Ablation of cytoskeletal scaffolding proteins, Band 4.1B and Whirlin, leads to cerebellar purkinje axon pathology and motor dysfunction
The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered...
Saved in:
Published in | Journal of neuroscience research Vol. 97; no. 3; pp. 313 - 331 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Wiley Subscription Services, Inc
01.03.2019
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered morphological organization and electrical properties of the Purkinje axons lead to detrimental changes in locomotor activity often leading to cerebellar ataxias. Two cytoskeletal scaffolding proteins Band 4.1B (4.1B) and Whirlin (Whrn) have been previously shown to play independent roles in axonal domain organization and maintenance in myelinated axons in the spinal cord and sciatic nerves. Immunoblot analysis had indicated cerebellar expression for both 4.1B and Whrn; however, their subcellular localization and cerebellum‐specific functions have not been characterized. Using 4.1B and Whrn single and double mutant animals, we show that both proteins are expressed in common cellular compartments of the cerebellum and play cooperative roles in preservation of the integrity of Purkinje neuron myelinated axons. We demonstrate that both 4.1B and Whrn are required for the maintenance of axonal ultrastructure and health. Loss of 4.1B and Whrn leads to axonal transport defects manifested by formation of swellings containing cytoskeletal components, membranous organelles, and vesicles. Moreover, ablation of both proteins progressively affects cerebellar function with impairment in locomotor performance detected by altered gait parameters. Together, our data indicate that 4.1B and Whrn are required for maintaining proper axonal cytoskeletal organization and axonal domains, which is necessary for cerebellum‐controlled fine motor coordination.
Purkinje neurons myelinated fibers require intact axonal cytoskeletal organization and axonal transport to effectively transmit neural signals. We show that proteins Band 4.1B and Whirlin cooperatively maintain axonal cytoskeletal integrity at the paranodal and juxtaparanodal regions, and their loss leads to axonal cytoskeletal disorganization and formation of swellings leading to axonal degeneration. |
---|---|
AbstractList | The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered morphological organization and electrical properties of the Purkinje axons lead to detrimental changes in locomotor activity often leading to cerebellar ataxias. Two cytoskeletal scaffolding proteins Band 4.1B (4.1B) and Whirlin (Whrn) have been previously shown to play independent roles in axonal domain organization and maintenance in myelinated axons in the spinal cord and sciatic nerves. Immunoblot analysis had indicated cerebellar expression for both 4.1B and Whrn; however, their subcellular localization and cerebellum‐specific functions have not been characterized. Using 4.1B and Whrn single and double mutant animals, we show that both proteins are expressed in common cellular compartments of the cerebellum and play cooperative roles in preservation of the integrity of Purkinje neuron myelinated axons. We demonstrate that both 4.1B and Whrn are required for the maintenance of axonal ultrastructure and health. Loss of 4.1B and Whrn leads to axonal transport defects manifested by formation of swellings containing cytoskeletal components, membranous organelles, and vesicles. Moreover, ablation of both proteins progressively affects cerebellar function with impairment in locomotor performance detected by altered gait parameters. Together, our data indicate that 4.1B and Whrn are required for maintaining proper axonal cytoskeletal organization and axonal domains, which is necessary for cerebellum‐controlled fine motor coordination.
Purkinje neurons myelinated fibers require intact axonal cytoskeletal organization and axonal transport to effectively transmit neural signals. We show that proteins Band 4.1B and Whirlin cooperatively maintain axonal cytoskeletal integrity at the paranodal and juxtaparanodal regions, and their loss leads to axonal cytoskeletal disorganization and formation of swellings leading to axonal degeneration. The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered morphological organization and electrical properties of the Purkinje axons lead to detrimental changes in locomotor activity often leading to cerebellar ataxias. Two cytoskeletal scaffolding proteins Band 4.1B (4.1B) and Whirlin (Whrn) have been previously shown to play independent roles in axonal domain organization and maintenance in myelinated axons in the spinal cord and sciatic nerves. Immunoblot analysis had indicated cerebellar expression for both 4.1B and Whrn; however, their subcellular localization and cerebellum‐specific functions have not been characterized. Using 4 . 