Effects of detyrosinated tubulin on Na+,K+-ATPase activity and erythrocyte function in hypertensive subjects

•Detyrosinated tubulin is able to inhibit the NKA activity.•Erythrocytes of hypertensive subjects have a reduced content and activity of TTL.•GluTub levels and NKA activity are related to erythrocyte deformability.•The mechanism explains involvement of tubulin in hypertension. Formation of tubulin/N...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 589; no. 3; pp. 364 - 373
Main Authors Amaiden, Marina R., Santander, Verónica S., Monesterolo, Noelia E., Nigra, Ayelen D., Rivelli, Juan F., Campetelli, Alexis N., Pie, Juan, Casale, Cesar H.
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 30.01.2015
Subjects
Online AccessGet full text

Cover

Loading…
Abstract •Detyrosinated tubulin is able to inhibit the NKA activity.•Erythrocytes of hypertensive subjects have a reduced content and activity of TTL.•GluTub levels and NKA activity are related to erythrocyte deformability.•The mechanism explains involvement of tubulin in hypertension. Formation of tubulin/Na+,K+-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development.
AbstractList Formation of tubulin/Na + ,K + ‐ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development. Detyrosinated tubulin is able to inhibit the NKA activity. Erythrocytes of hypertensive subjects have a reduced content and activity of TTL. GluTub levels and NKA activity are related to erythrocyte deformability. The mechanism explains involvement of tubulin in hypertension.
Formation of tubulin/Na+,K+‐ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development. Detyrosinated tubulin is able to inhibit the NKA activity. Erythrocytes of hypertensive subjects have a reduced content and activity of TTL. GluTub levels and NKA activity are related to erythrocyte deformability. The mechanism explains involvement of tubulin in hypertension.
Formation of tubulin/Na(+),K(+)-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development.
•Detyrosinated tubulin is able to inhibit the NKA activity.•Erythrocytes of hypertensive subjects have a reduced content and activity of TTL.•GluTub levels and NKA activity are related to erythrocyte deformability.•The mechanism explains involvement of tubulin in hypertension. Formation of tubulin/Na+,K+-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development.
Formation of tubulin/Na(+),K(+)-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development.Formation of tubulin/Na(+),K(+)-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that detyrosinated tubulin, which is increased in hypertensive erythrocytes membranes, enhances the inhibitory effect of acetylated tubulin on NKA activity. Moreover, we report a reduced content and activity of the enzyme tubulin tyrosine ligase in erythrocytes of hypertensive subjects. Such alterations are related to changes in erythrocyte deformability. Our findings indicate that the detyrosination/tyrosination cycle of tubulin is important in regulation of NKA activity, and that abnormalities in this cycle are involved in hypertension development.
Author Casale, Cesar H.
Nigra, Ayelen D.
Santander, Verónica S.
Pie, Juan
Amaiden, Marina R.
Monesterolo, Noelia E.
Rivelli, Juan F.
Campetelli, Alexis N.
Author_xml – sequence: 1
  givenname: Marina R.
  surname: Amaiden
  fullname: Amaiden, Marina R.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 2
  givenname: Verónica S.
  surname: Santander
  fullname: Santander, Verónica S.
  email: vsantander@exa.unrc.edu.ar
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 3
  givenname: Noelia E.
  surname: Monesterolo
  fullname: Monesterolo, Noelia E.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 4
  givenname: Ayelen D.
  surname: Nigra
  fullname: Nigra, Ayelen D.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 5
  givenname: Juan F.
  surname: Rivelli
  fullname: Rivelli, Juan F.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 6
  givenname: Alexis N.
  surname: Campetelli
  fullname: Campetelli, Alexis N.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
– sequence: 7
  givenname: Juan
  surname: Pie
  fullname: Pie, Juan
  organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, Medical School, University of Zaragoza, Spain
– sequence: 8
  givenname: Cesar H.
  surname: Casale
  fullname: Casale, Cesar H.
