The Myosin Va Head Domain Binds to the Neurofilament-L Rod and Modulates Endoplasmic Reticulum (ER) Content and Distribution within Axons
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{"title"=>"The myosin Va head domain binds to the neurofilament-L rod and modulates endoplasmic reticulum (ER) content and distribution within axons", "type"=>"journal", "authors"=>[{"first_name"=>"Mala V.", "last_name"=>"Rao", "scopus_author_id"=>"23969348000"}, {"first_name"=>"Panaiyur S.", "last_name"=>"Mohan", "scopus_author_id"=>"7103262656"}, {"first_name"=>"Asok", "last_name"=>"Kumar", "scopus_author_id"=>"55574185885"}, {"first_name"=>"Aidong", "last_name"=>"Yuan", "scopus_author_id"=>"7006862686"}, {"first_name"=>"Lee", "last_name"=>"Montagna", "scopus_author_id"=>"57197506248"}, {"first_name"=>"Jabbar", "last_name"=>"Campbell", "scopus_author_id"=>"56420529300"}, {"last_name"=>"Veeranna", "scopus_author_id"=>"7409937933"}, {"first_name"=>"Enilza M.", "last_name"=>"Espreafico", "scopus_author_id"=>"6604026481"}, {"first_name"=>"Jean P.", "last_name"=>"Julien", "scopus_author_id"=>"35237086200"}, {"first_name"=>"Ralph A.", "last_name"=>"Nixon", "scopus_author_id"=>"7102746041"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-79951891241", "sgr"=>"79951891241", "pui"=>"361318671", "isbn"=>"1932-6203 (Electronic)\r1932-6203 (Linking)", "pmid"=>"21359212", "doi"=>"10.1371/journal.pone.0017087"}, "id"=>"6fb3394b-5b71-31f7-b82e-84652ce33f2d", "abstract"=>"The neurofilament light subunit (NF-L) binds to myosin Va (Myo Va) in neurons but the sites of interaction and functional significance are not clear. We show by deletion analysis that motor domain of Myo Va binds to the NF-L rod domain that forms the NF backbone. Loss of NF-L and Myo Va binding from axons significantly reduces the axonal content of ER, and redistributes ER to the periphery of axon. Our data are consistent with a novel function for NFs as a scaffold in axons for maintaining the content and proper distribution of vesicular organelles, mediated in part by Myo Va. Based on observations that the Myo Va motor domain binds to intermediate filament (IF) proteins of several classes, Myo Va interactions with IFs may serve similar roles in organizing organelle topography in different cell types.", "link"=>"http://www.mendeley.com/research/myosin-va-head-domain-binds-neurofilamentl-rod-modulates-endoplasmic-reticulum-er-content-distributi", "reader_count"=>22, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>2, "Student > Doctoral Student"=>1, "Researcher"=>5, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>1, "Student > Master"=>3, "Other"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>2, "Student > Doctoral Student"=>1, "Researcher"=>5, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>1, "Student > Master"=>3, "Other"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>13, "Medicine and Dentistry"=>3, "Neuroscience"=>1, "Physics and Astronomy"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Neuroscience"=>{"Neuroscience"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>13}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}}, "reader_count_by_country"=>{"Chile"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/798197"], "description"=>"<p>Cytoskeletal (lanes 1&2), and supernatant fractions (lanes 3&4) from WT (lanes 1&3) and NF-L null (lanes 2&4) optic nerves were resolved by SDS-PAGE, transferred to membranes, Ponceau S stained (A), immunoblotted with NF-L (B), Rab-5 (C), Rho B (D), calnexin (E), Synaptophysin (SYP, F), actin (G), tubulin (H), and PSD-95 (I) antibodies. Densitometric quantification of signals from immunoblots in panels C-F indicate significantly reduced amounts of Rab-5 (C), Rho B (D), calnexin (E), Synaptophysin (SYP, F), in NF-L null cytoskeletal fractions compared to controls while actin (G), tubulin (H), and PSD-95 (I) were not decreased in the same fractions. (n = 6 for each genotype of 5–6 month old mice). (J). Total extracts of optic nerves from DLC (dilute lethal control), and DL20J mice were immunoblotted with Myo Va, calnexin, Synaptophysin (SYP), actin, tubulin and PSD-95 antibodies. Quantitation data for calnexin (K), synaptophysin (SYP; L), PSD-95, actin and tubulin is shown in M-O. (P). Morphometric analysis indicate reduced density of ER vesicles in NF-L null and DL20J optic axons (n = 4 for 5–6 month old WT and NF-L null, and 17 day for DL20J and DLC). *p<0.05, and **p<0.01. Error bars represent SEM in all experiments.