1B and Whrn single and double mutant animals, we show that both proteins are expressed in common cellular compartments of the cerebellum and play cooperative roles in preservation of the integrity of Purkinje neuron myelinated axons. We demonstrate that both 4.1B and Whrn are required for the maintenance of axonal ultrastructure and health. Loss of 4.1B and Whrn leads to axonal transport defects manifested by formation of swellings containing cytoskeletal components, membranous organelles, and vesicles. Moreover, ablation of both proteins progressively affects cerebellar function with impairment in locomotor performance detected by altered gait parameters. Together, our data indicate that 4.1B and Whrn are required for maintaining proper axonal cytoskeletal organization and axonal domains, which is necessary for cerebellum‐controlled fine motor coordination. The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered morphological organization and electrical properties of the Purkinje axons lead to detrimental changes in locomotor activity often leading to cerebellar ataxias. Two cytoskeletal scaffolding proteins Band 4.1B (4.1B) and Whirlin (Whrn) have been previously shown to play independent roles in axonal domain organization and maintenance in myelinated axons in the spinal cord and sciatic nerves. Immunoblot analysis had indicated cerebellar expression for both 4.1B and Whrn, however, their subcellular localization and cerebellum specific functions have not been characterized. Using 4.1B and Whrn single and double mutant animals, we show that both proteins are expressed in common cellular compartments of the cerebellum and play cooperative roles in preservation of the integrity of Purkinje neuron myelinated axons. We demonstrate that both 4.1B and Whrn are required for the maintenance of axonal ultrastructure and health. Loss of 4.1B and Whrn leads to axonal transport defects manifested by formation of swellings containing cytoskeletal components, membranous organelles and vesicles. Moreover, ablation of both proteins progressively affects cerebellar function with impairment in locomotor performance detected by altered gait parameters. Together, our data indicate that 4.1B and Whrn are required for maintaining proper axonal cytoskeletal organization and axonal domains, which is necessary for cerebellum controlled fine motor coordination. Purkinje neurons myelinated fibers require intact axonal cytoskeletal organization and axonal transport to effectively transmit neural signals. We show that proteins Band 4.1B and Whirlin cooperatively maintain axonal cytoskeletal integrity at the paranodal and juxtaparanodal regions, and their loss leads to axonal cytoskeletal disorganization and formation of swellings leading to axonal degeneration. The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from the cerebellum are the Purkinje neurons that transmit inhibitory responses to deep cerebellar nuclei through their myelinated axons. Altered morphological organization and electrical properties of the Purkinje axons lead to detrimental changes in locomotor activity often leading to cerebellar ataxias. Two cytoskeletal scaffolding proteins Band 4.1B (4.1B) and Whirlin (Whrn) have been previously shown to play independent roles in axonal domain organization and maintenance in myelinated axons in the spinal cord and sciatic nerves. Immunoblot analysis had indicated cerebellar expression for both 4.1B and Whrn; however, their subcellular localization and cerebellum‐specific functions have not been characterized. Using 4.1B and Whrn single and double mutant animals, we show that both proteins are expressed in common cellular compartments of the cerebellum and play cooperative roles in preservation of the integrity of Purkinje neuron myelinated axons. We demonstrate that both 4.1B and Whrn are required for the maintenance of axonal ultrastructure and health. Loss of 4.1B and Whrn leads to axonal transport defects manifested by formation of swellings containing cytoskeletal components, membranous organelles, and vesicles. Moreover, ablation of both proteins progressively affects cerebellar function with impairment in locomotor performance detected by altered gait parameters. Together, our data indicate that 4.1B and Whrn are required for maintaining proper axonal cytoskeletal organization and axonal domains, which is necessary for cerebellum‐controlled fine motor coordination. |
Author | Bhat, Manzoor A. Saifetiarova, Julia |
Author_xml | – sequence: 1 givenname: Julia surname: Saifetiarova fullname: Saifetiarova, Julia organization: University of Texas Health Science Center – sequence: 2 givenname: Manzoor A. orcidid: 0000-0003-0989-1498 surname: Bhat fullname: Bhat, Manzoor A. email: bhatm@uthscsa.edu organization: University of Texas Health Science Center |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30447021$$D View this record in MEDLINE/PubMed |