  organization: Departamento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, 5800 Córdoba, Argentina
BackLink https://www.ncbi.nlm.nih.gov/pubmed/25541490$$D View this record in MEDLINE/PubMed
BookMark eNqNkktvEzEUhS1URNPCTwB5iVQm-DEPj1igUqUtogIkytqyPdeqo4kntT1B8-_rUQILNunKsu937rXP8Rk68YMHhN5SsqSE1h_XSws69pCWjNBySdmSMPYCLahoeMHLWpygBcmVompaforOYlyTvBe0fYVOWVWVtGzJAvUra8GkiAeLO0hTGKLzKkGH06jH3nk8ePxdXXz4dlFc3v9UEbAyye1cmrDyHYYwpYcwmCkBtqPPpcxn1cO0hZDAR7cDHEe9noe8Ri-t6iO8Oazn6Pf16v7qtrj7cfP16vKuMLXgoihFw7TooKa61rWlTdNwxRtjuC1r3VS6zU-uBCPCCE1yEazNx1wwBRUows_R-33fbRgeR4hJblw00PfKwzBGybITjBKepcdQWjecC1KS56AV421bkyqj7w7oqDfQyW1wGxUm-df3DFR7wGTDYwD7D6FEzvnKtTzkK-d8JWUy55t1n_7TGZfUbHoKyvVH1bd79R_Xw_S8kfJ69YX9mn_S_JFoSUhLmMitPu9bQc5x5yDIaBx4A50LOWrZDe7IZZ4ADyXY7A
CitedBy_id crossref_primary_10_1007_s13105_023_00946_4
crossref_primary_10_3390_biomedicines9040377
crossref_primary_10_1097_MBP_0000000000000592
crossref_primary_10_1016_j_biocel_2017_08_012
crossref_primary_10_33549_physiolres_933402
crossref_primary_10_1007_s00018_019_03346_4
crossref_primary_10_1007_s12011_015_0504_3
crossref_primary_10_1093_jb_mvab016
crossref_primary_10_1139_cjpp_2018_0735
crossref_primary_10_1038_ncomms9526
crossref_primary_10_1016_j_bbamcr_2024_119700
crossref_primary_10_1016_j_biocel_2016_02_016
crossref_primary_10_1038_s41419_018_1018_7
crossref_primary_10_1007_s13105_021_00820_1
crossref_primary_10_1002_jcp_27610
crossref_primary_10_1016_j_bioactmat_2025_01_021
crossref_primary_10_1007_s12013_023_01206_4
Cites_doi 10.1182/blood.V63.5.1046.1046
10.1097/HJH.0b013e328353b19a
10.1083/jcb.105.1.251
10.1042/bj2260311
10.1146/annurev.biochem.71.102201.141218
10.1152/ajpheart.00109.2007
10.1111/j.1365-2362.1979.tb00898.x
10.1042/bj3150183
10.1016/0003-2697(72)90046-2
10.1111/j.1462-5822.2007.00901.x
10.1016/0092-8674(84)90273-3
10.1093/ajh/4.1.14
10.1158/0008-5472.CAN-06-3732
10.1111/j.1432-1033.1988.tb14402.x
10.1016/S0021-9258(17)32067-7
10.1042/BJ20082410
10.1016/0003-2697(76)90527-3
10.1007/s11010-006-9212-9
10.1146/annurev.cb.04.110188.003351
10.1007/s00018-010-0549-6
10.1111/j.1471-4159.1978.tb12449.x
10.1111/j.1432-1033.1980.tb04813.x
10.1247/csf.09027
10.1016/j.biocel.2012.04.011
10.1007/BF00231230
10.1158/0008-5472.CAN-09-4613
10.1074/jbc.273.34.21744
10.1155/2008/730594
10.1023/A:1011029125228
10.1161/01.HYP.9.1.18
10.1111/j.1471-4159.1973.tb07578.x
10.1083/jcb.200512058
10.1161/01.HYP.10.3.259
ContentType Journal Article
Copyright 2014 Federation of European Biochemical Societies
FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2014 Federation of European Biochemical Societies
– notice: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies
– notice: Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
DBID 6I.
AAFTH
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7ST
C1K
SOI
7S9
L.6
DOI 10.1016/j.febslet.2014.12.022
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
Environment Abstracts
Environmental Sciences and Pollution Management
Environment Abstracts
AGRICOLA
AGRICOLA - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
Environment Abstracts
Environmental Sciences and Pollution Management
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList CrossRef

MEDLINE
AGRICOLA

Environment Abstracts
MEDLINE - Academic
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
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
Biology
EISSN 1873-3468
EndPage 373
ExternalDocumentID 25541490
10_1016_j_febslet_2014_12_022
FEB2S0014579314009028
S0014579314009028
Genre shortCommunication
Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
-~X
.~1
0R~
0SF
1B1
1OC
1~.
1~5
24P
2WC
33P
4.4
4G.
53G
5GY
5RE
5VS
6I.
