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Article ; Online: Tissue-Targeted CRISPR-Cas9-Mediated Genome Editing of Multiple Homeologs in F

Corkins, Mark E / DeLay, Bridget D / Miller, Rachel K

Cold Spring Harbor protocols

2022 Volume 2022, Issue 3

MeSH term(s)	Animals ; CRISPR-Associated Protein 9/genetics ; CRISPR-Cas Systems ; Gene Editing/methods ; RNA, Guide, CRISPR-Cas Systems/genetics ; Xenopus laevis/genetics
Chemical Substances	RNA, Guide, CRISPR-Cas Systems ; CRISPR-Associated Protein 9 (EC 3.1.-)
Language	English
Publishing date	2022-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot107037
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Article ; Online: Aquatic models of human ciliary diseases.

Corkins, Mark E / Krneta-Stankic, Vanja / Kloc, Malgorzata / Miller, Rachel K

Genesis (New York, N.Y. : 2000)

2021 Volume 59, Issue 1-2, Page(s) e23410

Abstract: Cilia are microtubule-based structures that either transmit information into the cell or move fluid outside of the cell. There are many human diseases that arise from malfunctioning cilia. Although mammalian models provide vital insights into the ... ...

Abstract	Cilia are microtubule-based structures that either transmit information into the cell or move fluid outside of the cell. There are many human diseases that arise from malfunctioning cilia. Although mammalian models provide vital insights into the underlying pathology of these diseases, aquatic organisms such as Xenopus and zebrafish provide valuable tools to help screen and dissect out the underlying causes of these diseases. In this review we focus on recent studies that identify or describe different types of human ciliopathies and outline how aquatic organisms have aided our understanding of these diseases.
MeSH term(s)	Animals ; Ciliopathies/genetics ; Ciliopathies/metabolism ; Ciliopathies/pathology ; Disease Models, Animal ; Phenotype ; Xenopus laevis/genetics ; Xenopus laevis/metabolism ; Zebrafish/genetics ; Zebrafish/metabolism
Language	English
Publishing date	2021-01-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2004544-X
ISSN	1526-968X ; 1526-954X
ISSN (online)	1526-968X
ISSN	1526-954X
DOI	10.1002/dvg.23410
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Article ; Online: The Wnt/PCP formin Daam1 drives cell-cell adhesion during nephron development.

Krneta-Stankic, Vanja / Corkins, Mark E / Paulucci-Holthauzen, Adriana / Kloc, Malgorzata / Gladden, Andrew B / Miller, Rachel K

Cell reports

2021 Volume 36, Issue 1, Page(s) 109340

Abstract: E-cadherin junctions facilitate assembly and disassembly of cell contacts that drive development ... Dishevelled-associated activator of morphogenesis 1) in regulating E-cadherin-based intercellular adhesion ... localization of junctional E-cadherin, mediated by Daam1's formin homology domain 2 (FH2). Finally ...

Abstract	E-cadherin junctions facilitate assembly and disassembly of cell contacts that drive development and homeostasis of epithelial tissues. In this study, using Xenopus embryonic kidney and Madin-Darby canine kidney (MDCK) cells, we investigate the role of the Wnt/planar cell polarity (PCP) formin Daam1 (Dishevelled-associated activator of morphogenesis 1) in regulating E-cadherin-based intercellular adhesion. Using live imaging, we show that Daam1 localizes to newly formed cell contacts in the developing nephron. Furthermore, analyses of junctional filamentous actin (F-actin) upon Daam1 depletion indicate decreased microfilament localization and slowed turnover. We also show that Daam1 is necessary for efficient and timely localization of junctional E-cadherin, mediated by Daam1's formin homology domain 2 (FH2). Finally, we establish that Daam1 signaling promotes organized movement of renal cells. This study demonstrates that Daam1 formin junctional activity is critical for epithelial tissue organization.
MeSH term(s)	Actins/metabolism ; Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cadherins/metabolism ; Cell Adhesion ; Dogs ; Embryo, Nonmammalian/metabolism ; Embryo, Nonmammalian/ultrastructure ; Female ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Imaging, Three-Dimensional ; Madin Darby Canine Kidney Cells ; Male ; Nephrons/embryology ; Nephrons/metabolism ; Nephrons/ultrastructure ; Protein Domains ; Protein Transport ; Xenopus Proteins/chemistry ; Xenopus Proteins/metabolism ; Xenopus laevis/embryology
Chemical Substances	Actins ; Adaptor Proteins, Signal Transducing ; Cadherins ; Daam1 protein, Xenopus ; Xenopus Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2021-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.2021.109340
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Article: Identification of Multicolor Fluorescent Probes for Heterogeneous Aβ Deposits in Alzheimer's Disease.