BookMark | eNp1kV1rFDEUhoNU7LZ64R-QgDcK3W2-JuncCG3xk6IgipfhTCazm202GZMZdX6Bf9tMtxYVvErIefKcc3iP0EGIwSL0mJIVJYSdbkNaMcErdg8tKKnVUlRCHaAF4ZIsBaHsEB3lvCWE1HXFH6BDToRQhNEF-nneeBhcDDh22ExDzNfW2wE8zga6LvrWhTXuUxysC_kEX0BosVjRCzxfvmxc8i6cYG-hzXiI2NhkG-s9JNyP6dqFrcXwo-h7GDbRx_V083EXh5hwO-VuDGZu_xDd78Bn--j2PEafX738dPlmefXh9dvL86ulqUjNllKdSSBtSyUnDUjacsUaC0LUwGoGjDegKgakKWVTsVqyugEqKtuJ8nZm-DF6sff2Y7OzrbFhSOB1n9wO0qQjOP13JbiNXsdvWnLBpFJF8OxWkOLX0eZB71w288bBxjFrRnlFGRVKFvTpP-g2jimU9Qola1rVis_U8z1lUsw52e5uGEr0HK8u8eqbeAv75M_p78jfeRbgdA98d95O_zfpd-8_7pW_AIADsmk |
CitedBy_id | crossref_primary_10_1038_s41392_022_00989_x crossref_primary_10_3389_fcell_2022_951809 crossref_primary_10_1002_glia_23809 crossref_primary_10_1016_j_isci_2024_110170 |
Cites_doi | 10.1016/j.brainres.2009.10.039 10.1038/ng1208 10.1002/glia.22430 10.1073/pnas.96.23.13450 10.1523/JNEUROSCI.1527-05.2005 10.1056/NEJM199801293380502 10.1136/jnnp.73.3.310 10.1097/00001756-200504250-00002 10.1002/jnr.21374 10.1083/jcb.139.1.169 10.3389/fnmol.2015.00044 10.1242/jcs.00967 10.1523/JNEUROSCI.1860-14.2014 10.1371/journal.pone.0025043 10.1073/pnas.0601082103 10.1038/414643a 10.1093/brain/120.3.393 10.1038/sj.onc.1208057 10.1089/08977150150502613 10.3389/fncel.2017.00011 10.1523/JNEUROSCI.2661-16.2017 10.1038/nn1335 10.1242/jcs.00094 10.1002/glia.22968 10.1016/j.tins.2010.03.006 10.1016/j.ajhg.2007.09.015 10.1038/nrn3380 10.1038/nn.3859 10.1016/S0896-6273(01)00294-X 10.1046/j.1365-2990.1999.00167.x 10.1038/nn.2346 10.1016/0005-2736(82)90281-4 10.1523/JNEUROSCI.6248-09.2010 10.1002/jnr.22015 10.1523/JNEUROSCI.5602-11.2012 10.1083/jcb.200908164 10.1016/S0955-0674(99)00080-0 10.1074/jbc.275.5.3247 10.1016/S0169-328X(00)00233-3 10.1007/s004010050995 10.1159/000322473 10.1038/nrn1868 10.1186/1471-2202-14-96 10.1093/hmg/ddr503 10.1073/pnas.0600923103 10.1002/jnr.24052 10.1016/S0896-6273(01)00296-3 10.1523/JNEUROSCI.1015-11.2011 10.1089/neu.1988.5.47 10.1093/hmg/ddt618 10.1093/hmg/ddi490 10.1097/NEN.0b013e3181da84db 10.1073/pnas.91.21.9818 10.1002/jnr.21154 10.1046/j.1460-9568.2003.02441.x 10.1523/JNEUROSCI.3071-12.2012 10.1074/jbc.M509806200 10.1371/journal.pgen.1000955 10.1093/hmg/11.23.2837 10.1083/jcb.200110003 10.1083/jcb.200705132 |
ContentType | Journal Article |
Copyright | 2018 Wiley Periodicals, Inc 2018 Wiley Periodicals, Inc. 2019 Wiley Periodicals, Inc. |
Copyright_xml | – notice: 2018 Wiley Periodicals, Inc – notice: 2018 Wiley Periodicals, Inc. – notice: 2019 Wiley Periodicals, Inc. |
DBID | NPM AAYXX CITATION 7QG 7QP 7QR 7TK 7U7 8FD C1K FR3 K9. P64 7X8 5PM |
DOI | 10.1002/jnr.24352 |
DatabaseName | PubMed CrossRef Animal Behavior Abstracts Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Neurosciences Abstracts Toxicology Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database ProQuest Health & Medical Complete (Alumni) Biotechnology and BioEngineering Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | PubMed CrossRef Technology Research Database Toxicology Abstracts Animal Behavior Abstracts ProQuest Health & Medical Complete (Alumni) Chemoreception Abstracts Engineering Research Database Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management MEDLINE - Academic |
DatabaseTitleList | CrossRef Technology Research Database PubMed |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology |
EISSN | 1097-4547 |
EndPage | 331 |
ExternalDocumentID | 10_1002_jnr_24352 30447021 JNR24352 |
Genre | article Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIH NIGMS funderid: GM063074 – fundername: the Morrison Trust and the Owen’s Foundation – fundername: National Multiple Sclerosis Society – fundername: the Zachry Foundation – fundername: NIGMS NIH HHS grantid: R01 GM063074 |
GroupedDBID | --- -~X .3N .55 .GA .GJ .Y3 05W 0R~ 10A 1L6 1OB 1OC 1ZS 31~ 33P 3O- 3SF 3WU 4.4 4ZD 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABEML ABIJN ABIVO ABJNI ABPVW ACAHQ ACBWZ ACCFJ ACCZN ACGFS ACIWK ACPOU ACPRK ACSCC ACXBN ACXQS ADBBV ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFFNX AFFPM AFGKR AFPWT AFRAH AFZJQ AHBTC AHMBA AITYG AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AUFTA AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BY8 C45 CS3 D-E D-F DCZOG DPXWK DR1 DR2 DRFUL DRSTM DU5 EBD EBS EJD EMOBN F00 F01 F04 F5P FEDTE G-S G.N GAKWD GNP GODZA H.T H.X HBH HF~ HGLYW HHY HHZ HVGLF HZ~ IX1 J0M JPC KQQ LATKE LAW LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES M6M MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ NNB O66 O9- OIG OVD P2P P2W P2X P4D PALCI PQQKQ Q.N Q11 QB0 QRW R.K RIWAO RJQFR ROL RWD RWI RX1 RYL SAMSI SUPJJ SV3 TEORI UB1 V2E W8V W99 WBKPD WIB WIH WIK WJL WNSPC WOHZO WQJ WRC WUP WXSBR WYISQ X7M XG1 XV2 YYP ZGI ZXP ZZTAW ~IA ~WT NPM AAMNL AAYXX ACRPL ACYXJ CITATION 7QG 7QP 7QR 7TK 7U7 8FD C1K FR3 K9. P64 7X8 5PM |
ID | FETCH-LOGICAL-c5092-6786a0dd1630ba61d372bea449a292a23ba752a0b30bc529629ba145ef40b38c3 |