7-5
71M
8P~
AABNK
AACTN
AAEDW
AAESR
AAFTH
AAHHS
AAIKJ
AAJUZ
AALRI
AANLZ
AAQFI
AASGY
AAXRX
AAXUO
AAZKR
ABBQC
ABCUV
ABFNM
ABFRF
ABGSF
ABHUG
ABJNI
ABLJU
ABMAC
ABQWH
ABVKL
ABXGK
ACAHQ
ACCFJ
ACCZN
ACGFO
ACGFS
ACGOF
ACIUM
ACMXC
ACNCT
ACPOU
ACXBN
ACXQS
ADAWD
ADBBV
ADBTR
ADDAD
ADEOM
ADEZE
ADKYN
ADMGS
ADOZA
ADQTV
ADUVX
ADXAS
ADZMN
ADZOD
AEEZP
AEFWE
AEGXH
AEKER
AENEX
AEQDE
AEQOU
AEUQT
AEUYR
AEXQZ
AFBPY
AFFNX
AFFPM
AFGKR
AFPWT
AFVGU
AFZJQ
AGJLS
AGYEJ
AHBTC
AIACR
AIAGR
AITUG
AIURR
AIWBW
AJBDE
AJRQY
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
AMYDB
AZFZN
AZVAB
BAWUL
BFHJK
BMXJE
C45
CBWCG
CS3
DCZOG
DIK
DOVZS
DRFUL
DRMAN
DRSTM
DU5
E3Z
EBS
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FIRID
FNPLU
FUBAC
G-Q
GBLVA
GX1
HVGLF
IHE
IXB
J1W
KBYEO
L7B
LATKE
LCYCR
LEEKS
LITHE
LOXES
LUTES
LX3
LYRES
M41
MEWTI
MO0
MRFUL
MRMAN
MRSTM
MSFUL
MSMAN
MSSTM
MXFUL
MXMAN
MXSTM
N9A
NCXOZ
O-L
O9-
OK1
OVD
OZT
P-8
P-9
P2P
P2W
PC.
Q38
R9-
RIG
RNS
ROL
RPZ
SCC
SDF
SDG
SDP
SEL
SES
SFE
SSZ
SUPJJ
TEORI
TR2
UHB
UNMZH
WBKPD
WH7
WIH
WIJ
WIK
WIN
WOHZO
WXSBR
YK3
ZA5
ZZTAW
~02
AAHBH
AAHQN
AAIPD
AAMNL
AAYCA
ADVLN
AFWVQ
AITYG
AKRWK
ALUQN
ALVPJ
HGLYW
AAYWO
AAYXX
ACVFH
ADCNI
AEUPX
AEYWJ
AFPUW
AGYGG
AIGII
AKBMS
AKYEP
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
AAMMB
AEFGJ
AGXDD
AIDQK
AIDYY
7ST
C1K
SOI
7S9
L.6
ID FETCH-LOGICAL-c6838-4872b8de61b6b6f17773a37cc3f46b75b920158208c8b0773effb75382ae5ea03
IEDL.DBID IXB
ISSN 0014-5793
1873-3468
IngestDate Fri Jul 11 07:54:40 EDT 2025
Thu Jul 10 22:42:14 EDT 2025
Fri Jul 11 16:00:28 EDT 2025
Thu Apr 03 07:08:00 EDT 2025
Thu Apr 24 22:59:58 EDT 2025
Tue Jul 01 02:46:41 EDT 2025
Wed Jan 22 16:38:09 EST 2025
Fri Feb 23 02:33:21 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 3
Keywords Hypertension
GluTub
TyrTub
Na+,K+-ATPase
NKA
TTCP
PAGE
TTL
Human erythrocytes
PMSF
Detyrosinated tubulin
AcTub
Erythrocyte deformability
Na(+),K(+)-ATPase
Language English
License http://www.elsevier.com/open-access/userlicense/1.0
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c6838-4872b8de61b6b6f17773a37cc3f46b75b920158208c8b0773effb75382ae5ea03
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S0014579314009028
PMID 25541490
PQID 1652399605
PQPubID 23479
PageCount 10
ParticipantIDs proquest_miscellaneous_2000210377
proquest_miscellaneous_1673380407
proquest_miscellaneous_1652399605
pubmed_primary_25541490
crossref_primary_10_1016_j_febslet_2014_12_022
crossref_citationtrail_10_1016_j_febslet_2014_12_022
wiley_primary_10_1016_j_febslet_2014_12_022_FEB2S0014579314009028
elsevier_sciencedirect_doi_10_1016_j_febslet_2014_12_022
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate January 30, 2015
PublicationDateYYYYMMDD 2015-01-30
PublicationDate_xml – month: 01
  year: 2015
  text: January 30, 2015
  day: 30
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle FEBS letters
PublicationTitleAlternate FEBS Lett
PublicationYear 2015
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Rivelli, Amaiden, Monesterolo, Previtali, Santander, Fernandez, Arce, Casale (b0135) 2012; 44
