / Yoshioka, Katsuji

Drug discoveries & therapeutics

2021 Volume 15, Issue 2, Page(s) 66–72

Abstract: Curcumin, a major component of turmeric, is known to exhibit multiple biological functions including antitumor activity. We previously reported that the mitogen-activated protein kinase (MAPK) scaffold protein c-Jun ... ...

Abstract	Curcumin, a major component of turmeric, is known to exhibit multiple biological functions including antitumor activity. We previously reported that the mitogen-activated protein kinase (MAPK) scaffold protein c-Jun NH
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Signal Transducing/pharmacology ; Antineoplastic Agents/adverse effects ; Antineoplastic Agents/pharmacology ; Autophagy/drug effects ; Autophagy/genetics ; Cell Culture Techniques ; Cell Death/drug effects ; Cell Death/genetics ; Curcumin/adverse effects ; Curcumin/pharmacology ; Drug Development/methods ; Humans ; Leucine Zippers/genetics ; Lysosomes/drug effects ; Lysosomes/genetics ; MAP Kinase Signaling System/drug effects ; Mitogen-Activated Protein Kinase 9/metabolism ; Mitogen-Activated Protein Kinases/drug effects ; Mitogen-Activated Protein Kinases/metabolism ; Neoplasms/drug therapy ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/pharmacology ; Protective Agents ; Reactive Oxygen Species/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antineoplastic Agents ; MAPK8IP3 protein, human ; Nerve Tissue Proteins ; Protective Agents ; Reactive Oxygen Species ; Mitogen-Activated Protein Kinase 9 (EC 2.7.1.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Curcumin (IT942ZTH98)
Language	English
Publishing date	2021-03-14
Publishing country	Japan
Document type	Journal Article
ZDB-ID	2568828-5
ISSN	1881-784X ; 1881-784X
ISSN (online)	1881-784X
ISSN	1881-784X
DOI	10.5582/ddt.2021.01021
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Article: RNA interference silencing of DRAL affects processing of amyloid precursor protein.

Tanahashi, Hiroshi / Yoshioka, Katsuji

Neuroscience letters

2008 Volume 439, Issue 3, Page(s) 293–297

Abstract: In a previous study, we reported that Alzheimer's disease-associated presenilin-2 interacts with a LIM-domain protein, namely, DRAL/FHL2/SLIM3. In this study, we investigated whether DRAL modifies the metabolism of the amyloid precursor protein (APP). We ...

Abstract	In a previous study, we reported that Alzheimer's disease-associated presenilin-2 interacts with a LIM-domain protein, namely, DRAL/FHL2/SLIM3. In this study, we investigated whether DRAL modifies the metabolism of the amyloid precursor protein (APP). We used small interfering RNA (siRNA) to knockdown DRAL in COS7 and HEK293 cells that stably overexpress APP695. We found that the knockdown was accompanied by a decrease in the amount of secreted alpha-secretase-cleaved APP and the membrane-bound C-terminal fragment C83 and an increase in the amount of secreted beta-amyloid peptide (Abeta) from the cells. We also found that in addition to a disintegrin and metalloprotease (ADAM)-17, DRAL binds to ADAM-10. Thus, DRAL may be involved in the processing of APP through the alpha-secretase pathway.
MeSH term(s)	ADAM Proteins/metabolism ; ADAM10 Protein ; ADAM17 Protein ; Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Cell Line, Transformed ; Cercopithecus aethiops ; Cricetinae ; Homeodomain Proteins/metabolism ; Humans ; LIM-Homeodomain Proteins ; Membrane Proteins/metabolism ; Muscle Proteins/metabolism ; Phorbol Esters/pharmacology ; Prostanoic Acids/metabolism ; RNA, Small Interfering/metabolism ; Transcription Factors/metabolism ; Transfection
Chemical Substances	Amyloid beta-Protein Precursor ; FHL2 protein, human ; Homeodomain Proteins ; LIM-Homeodomain Proteins ; Membrane Proteins ; Muscle Proteins ; Phorbol Esters ; Prostanoic Acids ; RNA, Small Interfering ; Transcription Factors ; phorbol-12-myristate (20839-06-9) ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; ADAM Proteins (EC 3.4.24.-) ; ADAM10 Protein (EC 3.4.24.81) ; ADAM10 protein, human (EC 3.4.24.81) ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86) ; rosaprostol (W4459A2P0J)
Language	English
Publishing date	2008-07-18
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2008.05.039
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Article ; Online: JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis.

Tuvshintugs, Baljinnyam / Sato, Tokiharu / Enkhtuya, Radnaa / Yamashita, Katsumi / Yoshioka, Katsuji

Genes to cells : devoted to molecular & cellular mechanisms

2014 Volume 19, Issue 9, Page(s) 692–703

Abstract: The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding ... ...

Abstract	The ADP-ribosylation factor 6 (ARF6) GTPase is important in cytokinesis and localizes to the midbody. However, the mechanism and regulation of ARF6's recruitment to the midbody are largely unknown. Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2 -terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts. Depleting both JSAP1 and JLP impaired ARF6's localization to the midbody and delayed cytokinesis. These defects were almost completely rescued by wild-type JSAP1 or JLP, but not by JSAP1 or JLP mutants that were unable to interact with active ARF6 or with the kinesin heavy chain (KHC) of kinesin-1. In transfected cells, a constitutively active form of ARF6 associated with KHC only when co-expressed with wild-type JSAP1 or JLP and not with a JSAP1 or JLP mutant. These findings suggest that JSAP1 and JLP, which might be paralogous to each other, are critical and functionally redundant in cytokinesis and control ARF6 localization to the midbody by forming a tripartite complex of JSAP1/JLP, active ARF6, and kinesin-1.
MeSH term(s)	ADP-Ribosylation Factors/metabolism ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cells, Cultured ; Cytokinesis ; Embryo, Mammalian/cytology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Humans ; Kinesin/metabolism ; Mice, Inbred C57BL ; Mice, Knockout ; Mutation ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Protein Multimerization
Chemical Substances	Adaptor Proteins, Signal Transducing ; Mapk8ip3 protein, mouse ; Nerve Tissue Proteins ; Spag9 protein, mouse ; Kinesin (EC 3.6.4.4) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ADP-ribosylation factor 6 (EC 3.6.5.2)
Language	English
Publishing date	2014-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1330000-3
ISSN	1365-2443 ; 1356-9597
ISSN (online)	1365-2443
ISSN	1356-9597
DOI	10.1111/gtc.12170
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