IEDL.DBID | DR2 |
ISSN | 0360-4012 |
IngestDate | Tue Sep 17 21:12:19 EDT 2024 Wed Dec 04 11:58:26 EST 2024 Thu Oct 10 22:10:18 EDT 2024 Fri Dec 06 02:53:35 EST 2024 Sat Sep 28 08:29:24 EDT 2024 Sat Aug 24 00:41:05 EDT 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Keywords | Band 4.1B myelinated axons axonal degeneration whirlin cerebellum motor coordination Purkinje neurons |
Language | English |
License | 2018 Wiley Periodicals, Inc. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c5092-6786a0dd1630ba61d372bea449a292a23ba752a0b30bc529629ba145ef40b38c3 |
Notes | Funding information This work was supported by grants from NIH NIGMS GM063074, National Multiple Sclerosis Society, the Zachry Foundation, the Morrison Trust and the Owen's Foundation ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceptualization, J.S. and M.A.B. Writing – Original Draft, J.S. and M.A.B. Investigation, J.S. Writing – Review & Editing, J.S. and M.A.B. Visualization, J.S. Supervision and Funding acquisition, M.A.B. Methodology, J.S. and M.A.B. Author Contributions Formal Analysis, J.S. Resources, M.A.B. All authors in this study take responsibility for integrity of the research, as well as for accuracy of data acquisition and analysis. |
ORCID | 0000-0003-0989-1498 |
OpenAccessLink | https://europepmc.org/articles/pmc6342677?pdf=render |
PMID | 30447021 |
PQID | 2169159736 |
PQPubID | 1006396 |
PageCount | 19 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_6342677 proquest_miscellaneous_2135121476 proquest_journals_2169159736 crossref_primary_10_1002_jnr_24352 pubmed_primary_30447021 wiley_primary_10_1002_jnr_24352_JNR24352 |
PublicationCentury | 2000 |
PublicationDate | March 2019 |
PublicationDateYYYYMMDD | 2019-03-01 |
PublicationDate_xml | – month: 03 year: 2019 text: March 2019 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Hoboken |
PublicationTitle | Journal of neuroscience research |
PublicationTitleAlternate | J Neurosci Res |
PublicationYear | 2019 |
Publisher | Wiley Subscription Services, Inc |
Publisher_xml | – name: Wiley Subscription Services, Inc |
References | 2009; 87 2013; 61 2004; 7 2000; 85 2004; 23 2002; 11 2002; 156 2002; 115 2003; 17 2014; 23 2005; 25 2009; 12 2007; 178 2013; 14 2010; 69 2017; 37 2000; 12 2011; 70 1993; 30 1999; 97 1999; 96 2001; 18 2014; 17 2006; 281 2010; 30 2012; 21 2010; 6 2001; 414 2010; 33 1997; 139 2002; 73 1999; 25 2006; 15 2006; 7 2011; 31 1998; 338 1982; 688 2000; 275 2011; 6 2015; 8 2012; 32 2003; 34 2017; 95 1997; 120 2017; 11 1988; 5 2009; 187 2010; 1307 2007; 85 2005; 16 1994; 91 2008; 82 2004; 117 2014; 34 2001; 30 2006; 103 e_1_2_10_23_1 e_1_2_10_46_1 e_1_2_10_21_1 e_1_2_10_44_1 e_1_2_10_42_1 e_1_2_10_40_1 e_1_2_10_2_1 e_1_2_10_4_1 e_1_2_10_18_1 e_1_2_10_53_1 e_1_2_10_6_1 e_1_2_10_16_1 e_1_2_10_39_1 e_1_2_10_55_1 e_1_2_10_14_1 e_1_2_10_37_1 e_1_2_10_57_1 e_1_2_10_58_1 e_1_2_10_13_1 e_1_2_10_34_1 e_1_2_10_11_1 e_1_2_10_32_1 e_1_2_10_30_1 e_1_2_10_51_1 e_1_2_10_61_1 e_1_2_10_29_1 e_1_2_10_63_1 e_1_2_10_27_1 e_1_2_10_25_1 e_1_2_10_48_1 e_1_2_10_24_1 e_1_2_10_45_1 e_1_2_10_22_1 e_1_2_10_43_1 e_1_2_10_20_1 e_1_2_10_41_1 e_1_2_10_52_1 e_1_2_10_3_1 e_1_2_10_19_1 e_1_2_10_54_1 e_1_2_10_5_1 e_1_2_10_17_1 e_1_2_10_38_1 e_1_2_10_56_1 e_1_2_10_7_1 e_1_2_10_36_1 e_1_2_10_12_1 e_1_2_10_35_1 e_1_2_10_9_1 Conboy J. G. (e_1_2_10_15_1) 1993; 30 e_1_2_10_59_1 e_1_2_10_10_1 e_1_2_10_33_1 e_1_2_10_31_1 e_1_2_10_50_1 Brownlees J. (e_1_2_10_8_1) 2002; 11 e_1_2_10_60_1 e_1_2_10_62_1 e_1_2_10_28_1 e_1_2_10_49_1 e_1_2_10_26_1 e_1_2_10_47_1 |
References_xml | – volume: 30 start-page: 369 year: 2001 end-page: 383 article-title: Axon‐glia interactions and the domain organization of myelinated axons requires neurexin IV/Caspr/Paranodin publication-title: Neuron – volume: 11 start-page: 2837 year: 2002 end-page: 2844 article-title: Charcot‐Marie‐Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport publication-title: Human Molecular Genetics – volume: 8 start-page: 44 year: 2015 article-title: The axonal cytoskeleton: From organization to function publication-title: Frontiers in Molecular Neuroscience – volume: 30 start-page: 385 year: 2001 end-page: 397 article-title: Contactin orchestrates assembly of the septate‐like junctions at the paranode in myelinated peripheral nerve publication-title: Neuron – volume: 6 start-page: e25043 year: 2011 article-title: Protein 4.1B contributes to the organization of peripheral myelinated axons publication-title: PLoS ONE – volume: 30 start-page: 2480 year: 2010 end-page: 2489 article-title: Organization of myelinated axons by Caspr and Caspr2 requires the cytoskeletal adapter protein 4.1B publication-title: Journal of Neuroscience – volume: 120 start-page: 393 issue: Pt 3 year: 1997 end-page: 399 article-title: Axonal damage in acute multiple sclerosis lesions publication-title: Brain – volume: 33 start-page: 335 year: 2010 end-page: 344 article-title: Retrograde