Mukherjee, Abhisek / Al-Lahham, Rabab / Corkins, Mark E / Samanta, Sourav / Schmeichel, Ann M / Singer, Wolfgang / Low, Phillip A / Govindaraju, Thimmaiah / Soto, Claudio

Frontiers in aging neuroscience

2022 Volume 13, Page(s) 802614

Abstract: ... into neurofibrillary tangles (NFTs) are pathological hallmarks of Alzheimer's disease (AD). There is a significant intra- and ...

Abstract	Accumulation of amyloid-beta (Aβ) into amyloid plaques and hyperphosphorylated tau into neurofibrillary tangles (NFTs) are pathological hallmarks of Alzheimer's disease (AD). There is a significant intra- and inter-individual variability in the morphology and conformation of Aβ aggregates, which may account in part for the extensive clinical and pathophysiological heterogeneity observed in AD. In this study, we sought to identify an array of fluorescent dyes to specifically probe Aβ aggregates, in an effort to address their diversity. We screened a small library of fluorescent probes and identified three benzothiazole-coumarin derivatives that stained both vascular and parenchymal Aβ deposits in AD brain sections. The set of these three dyes allowed the visualization of Aβ deposits in three different colors (blue, green and far-red). Importantly, two of these dyes specifically stained Aβ deposits with no apparent staining of hyperphosphorylated tau or α-synuclein deposits. Furthermore, this set of dyes demonstrated differential interactions with distinct types of Aβ deposits present in the same subject. Aβ aggregate-specific dyes identified in this study have the potential to be further developed into Aβ imaging probes for the diagnosis of AD. In addition, the far-red dye we identified in this study may serve as an imaging probe for small animal imaging of Aβ pathology. Finally, these dyes in combination may help us advance our understanding of the relation between the various Aβ deposits and the clinical diversity observed in AD.
Language	English
Publishing date	2022-02-03
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2021.802614
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Article ; Online: A comparative study of cellular diversity between the Xenopus pronephric and mouse metanephric nephron.

Corkins, Mark E / Achieng, MaryAnne / DeLay, Bridget D / Krneta-Stankic, Vanja / Cain, Margo P / Walker, Brandy L / Chen, Jichao / Lindström, Nils O / Miller, Rachel K

Kidney international

2022 Volume 103, Issue 1, Page(s) 77–86

Abstract: The kidney is an essential organ that ensures bodily fluid homeostasis and removes soluble waste products from the organism. Nephrons, the functional units of the kidney, comprise a blood filter, the glomerulus or glomus, and an epithelial tubule that ... ...

Abstract	The kidney is an essential organ that ensures bodily fluid homeostasis and removes soluble waste products from the organism. Nephrons, the functional units of the kidney, comprise a blood filter, the glomerulus or glomus, and an epithelial tubule that processes the filtrate from the blood or coelom and selectively reabsorbs solutes, such as sugars, proteins, ions, and water, leaving waste products to be eliminated in the urine. Genes coding for transporters are segmentally expressed, enabling the nephron to sequentially process the filtrate. The Xenopus embryonic kidney, the pronephros, which consists of a single large nephron, has served as a valuable model to identify genes involved in nephron formation and patterning. Therefore, the developmental patterning program that generates these segments is of great interest. Prior work has defined the gene expression profiles of Xenopus nephron segments via in situ hybridization strategies, but a comprehensive understanding of the cellular makeup of the pronephric kidney remains incomplete. Here, we carried out single-cell mRNA sequencing of the functional Xenopus pronephric nephron and evaluated its cellular composition through comparative analyses with previous Xenopus studies and single-cell mRNA sequencing of the adult mouse kidney. This study reconstructs the cellular makeup of the pronephric kidney and identifies conserved cells, segments, and associated gene expression profiles. Thus, our data highlight significant conservation in podocytes, proximal and distal tubule cells, and divergence in cellular composition underlying the capacity of each nephron to remove wastes in the form of urine, while emphasizing the Xenopus pronephros as a model for physiology and disease.
MeSH term(s)	Animals ; Mice ; Gene Expression Regulation, Developmental ; Kidney/embryology ; Kidney Glomerulus/embryology ; Nephrons/embryology ; RNA, Messenger/genetics ; Xenopus laevis/embryology
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2022-08-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120573-0
ISSN	1523-1755 ; 0085-2538
ISSN (online)	1523-1755
ISSN	0085-2538
DOI	10.1016/j.kint.2022.07.027
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Article ; Online: Zinc transporters belonging to the Cation Diffusion Facilitator (CDF) family have complementary roles in transporting zinc out of the cytosol.