</p>", "links"=>[], "tags"=>["cellular", "organelles", "reduced", "nf-l", "null", "optic"], "article_id"=>468560, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g004", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NF_network_dependent_association_of_cellular_organelles_is_reduced_in_NF_L_null_optic_axons_/468560", "title"=>"NF-network-dependent association of cellular organelles is reduced in NF-L null optic axons.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:22:40"}
  • {"files"=>["https://ndownloader.figshare.com/files/798030"], "description"=>"<p>(A) Schematic representation of NF-L subunit domains and the deletions. Amino acids are numbered according to <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Lewis1\" target=\"_blank\">[31]</a>. See materials and <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#s2\" target=\"_blank\">methods</a> for construction of NF-L domain deletions. B. The amino-terminal motor domain of Myo Va (41–326) binds to the N-terminal rod domain of NF-L. Myo Va constructs were MBP-tagged while NF-L was myc-tagged. Co-immunoprecipitation of NF-L deletion constructs with Myo Va motor domain (41–326). Myo Va was incubated without NF-L (lane 1), with full length NF-L 1-543 (lane 2); NF-L 1-243 (lane 3); NF-L 94-243 (lane 4) and NF-L 1-93 (lane 5) were immunoprecipitated with Myc antibody (9E10), IPs and Sups (10%) were immunoblotted with anti-MBP or anti-Myc antibodies. The molecular weights of NF-L 1-543, 1-243, 94-243 and 1-93 are 68, 27, 20 and 17-kDa respectively. (C) Magnesium ions potentiate Myo Va and NF-L binding. Myo Va motor domain (41–326) was incubated with NF-L (Full length) and immunoprecipitated with α-Myc antibody. The resulting IPs and 5% of sups were immunoblotted with α-MBP-HRP or α-Myc Abs. Addition of magnesium (5 mM) increased binding (see the graph in 3C) while addition of magnesium and calcium (5 mM) further increased the binding of NF-L to Myo Va (compare lane 6 with 5 and 7). Arrows indicate the position of Myo Va motor domain (41–326) of 75-kDa protein. The *-indicates proteolytic fragments of 41–326 construct generated with incubation of calcium and magnesium in both IP and supernatant fractions in lanes 4&5 while these are seen only in IP fractions of lanes 6&7. (D). Myo Va head domain binds to different IF family members. Cytoskeletal preparations from brain (lane 1), sciatic nerve (lane 2), spinal cord (lane 3), purified NF-L (lane 4), purified actin (lane 5), purified vimentin (lane 6), purified desmin (lane 7) and fractionated keratin from human skin (lane 8) were separated on gels and transferred to membranes. Blot overlay assays were performed on membranes with MBP-Myo Va (41–326) protein and immunoblotted with α-MBP-HRP antibody. Anti-MBP: α-MBP; anti-NF-L: α-NF-L and anti-myc: α-myc. <i>(E) Schematic representation of NF-L and Actin binding sites on Myo Va head domain</i> (1-752). The amino acids are numbered according to <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Mercer1\" target=\"_blank\">[6]</a>. (F). <i>Actin activates Myo Va-ATPase activity while NF-L does not.</i> Myo Va was fractionated from adult mouse brain according to <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Evans1\" target=\"_blank\">[26]</a> (P2 fraction enriched in vesicular Myo Va) and incubated with either actin or NF-L and assayed for ATPase activity. Addition of actin to P2 fraction activated Myo Va-ATPase activity while addition of NF-L did not. *p<0.02. Error bars represent SEM in all experiments.</p>", "links"=>[], "tags"=>["n-terminal", "nf-l", "binds", "myo"], "article_id"=>468388, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g003", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_N_terminal_rod_domain_of_NF_L_binds_to_the_motor_domain_of_Myo_Va_/468388", "title"=>"The N-terminal rod domain of NF-L binds to the motor domain of Myo Va.