axonal transport: Pathways to cell death? publication-title: Trends in Neurosciences – volume: 37 start-page: 2524 year: 2017 end-page: 2538 article-title: Early and late loss of the cytoskeletal scaffolding protein, ankyrin G reveals its role in maturation and maintenance of nodes of ranvier in myelinated axons publication-title: Journal of Neuroscience – volume: 91 start-page: 9818 year: 1994 end-page: 9822 article-title: Cloning and characterization of hdlg: The human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1 publication-title: Proceedings of the National Academy of Sciences – volume: 87 start-page: 1773 year: 2009 end-page: 1793 article-title: Spatiotemporal ablation of myelinating glia‐specific neurofascin (Nfasc NF155) in mice reveals gradual loss of paranodal axoglial junctions and concomitant disorganization of axonal domains publication-title: Journal of Neuroscience Research – volume: 31 start-page: 8013 year: 2011 end-page: 8024 article-title: The cytoskeletal adaptor protein band 4.1B is required for the maintenance of paranodal axoglial septate junctions in myelinated axons publication-title: Journal of Neuroscience – volume: 16 start-page: 533 year: 2005 end-page: 536 article-title: Mutant superoxide dismutase disrupts cytoplasmic dynein in motor neurons publication-title: NeuroReport – volume: 18 start-page: 187 year: 2001 end-page: 201 article-title: Automated quantitative gait analysis during overground locomotion in the rat: Its application to spinal cord contusion and transection injuries publication-title: Journal of Neurotrauma – volume: 103 start-page: 10973 year: 2006 end-page: 10978 article-title: Whirlin complexes with p55 at the stereocilia tip during hair cell development publication-title: Proceedings of the National Academy of Sciences – volume: 7 start-page: 207 year: 2006 end-page: 219 article-title: Expanding insights of mitochondrial dysfunction in Parkinson's disease publication-title: Nature Reviews Neuroscience – volume: 103 start-page: 5137 year: 2006 end-page: 5142 article-title: Disruption of axo‐glial junctions causes cytoskeletal disorganization and degeneration of Purkinje neuron axons publication-title: Proceedings of the National Academy of Sciences – volume: 69 start-page: 455 year: 2010 end-page: 472 article-title: Mechanisms of axonal spheroid formation in central nervous system Wallerian degeneration publication-title: Journal of Neuropathology and Experimental Neurology – volume: 32 start-page: 14288 year: 2012 end-page: 14293 article-title: Localization of PDZD7 to the stereocilia ankle‐link associates this scaffolding protein with the Usher syndrome protein network publication-title: Journal of Neuroscience – volume: 414 start-page: 643 year: 2001 end-page: 648 article-title: Kinesin‐mediated axonal transport of a membrane compartment containing beta‐secretase and presenilin‐1 requires APP publication-title: Nature – volume: 12 start-page: 864 year: 2009 end-page: 871 article-title: Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin publication-title: Nature Neuroscience – volume: 688 start-page: 691 year: 1982 end-page: 701 article-title: The role of band 4.1 in the association of actin with erythrocyte membranes publication-title: Biochimica Biophysica Acta – volume: 187 start-page: 761 year: 2009 end-page: 772 article-title: Non‐cell autonomous toxicity in neurodegenerative disorders: ALS and beyond publication-title: Journal of Cell Biology – volume: 139 start-page: 169 year: 1997 end-page: 179 article-title: Identification of EBP50: A PDZ‐containing phosphoprotein that associates with members of the ezrin‐radixin‐moesin family publication-title: Journal of Cell Biology – volume: 23 start-page: 7761 year: 2004 end-page: 7771 article-title: DAL‐1/4.1B tumor suppressor interacts with protein arginine N‐methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo publication-title: Oncogene – volume: 85 start-page: 2318 year: 2007 end-page: 2331 article-title: No effect of genetic deletion of contactin‐associated protein (CASPR) on axonal orientation and synaptic plasticity publication-title: Journal of Neuroscience Research – volume: 82 start-page: 160 year: 2008 end-page: 164 article-title: A common genetic variant in the neurexin superfamily member CNTNAP2 increases familial risk of autism publication-title: American Journal of Human Genetics – volume: 25 start-page: 6667 year: 2005 end-page: 6675 article-title: The 4.1 protein coracle mediates subunit‐selective anchoring of Drosophila glutamate receptors to the postsynaptic actin cytoskeleton publication-title: Journal of Neuroscience – volume: 17 start-page: 411 year: 2003 end-page: 416 article-title: Protein 4.1B associates with both Caspr/paranodin and Caspr2 at paranodes and juxtaparanodes of myelinated fibres publication-title: European Journal of Neuroscience – volume: 15 start-page: 751 year: 2006 