Choi, Sangyong / Hu, Ya-Mei / Corkins, Mark E / Palmer, Amy E / Bird, Amanda J

PLoS genetics

2018 Volume 14, Issue 3, Page(s) e1007262

Abstract: Zinc is an essential trace element that is required for the function of a large number of proteins. As these zinc-binding proteins are found within the cytosol and organelles, all eukaryotes require mechanisms to ensure that zinc is delivered to ... ...

Abstract	Zinc is an essential trace element that is required for the function of a large number of proteins. As these zinc-binding proteins are found within the cytosol and organelles, all eukaryotes require mechanisms to ensure that zinc is delivered to organelles, even under conditions of zinc deficiency. Although many zinc transporters belonging to the Cation Diffusion Facilitator (CDF) families have well characterized roles in transporting zinc into the lumens of intracellular compartments, relatively little is known about the mechanisms that maintain organelle zinc homeostasis. The fission yeast Schizosaccharomyces pombe is a useful model system to study organelle zinc homeostasis as it expresses three CDF family members that transport zinc out of the cytosol into intracellular compartments: Zhf1, Cis4, and Zrg17. Zhf1 transports zinc into the endoplasmic reticulum, and Cis4 and Zrg17 form a heterodimeric complex that transports zinc into the cis-Golgi. Here we have used the high and low affinity ZapCY zinc-responsive FRET sensors to examine cytosolic zinc levels in yeast mutants that lack each of these CDF proteins. We find that deletion of cis4 or zrg17 leads to higher levels of zinc accumulating in the cytosol under conditions of zinc deficiency, whereas deletion of zhf1 results in zinc accumulating in the cytosol when zinc is not limiting. We also show that the expression of cis4, zrg17, and zhf1 is independent of cellular zinc status. Taken together our results suggest that the Cis4/Zrg17 complex is necessary for zinc transport out of the cytosol under conditions of zinc-deficiency, while Zhf1 plays the dominant role in removing zinc from the cytosol when labile zinc is present. We propose that the properties and/or activities of individual CDF family members are fine-tuned to enable cells to control the flux of zinc out of the cytosol over a broad range of environmental zinc stress.
MeSH term(s)	Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Cell Compartmentation ; Cytosol/metabolism ; Fluorescence Resonance Energy Transfer ; Homeostasis ; Ion Transport ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mutation ; Organelles/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Zinc/metabolism
Chemical Substances	Cation Transport Proteins ; Cis4 protein, S pombe ; Membrane Transport Proteins ; Schizosaccharomyces pombe Proteins ; Zhf1 protein, S pombe ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2018-03-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1007262
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Article ; Online: Divergent roles of the Wnt/PCP Formin Daam1 in renal ciliogenesis.

Corkins, Mark E / Krneta-Stankic, Vanja / Kloc, Malgorzata / McCrea, Pierre D / Gladden, Andrew B / Miller, Rachel K

PloS one

2019 Volume 14, Issue 8, Page(s) e0221698

Abstract: Kidneys are composed of numerous ciliated epithelial tubules called nephrons. Each nephron functions to reabsorb nutrients and concentrate waste products into urine. Defects in primary cilia are associated with abnormal formation of nephrons and cyst ... ...