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:19:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/399071"], "description"=>"<div><p>The neurofilament light subunit (NF-L) binds to myosin Va (Myo Va) in neurons but the sites of interaction and functional significance are not clear. We show by deletion analysis that motor domain of Myo Va binds to the NF-L rod domain that forms the NF backbone. Loss of NF-L and Myo Va binding from axons significantly reduces the axonal content of ER, and redistributes ER to the periphery of axon. Our data are consistent with a novel function for NFs as a scaffold in axons for maintaining the content and proper distribution of vesicular organelles, mediated in part by Myo Va. Based on observations that the Myo Va motor domain binds to intermediate filament (IF) proteins of several classes, Myo Va interactions with IFs may serve similar roles in organizing organelle topography in different cell types.</p> </div>", "links"=>[], "tags"=>["myosin", "va", "binds", "neurofilament-l", "modulates", "endoplasmic", "reticulum", "axons"], "article_id"=>138821, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Myosin_Va_Head_Domain_Binds_to_the_Neurofilament_L_Rod_and_Modulates_Endoplasmic_Reticulum_ER_Content_and_Distribution_within_Axons/138821", "title"=>"The Myosin Va Head Domain Binds to the Neurofilament-L Rod and Modulates Endoplasmic Reticulum (ER) Content and Distribution within Axons", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:27:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/798513"], "description"=>"<p>Tethering of ER, endosomes (En), and other related vesicles to NFs are mediated by Myo Va to maintain normal abundance and distribution of these organelles in the axoplasm. The abundance of NFs in large caliber axons and their intercalation with actin and microtubule systems provides a physical continuity that may facilitate local distribution of organelles along these different filament systems via Myo Va. Loss of Myo Va-NF-L interaction in axons leads to reduced abundance of organelles as they resume transport and are ultimately turned over in the cell body.</p>", "links"=>[], "tags"=>["depicting", "nf-mediated", "anchoring", "organelles", "myo"], "article_id"=>468874, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_model_depicting_NF_mediated_anchoring_and_movement_of_organelles_via_Myo_Va_/468874", "title"=>"A model depicting NF-mediated anchoring and movement of organelles via Myo Va.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:27:54"}
  • {"files"=>["https://ndownloader.figshare.com/files/797881"], "description"=>"<p>(A) The N-terminal motor domain (41–326) of Myo Va binds to NF-L in co-IPs. Myo Va head domain (41–505), N-terminal head domain (41–326), C-terminal head domain (327–505) proteins were incubated with or without NF-L and immunoprecipitated with NF-L antibody (NR-4), IPs and Sups (10%) were immunoblotted with anti-MBP-HRP, and anti-NF-L antibody (NR-4). The immunoreactive bands were detected as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone-0017087-g001\" target=\"_blank\">Fig. 1B</a>. Myo Va head domain (41–505) is 95-kDa, 41-326 is 75-kDa and 327–505 is 52-kDa. (B) The N-terminal domain of Myo Va (41–326) binds to NF-L in blot overlay assays at equimolar concentrations with spinal cord cytoskeletal fractions. Lane 1 Ponceau S stain (Ponc. S.) of SC cytoskeletal fraction, SC cytoskeletal fractions in lane 2 and 3 were incubated with 41–326 and 327–505 of Myo Va head mutants and blot overlay assays were performed as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone-0017087-g001\" target=\"_blank\">Fig. 1C</a>. (C&D) Myo Va head domain (41–505) shows significantly more binding to NF-L in co-IPs (C&D, *-p<0.011) and blot overlay assays (E) compared to neck region (800–881). The MW of 800–881 is 50-kDa. Error bars represent SEM. Myo Va head domain (41–505) and neck region (800–881) were separately incubated with or without NF-L and immunoprecipitated with NF-L antibody (NR-4). IPs and Sups (10%) were immunoblotted with MBP-HRP and NF-L antibodies in panel D. (E) Cytoskeletal fractions from spinal cord (SC, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone-0017087-g002\" target=\"_blank\">Fig. 2E</a>, lanes 1, 3&5) and sciatic nerves (SN, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone-0017087-g002\" target=\"_blank\">Fig. 2E</a>, lanes 2, 4&6) of WT mice were transferred to nitrocellulose membranes and Ponceau S stained (<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone-0017087-g002\" target=\"_blank\">Fig. 2E</a>, lanes 1&2), and blot overlay assays were performed with Myo Va head (41–505, lanes 3&4) and neck regions (800–881, lanes 5&6) at equimolar concentrations. The positions of proteins in all membranes were indicated with an arrow. Anti-MBP: α-MBP; anti-NF-L:α-NF-L.