end-page: 765 article-title: The DFNB31 gene product whirlin connects to the Usher protein network in the cochlea and retina by direct association with USH2A and VLGR1 publication-title: Human Molecular Genetics – volume: 275 start-page: 3247 year: 2000 end-page: 3255 article-title: Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain publication-title: The Journal of Biological Chemistry – volume: 34 start-page: 11929 issue: 36 year: 2014 end-page: 11947 article-title: An RNA‐sequencing transcriptome and splicing database of glia, neurons, and vascular cells of the cerebral cortex publication-title: Journal of Neuroscience – volume: 338 start-page: 278 year: 1998 end-page: 285 article-title: Axonal transection in the lesions of multiple sclerosis publication-title: New England Journal of Medicine – volume: 156 start-page: 337 year: 2002 end-page: 348 article-title: [Beta]IV‐spectrin regulates sodium channel clustering through ankyrin‐G at axon initial segments and nodes of Ranvier publication-title: Journal of Cell Biology – volume: 30 start-page: 4232 year: 2010 end-page: 4240 article-title: Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex publication-title: Journal of Neuroscience – volume: 97 start-page: 329 year: 1999 end-page: 334 article-title: Neuroaxonal pathology in Creutzfeldt‐Jakob disease publication-title: Acta Neuropathologica – volume: 34 start-page: 421 year: 2003 end-page: 428 article-title: Defects in whirlin, a PDZ domain molecule involved in stereocilia elongation, cause deafness in the whirler mouse and families with DFNB31 publication-title: Nature Genetics – volume: 178 start-page: 861 year: 2007 end-page: 874 article-title: Nectin‐like proteins mediate axon Schwann cell interactions along the internode and are essential for myelination publication-title: Journal of Cell Biology – volume: 1307 start-page: 53 year: 2010 end-page: 62 article-title: Protein 4.1 expression in the developing hair cells of the mouse inner ear publication-title: Brain Research – volume: 11 start-page: 11 year: 2017 article-title: Postnatal loss of neuronal and glial neurofascins differentially affects node of ranvier maintenance and myelinated axon function publication-title: Frontiers of Cellular Neuroscience – volume: 21 start-page: 692 year: 2012 end-page: 710 article-title: Whirlin interacts with espin and modulates its actin‐regulatory function: An insight into the mechanism of Usher syndrome type II publication-title: Human Molecular Genetics – volume: 70 start-page: 56 year: 2011 end-page: 65 article-title: Usher syndrome: Hearing loss with vision loss publication-title: Advances in Oto‐Rhino‐Laryngology – volume: 281 start-page: 3552 year: 2006 end-page: 3559 article-title: Interaction of Huntingtin‐associated protein‐1 with kinesin light chain: Implications in intracellular trafficking in neurons publication-title: The Journal of Biological Chemistry – volume: 117 start-page: 1017 year: 2004 end-page: 1024 article-title: Parkinson's disease alpha‐synuclein mutations exhibit defective axonal transport in cultured neurons publication-title: Journal of Cell Science – volume: 73 start-page: 310 year: 2002 end-page: 312 article-title: Typical features of cerebellar ataxic gait publication-title: Journal of Neurology, Neurosurgery and Psychiatry – volume: 23 start-page: 2279 year: 2014 end-page: 2289 article-title: Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis multiplex congenita with axoglial defects publication-title: Human Molecular Genetics – volume: 85 start-page: 41 year: 2000 end-page: 52 article-title: Type II brain 4.1 (4.1B/KIAA0987), a member of the protein 4.1 family, is localized to neuronal paranodes publication-title: Brain Research. Molecular Brain Research – volume: 95 start-page: 1373 year: 2017 end-page: 1390 article-title: Axonal domain disorganization in Caspr1 and Caspr2 mutant myelinated axons affects neuromuscular junction integrity, leading to muscle atrophy publication-title: Journal of Neuroscience Research – volume: 7 start-page: 1181 year: 2004 end-page: 1183 article-title: Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches publication-title: Nature Neuroscience – volume: 5 start-page: 47 year: 1988 end-page: 60 article-title: The effect of traumatic brain injury on the visual system: A morphologic characterization of reactive axonal change publication-title: Journal of Neurotrauma – volume: 17 start-page: 1664 year: 2014 end-page: 1672 article-title: A hierarchy of ankyrin‐spectrin complexes clusters sodium channels at nodes of Ranvier publication-title: Nature Neuroscience – volume: 12 start-page: 229 year: 2000 end-page: 234 article-title: The genetics of the protein 4.1 family: organizers of the membrane and cytoskeleton publication-title: Current Opinion in Cell Biology – volume: 25 start-page: 123 year: 1999 end-page: 133 article-title: Neuronal apoptosis does not