Abstract	Kidneys are composed of numerous ciliated epithelial tubules called nephrons. Each nephron functions to reabsorb nutrients and concentrate waste products into urine. Defects in primary cilia are associated with abnormal formation of nephrons and cyst formation in a wide range of kidney disorders. Previous work in Xenopus laevis and zebrafish embryos established that loss of components that make up the Wnt/PCP pathway, Daam1 and ArhGEF19 (wGEF) perturb kidney tubulogenesis. Dishevelled, which activates both the canonical and non-canonical Wnt/PCP pathway, affect cilia formation in multiciliated cells. In this study, we investigated the role of the noncanoncial Wnt/PCP components Daam1 and ArhGEF19 (wGEF) in renal ciliogenesis utilizing polarized mammalian kidney epithelia cells (MDCKII and IMCD3) and Xenopus laevis embryonic kidney. We demonstrate that knockdown of Daam1 and ArhGEF19 in MDCKII and IMCD3 cells leads to loss of cilia, and Daam1's effect on ciliogenesis is mediated by the formin-activity of Daam1. Moreover, Daam1 co-localizes with the ciliary transport protein Ift88 and is present in cilia. Interestingly, knocking down Daam1 in Xenopus kidney does not lead to loss of cilia. These data suggests a new role for Daam1 in the formation of primary cilia.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Differentiation/genetics ; Cells, Cultured ; Cilia/metabolism ; Ciliopathies/etiology ; Ciliopathies/metabolism ; Ciliopathies/pathology ; Epithelial Cells/metabolism ; Formins ; Gene Knockdown Techniques ; Kidney/cytology ; Phenotype ; Wnt Proteins/metabolism ; Wnt Signaling Pathway ; Xenopus Proteins/genetics ; Xenopus Proteins/metabolism ; Xenopus laevis
Chemical Substances	Adaptor Proteins, Signal Transducing ; Daam1 protein, Xenopus ; Formins ; Wnt Proteins ; Xenopus Proteins
Language	English
Publishing date	2019-08-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0221698
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Article ; Online: The gluconate shunt is an alternative route for directing glucose into the pentose phosphate pathway in fission yeast.

Corkins, Mark E / Wilson, Stevin / Cocuron, Jean-Christophe / Alonso, Ana P / Bird, Amanda J

The Journal of biological chemistry

2017 Volume 292, Issue 33, Page(s) 13823–13832

Abstract: Glycolysis and the pentose phosphate pathway both play a central role in the degradation of glucose in all domains of life. Another metabolic route that can facilitate glucose breakdown is the gluconate shunt. In this shunt glucose dehydrogenase and ... ...

Abstract	Glycolysis and the pentose phosphate pathway both play a central role in the degradation of glucose in all domains of life. Another metabolic route that can facilitate glucose breakdown is the gluconate shunt. In this shunt glucose dehydrogenase and gluconate kinase catalyze the two-step conversion of glucose into the pentose phosphate pathway intermediate 6-phosphogluconate. Despite the presence of these enzymes in many organisms, their only established role is in the production of 6-phosphogluconate for the Entner-Doudoroff pathway. In this report we performed metabolic profiling on a strain of
MeSH term(s)	Energy Metabolism ; Gene Deletion ; Gluconates/metabolism ; Glucose Dehydrogenases/genetics ; Glucose Dehydrogenases/metabolism ; Glucosephosphate Dehydrogenase/genetics ; Glucosephosphate Dehydrogenase/metabolism ; Metabolomics/methods ; Pentose Phosphate Pathway ; Phosphotransferases (Alcohol Group Acceptor)/genetics ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Recombinant Proteins/metabolism ; Schizosaccharomyces/enzymology ; Schizosaccharomyces/growth & development ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Gluconates ; Loz1 protein, S pombe ; Recombinant Proteins ; Schizosaccharomyces pombe Proteins ; Transcription Factors ; Gcd1 protein, S pombe (EC 1.1.1.-) ; Glucose Dehydrogenases (EC 1.1.1.-) ; Glucosephosphate Dehydrogenase (EC 1.1.1.49) ; Zwf1 protein, S pombe (EC 1.1.1.49) ; Idn1 protein, S pombe (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; gluconokinase (EC 2.7.1.12) ; gluconic acid (R4R8J0Q44B)
Language	English
Publishing date	2017-06-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M117.798488
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Article: Food Insecurity and Pediatric Malnutrition Related to Under- and Overweight in the United States: An Evidence Analysis Center Systematic Review.

Spoede, Elizabeth / Corkins, Mark R / Spear, Bonnie A / Becker, Patricia J / Gunnell Bellini, Sarah / Hoy, M Katherine / Piemonte, Tami A / Rozga, Mary

Journal of the Academy of Nutrition and Dietetics

2020 Volume 121, Issue 5, Page(s) 952–978.e4

Abstract: Both food insecurity and malnutrition are associated with adverse health outcomes in the pediatric population. However, the research on the relationship between these factors has been inconsistent, leading to uncertainty regarding whether or how ... ...