</p>", "links"=>[], "tags"=>["va", "binds"], "article_id"=>468240, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g002", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Myo_Va_motor_domain_binds_to_NF_L_/468240", "title"=>"Myo Va motor domain binds to NF-L.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:17:20"}
  • {"files"=>["https://ndownloader.figshare.com/files/797657"], "description"=>"<p>(A). Amino acid numbers correspond to the mouse dilute gene product <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Mercer1\" target=\"_blank\">[6]</a>. The three domains of Myo Va are color coded (head-grey; rod-black and tail-white). The mutant proteins are either tagged with MBP (Hatched-circle) or hexa-His-peptide (star) or 3-kDa β-gal peptide (hatched-triangle). Constructs 5–752, 760–922 and 899–1830 are from chicken <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Costa1\" target=\"_blank\">[11]</a>. The construct tagged with β-gal-654-1402 is of human origin <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Engle1\" target=\"_blank\">[15]</a>, and the tail clones originate from the mouse sequence <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Mercer1\" target=\"_blank\">[6]</a>. Clones 718-799 and 800–881 are PCR products from chicken Myo Va <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017087#pone.0017087-Costa1\" target=\"_blank\">[11]</a>. (B) <i>Relative binding of Myo Va tail, head and neck regions to NF-L.</i> Myo Va head, neck and tail domains were incubated with NF-L, co-immunoprecipitated with NF-L antibody (NR-4), immunoprecipitates (IPs) and supernatants (Sup, 10%) were immunoblotted with anti-MBP and NF-L antibody (NR-4) and immunoreactive bands were detected with ECL reagent. The molecular weight (MW) of Myo Va head domain-120, neck-60 and tail is 140-kDa. *-indicates non-specific binding. (C) Myo Va head region shows more binding to NF-L compared to the neck region in blot overlay assays. Cytoskeletal fractions from spinal cord fractionated on 7% acrylamide gels containing SDS, transferred to nitrocellulose membranes, blocked with 3% milk, incubated with head and neck constructs tagged with MBP at equimolar concentrations, immunoblotted with anti-MBP-HRP antibody and immunoreactive bands were detected with ECL reagent. Ponc. S: Pnoceau S. (D) Myo Va head region binds to NF-L, α-internexin, peripherin and GFAP in blot overlay assays. Cytoskeletal fractions from optic nerve (ON), spinal cord (SC), and sciatic nerve (SN) were fractionated, and the Myo Va head domain binding activity was detected by blot overlay assay as described in panel C. (E) Myo Va head region binding to NF-L is specific since NF-L deficient cytoskeletal preparations do not show NF-L binding activity. Cytoskeletal fractions from WT and NF-L null (NF-L KO) mice spinal cord (SC) and sciatic nerve (SN) were fractionated and blot overlay assays were performed to detect Myo Va head domain binding activity as described in panel E. The positions of the bands on the membranes are indicated with arrows in all panels. Anti-MBP: α-MBP; anti-NF-L:α-NF-L.</p>", "links"=>[], "tags"=>["myo", "va", "deletion"], "article_id"=>468018, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_representation_of_Myo_Va_deletion_constructs_/468018", "title"=>"Schematic representation of Myo Va deletion constructs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:13:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/798624"], "description"=>"<p>Some Physiochemical Properties of Engineered NF-L Constructs.</p>", "links"=>[], "tags"=>["physiochemical", "properties", "engineered", "nf-l"], "article_id"=>468988, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.t001", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Some_Physiochemical_Properties_of_Engineered_NF_L_Constructs_/468988", "title"=>"Some Physiochemical Properties of Engineered NF-L Constructs.