correlate with dementia in HIV infection but is related to microglial activation and axonal damage publication-title: Neuropathology and Applied Neurobiology – volume: 61 start-page: 240 year: 2013 end-page: 253 article-title: The 4.1B cytoskeletal protein regulates the domain organization and sheath thickness of myelinated axons publication-title: Glia – volume: 30 start-page: 58 year: 1993 end-page: 73 article-title: Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells publication-title: Seminars in Hematology – volume: 14 start-page: 96 year: 2013 article-title: Whirlin, a cytoskeletal scaffolding protein, stabilizes the paranodal region and axonal cytoskeleton in myelinated axons publication-title: BMC Neuroscience – volume: 32 start-page: 4724 year: 2012 end-page: 4742 article-title: Pinceau organization in the cerebellum requires distinct functions of Neurofascin in Purkinje and basket neurons during postnatal development publication-title: Journal of Neuroscience – volume: 96 start-page: 13450 year: 1999 end-page: 13455 article-title: Axon pathology in Parkinson's disease and Lewy body dementia hippocampus contains alpha‐, beta‐, and gamma‐synuclein publication-title: Proceedings of the National Academy of Sciences – volume: 6 start-page: e1000955 year: 2010 article-title: Ablation of whirlin long isoform disrupts the USH2 protein complex and causes vision and hearing loss publication-title: PLoS Genetics – volume: 85 start-page: 2620 year: 2007 end-page: 2630 article-title: Tau binding to microtubules does not directly affect microtubule‐based vesicle motility publication-title: Journal of Neuroscience Research – volume: 115 start-page: 3991 year: 2002 end-page: 4000 article-title: Protein 4.1 tumor suppressors: Getting a FERM grip on growth regulation publication-title: Journal of Cell Science – volume: 14 start-page: 161 year: 2013 end-page: 176 article-title: Axonal transport deficits and neurodegenerative diseases publication-title: Nature Reviews Neuroscience – ident: e_1_2_10_45_1 doi: 10.1016/j.brainres.2009.10.039 – ident: e_1_2_10_38_1 doi: 10.1038/ng1208 – ident: e_1_2_10_17_1 doi: 10.1002/glia.22430 – ident: e_1_2_10_20_1 doi: 10.1073/pnas.96.23.13450 – ident: e_1_2_10_11_1 doi: 10.1523/JNEUROSCI.1527-05.2005 – ident: e_1_2_10_58_1 doi: 10.1056/NEJM199801293380502 – ident: e_1_2_10_55_1 doi: 10.1136/jnnp.73.3.310 – ident: e_1_2_10_34_1 doi: 10.1097/00001756-200504250-00002 – ident: e_1_2_10_48_1 doi: 10.1002/jnr.21374 – ident: e_1_2_10_50_1 doi: 10.1083/jcb.139.1.169 – ident: e_1_2_10_30_1 doi: 10.3389/fnmol.2015.00044 – ident: e_1_2_10_51_1 doi: 10.1242/jcs.00967 – volume: 30 start-page: 58 year: 1993 ident: e_1_2_10_15_1 article-title: Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells publication-title: Seminars in Hematology contributor: fullname: Conboy J. G. – ident: e_1_2_10_63_1 doi: 10.1523/JNEUROSCI.1860-14.2014 – ident: e_1_2_10_13_1 doi: 10.1371/journal.pone.0025043 – ident: e_1_2_10_21_1 doi: 10.1073/pnas.0601082103 – ident: e_1_2_10_29_1 doi: 10.1038/414643a – ident: e_1_2_10_18_1 doi: 10.1093/brain/120.3.393 – ident: e_1_2_10_54_1 doi: 10.1038/sj.onc.1208057 – ident: e_1_2_10_24_1 doi: 10.1089/08977150150502613 – ident: e_1_2_10_57_1 doi: 10.3389/fncel.2017.00011 – ident: e_1_2_10_53_1 doi: 10.1523/JNEUROSCI.2661-16.2017 – ident: e_1_2_10_59_1 doi: 10.1038/nn1335 – ident: e_1_2_10_56_1 doi: 10.1242/jcs.00094 – ident: e_1_2_10_27_1 doi: 10.1002/glia.22968 – ident: e_1_2_10_47_1 doi: 10.1016/j.tins.2010.03.006 – ident: e_1_2_10_4_1 doi: 10.1016/j.ajhg.2007.09.015 – ident: e_1_2_10_40_1 doi: 10.1038/nrn3380 – ident: e_1_2_10_25_1 doi: 10.1038/nn.3859 – ident: e_1_2_10_6_1 doi: 10.1016/S0896-6273(01)00294-X – ident: e_1_2_10_3_1 doi: 10.1046/j.1365-2990.1999.00167.x – ident: e_1_2_10_43_1 doi: 10.1038/nn.2346 – ident: e_1_2_10_14_1 doi: 10.1016/0005-2736(82)90281-4 – ident: e_1_2_10_41_1 doi: 10.1523/JNEUROSCI.6248-09.2010 – ident: e_1_2_10_49_1 doi: 10.1002/jnr.22015 – ident: e_1_2_10_10_1 doi: 10.1523/JNEUROSCI.5602-11.2012 – ident: e_1_2_10_28_1 doi: 10.1083/jcb.200908164 – ident: e_1_2_10_26_1 doi: 10.1016/S0955-0674(99)00080-0 – ident: e_1_2_10_46_1 doi: 10.1074/jbc.275.5.3247 – ident: e_1_2_10_44_1 doi: 10.1016/S0169-328X(00)00233-3 – ident: e_1_2_10_33_1 doi: 10.1007/s004010050995 – ident: e_1_2_10_19_1 doi: 10.1159/000322473 – ident: e_1_2_10_2_1 doi: 10.1038/nrn1868 – ident: e_1_2_10_23_1 doi: 10.1186/1471-2202-14-96 – ident: e_1_2_10_61_1 doi: 10.1093/hmg/ddr503 – ident: e_1_2_10_37_1 doi: 10.1073/pnas.0600923103 – ident: e_1_2_10_52_1 doi: 10.1002/jnr.24052 – ident: e_1_2_10_7_1 doi: 10.1016/S0896-6273(01)00296-3 – ident: e_1_2_10_9_1 doi: 10.1523/JNEUROSCI.1015-11.2011 – ident: e_1_2_10_12_1 doi: 10.1089/neu.1988.5.47 – ident: e_1_2_10_32_1 doi: 10.1093/hmg/ddt618 – ident: e_1_2_10_60_1 doi: 10.1093/hmg/ddi490 – ident: e_1_2_10_5_1 doi: 10.1097/NEN.0b013e3181da84db – ident: e_1_2_10_35_1 doi: 10.1073/pnas.91.21.9818 – ident: e_1_2_10_42_1 doi: 10.1002/jnr.21154 – ident: e_1_2_10_16_1 doi: 10.1046/j.1460-9568.2003.02441.x – ident: e_1_2_10_22_1 doi: 10.1523/JNEUROSCI.3071-12.2012 – ident: e_1_2_10_39_1 doi: 10.1074/jbc.M509806200 – ident: e_1_2_10_62_1 doi: 10.1371/journal.pgen.1000955 – volume: 11 start-page: 2837 year: 2002 ident: e_1_2_10_8_1 article-title: Charcot‐Marie‐Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport publication-title: Human Molecular Genetics doi: 10.1093/hmg/11.23.2837 contributor: fullname: Brownlees J. – ident: e_1_2_10_31_1 doi: 10.1083/jcb.200110003 – ident: e_1_2_10_36_1 doi: 10.1083/jcb.200705132 |