Abstract	Both food insecurity and malnutrition are associated with adverse health outcomes in the pediatric population. However, the research on the relationship between these factors has been inconsistent, leading to uncertainty regarding whether or how evaluation of food insecurity should be incorporated into nutrition screening or the nutrition care process. The objective of this systematic review was to determine the association between food insecurity and malnutrition related to undernutrition or overnutrition (defined by anthropometrics) in the pediatric population in the United States. A literature search was conducted using Medline, Embase, and CINAHL databases for studies published from January 2002 through November 2017. A total of 23 studies (19 cross-sectional and 4 prospective cohort studies) met inclusion criteria and were included in qualitative analysis. In 6 studies, there was no overall relationship between food insecurity and underweight. All included studies examined the relationship between food insecurity status and overweight/obesity and results were mixed, with large cross-sectional studies demonstrating a positive relationship between food insecurity and overweight/obesity. There were no clear patterns according to subpopulation. Evidence quality was graded as fair due to heterogeneity in how food insecurity was measured and populations included as well as inconsistency in results. Use of a 2-item food insecurity screening tool may allow for efficient, effective screening of food insecurity in order to identify potential contributors overweight and obesity.
MeSH term(s)	Child ; Child Nutrition Disorders/epidemiology ; Child Nutrition Disorders/etiology ; Cross-Sectional Studies ; Female ; Food Insecurity ; Humans ; Male ; Mass Screening ; Nutrition Assessment ; Pediatric Obesity/epidemiology ; Pediatric Obesity/etiology ; Prospective Studies ; Qualitative Research ; Thinness/epidemiology ; Thinness/etiology ; United States/epidemiology
Language	English
Publishing date	2020-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Systematic Review
ZDB-ID	2646718-5
ISSN	2212-2672
ISSN	2212-2672
DOI	10.1016/j.jand.2020.03.009
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Article ; Online: The double zinc finger domain and adjacent accessory domain from the transcription factor loss of zinc sensing 1 (loz1) are necessary for DNA binding and zinc sensing.

Ehrensberger, Kate M / Corkins, Mark E / Choi, Sangyong / Bird, Amanda J

The Journal of biological chemistry

2014 Volume 289, Issue 26, Page(s) 18087–18096

Abstract: The Loz1 transcription factor from Schizosaccharomyces pombe plays an essential role in zinc homeostasis by repressing target gene expression in zinc-replete cells. To determine how Loz1 function is regulated by zinc, we employed a genetic screen to ... ...

Abstract	The Loz1 transcription factor from Schizosaccharomyces pombe plays an essential role in zinc homeostasis by repressing target gene expression in zinc-replete cells. To determine how Loz1 function is regulated by zinc, we employed a genetic screen to isolate mutants with impaired zinc-dependent gene expression and analyzed Loz1 protein truncations to map a minimal zinc-responsive domain. In the screen, we isolated 36 new loz1 alleles. 27 of these alleles contained mutations resulting in the truncation of the Loz1 protein. The remaining nine alleles contained point mutations leading to an amino acid substitution within a C-terminal double zinc finger domain. Further analysis of two of these substitutions revealed that they disrupted Loz1 DNA activity in vitro. By analyzing Loz1 protein truncations, we found that the last 96 amino acids of Loz1 was the smallest region that was able to confer partial zinc-dependent repression in vivo. This 96-amino acid region contains the double zinc finger domain and an accessory domain that enhances DNA binding. These results were further supported by the findings that MtfA, a transcription factor from Aspergillus nidulans that contains a related double zinc finger, is unable to complement loz1Δ, whereas a chimera of MtfA containing the Loz1 accessory domain is able to complement loz1Δ. Together, our studies indicate that the double zinc finger domain and adjacent accessory domain preceding zinc finger 1 are necessary for DNA binding and zinc-dependent repression.
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; DNA, Fungal/genetics ; DNA, Fungal/metabolism ; Down-Regulation ; Gene Expression Regulation, Fungal ; Molecular Sequence Data ; Protein Structure, Tertiary ; Schizosaccharomyces/chemistry ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Zinc/metabolism ; Zinc Fingers
Chemical Substances	DNA, Fungal ; Loz1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Transcription Factors ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2014-05-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M114.551333
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