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-02-16 02:29:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/798397"], "description"=>"<p>In cross sections of WT (A), and dilute lethal control (DLC) (C) axons a clear tubulo-vesicular and vesicular profiles distribute diffusely in the radial dimension (A&C) but are more peripherally distributed in NF-L null (B) and DL20J (D) optic axons (see arrows in A–D). In comparison to WT axons (E, F, see arrows), cellular organelles in NF-L null optic axons (G) are peripherally distributed along channels beneath the axolemma in longitudinal sections (see the arrows in G). Quantitative measurements of distribution of organelles within 100 nm from periphery of axons that are larger than 1 µm demonstrate that increased peripheral distribution of ER in both NF-L null (H) and DL20J (I). (n = 5 animals for 6-month old WT and NF-L null, and 17 day DL20J and DLC). **p<0.01, and ***p<0.001. Error bars represent SEM. NF: neurofilaments; MT: microtubules; Mito: mitochondria; Peri: peripheral; Non-peri: non-peripheral.</p>", "links"=>[], "tags"=>["nf-l", "myo", "va", "leads", "peripheral", "er", "vesicles", "optic"], "article_id"=>468752, "categories"=>["Biochemistry", "Neuroscience", "Cell Biology"], "users"=>["Mala V. Rao", "Panaiyur S. Mohan", "Asok Kumar", "Aidong Yuan", "Lee Montagna", "Jabbar Campbell", "Veeranna", "Enilza M. Espreafico", "Jean P. Julien", "Ralph A. Nixon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017087.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Loss_of_NF_L_and_Myo_Va_leads_to_increased_peripheral_distribution_of_ER_vesicles_in_optic_axons_/468752", "title"=>"Loss of NF-L and Myo Va leads to increased peripheral distribution of ER vesicles in optic axons.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-16 02:25:52"}

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  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"9"}
  • {"unique-ip"=>"8", "full-text"=>"11", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"7", "supp-data"=>"1", "cited-by"=>"1", "year"=>"2014", "month"=>"10"}
  • {"unique-ip"=>"3", "full-text"=>"12", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"2"}
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  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"12"}
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  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2015", "month"=>"11"}
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  • {"unique-ip"=>"7", "full-text"=>"3", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"1"}
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  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"9"}
  • {"unique-ip"=>"6", "full-text"=>"2", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"10"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"11"}
  • {"unique-ip"=>"4", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"12"}
  • {"unique-ip"=>"7", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2017", "month"=>"1"}
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  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"3"}
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  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"5"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"6"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"7"}
  • {"unique-ip"=>"2", "full-text"=>"2", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"8"}
  • {"unique-ip"=>"6", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"9"}
  • {"unique-ip"=>"8", "full-text"=>"4", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"1", "year"=>"2017", "month"=>"10"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"11"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"12"}
  • {"unique-ip"=>"8", "full-text"=>"3", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"3", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"8", "full-text"=>"7", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"15", "full-text"=>"14", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"7", "full-text"=>"10", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
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Relative Metric

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