SSID | ssj0009953 |
Score | 2.3497488 |
Snippet | The cerebellar cortex receives neural information from other brain regions to allow fine motor coordination and motor learning. The primary output neurons from... |
SourceID | pubmedcentral proquest crossref pubmed wiley |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 313 |
SubjectTerms | Ablation axonal degeneration Axonal transport Axons Band 4.1B Brain Cerebellum Cytoskeleton Domains Electrical properties Gait Gait recognition Localization Locomotor activity Motor ability motor coordination Motor skill learning Motors myelinated axons Nerves Neurons Organelles Preservation Proteins Purkinje cells Purkinje neurons Scaffolding Spinal cord Ultrastructure whirlin |
Title | Ablation of cytoskeletal scaffolding proteins, Band 4.1B and Whirlin, leads to cerebellar purkinje axon pathology and motor dysfunction |
URI | https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjnr.24352 https://www.ncbi.nlm.nih.gov/pubmed/30447021 https://www.proquest.com/docview/2169159736 https://search.proquest.com/docview/2135121476 https://pubmed.ncbi.nlm.nih.gov/PMC6342677 |
Volume | 97 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwELWqnrgApXyEFmQQQhyabeJ447U4bYGqqkQPFRU9IEUex1G3pU6VZKUuf6B_u2N7k7JUSIibFduxY8943tiTZ0LegWSaG65jCULFHAzEcsJ4DAzQ98lRhDxPwdej_OCEH56OT9fIx_5fmMAPMWy4Oc3w67VTcAXt7h1p6LltRgyNvVt_00y4cL7Px3fUUVIGBsosT9BHSlnPKpSw3aHmqi26BzDvx0n-jl-9Adp_RH70XQ9xJxejeQcj_esPVsf__LbH5OESmNJpkKQNsmbsE7I5teiUXy7oe-pDRf0e_Ca5mUIIoaN1RfWiq9sLtF4I42mrVVWFAy3qKSBmtt2he8qWlI_SPeoS389mjmJrh_5E-WppV1NtGuMOQFRDr-Zu8_7cUHWNr3f3Jfs2fUWUqrqh5aJ1xtg1_5Sc7H_59ukgXt7oEGsEJixGy5irpCwRBCag8rTMBAOjOJeKSaZYBkqMmUoAs7U7EWYSVMrHpuL4bKKzZ2Td1ta8IBRAc80RXyVVzqXJQU2UGmsQ6AIaDklE3vZzW1wF4o4iUDSzAoe38MMbke1-1oul7rYFc_xB6GdleUTeDNmode4oRVlTz12ZDJFSygWWeR6EZGglSzgXCJ0iIlbEZyjgGL1Xc-zszDN75xkCJiEi8sFLx987XhweHfvEy38vukUeINqTIYBum6x3zdy8QkTVwWuvOrcszh8z |
link.rule.ids | 230,314,780,784,885,1375,27924,27925,46294,46718 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwELWqcoALXwUaKGAQQhyabeJ4nbXEZQtUS2n3ULWiFxR5HEfdFpIqyUosf4C_zdjepCwVEuJmxXbs2DOeN_bkmZBXIJnmhutQQqpCDgZCOWI8BAbo-wgUIcdTcDgVkxO-fzo8XSNvu39hPD9Ev-FmNcOt11bB7Yb0zhVr6HlZDxhae1yAb6C6xzag6_3RFXmUlJ6DMhERekkx63iFIrbTV121Rtcg5vVIyd8RrDNBe3fIl67zPvLkYjBvYaB__MHr-L9fd5fcXmJTOvbCdI-smfI-2RiX6Jd_W9DX1EWLum34DfJzDD6KjlYF1Yu2ai7QgCGSp41WReHPtKhjgZiVzTbdVWVO-SDepTbx-WxmWba26VcUsYa2FdWmNvYMRNX0cm73788NVd_x9fbKZNemq4iCVdU0XzTWHtvmH5CTvQ_H7ybh8lKHUCM2YSEaR6GiPEccGIEScZ6kDIziXCommWIJqHTIVASYre2hMJOgYj40BcdnI508JOtlVZpNQgE01xwhVlQILo0ANVJqqCFFL9BwiALyspvc7NJzd2SepZllOLyZG96AbHXTni3Vt8mYpRBCVysRAXnRZ6Pi2dMUVZpqbsskCJZinmKZR15K-laSiPMU0VNA0hX56QtYUu_VnHJ25si9RYKYKU0D8saJx987nu1Pj1zi8b8XfU5uTo4PD7KDj9NPT8gtBH_Sx9NtkfW2npunCLBaeOb06BcNiiNU |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwED9NQ0K88DU-AgMMQoiHpUsc16nFU8eoxoAKTUzsASmyHUfrBkmVpBLlH-Df5mw3GWVCQrxZsR079p3vd_blZ4DnSlDNDNOhUKkMmTIqFCPKQkUV-j4cRcjxFHyY8oNjdngyPNmAV92_MJ4fot9ws5rh1mur4PO82L0gDT0r6wFFY4_r7xXGqbDE-ftHF9xRQngKyoRH6CTFtKMViuhuX3XdGF1CmJcDJX8HsM4CTW7Al67vPvDkfLBo1UD_-IPW8T8_7iZcXyFTMvaidAs2THkbtsYleuXfluQFcbGibhN-C36OlY-hI1VB9LKtmnM0X4jjSaNlUfgTLeI4IGZls0P2ZJkTNoj3iE18Pp1Zjq0d8hUFrCFtRbSpjT0BkTWZL-zu_Zkh8ju-3l6Y7Np0FVGsqprky8ZaY9v8HTievPn0-iBcXekQakQmNETTyGWU54gCIyV5nCcpVUYyJiQVVNJEyXRIZaQwW9sjYSqUjNnQFAyfjXRyFzbLqjT3gSilmWYIsKKCM2G4kiMph1ql6AMapqIAnnVzm809c0fmOZpphsObueENYLub9WylvE1GLYEQOloJD-Bpn41qZ89SZGmqhS2TIFSKWYpl7nkh6VtJIsZSxE4BpGvi0xewlN7rOeXs1FF78wQRU5oG8NJJx987nh1Oj1ziwb8XfQJXP-5Psvdvp-8ewjVEfsIH023DZlsvzCNEV6167LToF5XJIgM |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Ablation+of+cytoskeletal+scaffolding+proteins%2C+Band+4.1B+and+Whirlin%2C+leads+to+cerebellar+purkinje+axon+pathology+and+motor+dysfunction&rft.jtitle=Journal+of+neuroscience+research&rft.au=Saifetiarova%2C+Julia&rft.au=Bhat%2C+Manzoor+A.&rft.date=2019-03-01&rft.issn=0360-4012&rft.eissn=1097-4547&rft.volume=97&rft.issue=3&rft.spage=313&rft.epage=331&rft_id=info:doi/10.1002%2Fjnr.24352&rft.externalDBID=n%2Fa&rft.externalDocID=10_1002_jnr_24352 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0360-4012&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0360-4012&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0360-4012&client=summon |