Zampar, Chesta, Carbajal, Chanaday, Díaz, Casale, Arce (b0080) 2009; 422
Sullivan (b0005) 1988; 4
Peris, Thery, Fauré, Saoudi, Lafanechère, Chilton, Gordon-Weeks, Galjart, Bornens, Wordeman, Wehland, Andrieux, Job (b0035) 2006; 174
Argaraña, Barra, Caputto (b0010) 1978; 19
Wambach, Overhoff, Hossmann (b0150) 1985; 63
Rygielski, Reddi, Kuriyama, Lasker, Aviv (b0050) 1987; 10
Laemmli (b0110) 1970; 227
Alonso, Arce, Barra (b0090) 1988; 177
Barra, Arce, Rodriguez, Caputto (b0020) 1973; 21
Casale, Alonso, Barra (b0075) 2001; 216
Gundersen, Khawaja, Bulinski (b0070) 1987; 105
Khalil-Manesh, Venkataraman, Samant, Gadgil (b0175) 1987; 9
Arce, Barra (b0100) 1985; 226
Barra, Arce, Caputto (b0085) 1980; 109
Santander, Bisig, Purro, Casale, Arce, Barra (b0055) 2006; 291
Ballas, Clark, Mohandas, Colfer, Caswell, Bergren, Perkins, Shohet (b0145) 1984; 63
Borisy (b0095) 1972; 50
Lingrel, Kuntzweiler (b0165) 1994; 269
Arce, Hallak, Rodríguez, Barra, Caputto (b0015) 1978; 31
Whipple, Matrone, Cho, Balzer, Vitolo, Yoon, Ioffe, Tuttle, Yang, Martin (b0040) 2010; 70
Alet, Chiesa, D’Arrigo, Foresto, Valverde, Rasia (b0065) 2001; 35
Aderounmu, Salako (b0045) 1979; 9
Gundersen, Kalnoski, Bulinski (b0025) 1984; 38
Bradford (b0125) 1976; 72
De Witt, dos Santos, Allen, Slayman (b0105) 1998; 273
Cabrales (b0120) 2007; 293
Hach, Forst, Kunt, Ekberg, Pfützner, Wahren (b0155) 2008
Kaplan (b0170) 2002; 71
Gobel, Schulte, Weisser, Glanzer, Vetter, Dusing (b0060) 1991; 4
Ikegami, Setou (b0160) 2010; 35
Salvador, Mata (b0115) 1996; 315
Fonrose, Ausseil, Soleilhac, Masson, David, Pouny, Cintrat, Rousseau, Barette, Massiot, Lafanechère (b0130) 2007; 67
Amaiden, Monesterolo, Santander, Campetelli, Arce, Pie, Hope, Vatta, Casale (b0140) 2012; 30
Amaiden, Santander, Monesterolo, Campetelli, Rivelli, Previtali, Arce, Casale (b0030) 2011; 68
1991; 4
1984; 63
1987; 10
2010; 35
1987; 105
1987; 9
1978; 31
2006; 174
1978; 19
2008
2006; 291
1985; 226
1985; 63
1970; 227
2012; 30
1998; 273
1988; 4
1980; 109
1994; 269
2007; 293
1973; 21
1984; 38
1976; 72
1972; 50
1988; 177
2011; 68
2002; 71
2010; 70
2001; 35
2007; 67
2012; 44
2009; 422
1979; 9
2001; 216
1996; 315
e_1_2_6_32_1
e_1_2_6_10_1
e_1_2_6_30_1
Alet A. (e_1_2_6_14_1) 2001; 35
e_1_2_6_19_1
Wambach G. (e_1_2_6_31_1) 1985; 63
e_1_2_6_13_1
e_1_2_6_36_1
e_1_2_6_35_1
e_1_2_6_11_1
e_1_2_6_34_1
e_1_2_6_12_1
e_1_2_6_33_1
e_1_2_6_17_1
e_1_2_6_18_1
e_1_2_6_15_1
e_1_2_6_16_1
e_1_2_6_21_1
e_1_2_6_20_1
e_1_2_6_9_1
e_1_2_6_8_1
e_1_2_6_5_1
e_1_2_6_4_1
e_1_2_6_7_1
e_1_2_6_6_1
e_1_2_6_25_1
e_1_2_6_24_1
e_1_2_6_3_1
e_1_2_6_23_1
e_1_2_6_2_1
e_1_2_6_22_1
e_1_2_6_29_1
e_1_2_6_28_1
e_1_2_6_27_1
e_1_2_6_26_1
References_xml – volume: 35
  start-page: 63
  year: 2001
  end-page: 68
  ident: b0065
  article-title: Hemorreología comparativa. Estudio en diabéticos e hipertensos
  publication-title: Acta Bioquim. Clin. Latinoam.
– volume: 50
  start-page: 373
  year: 1972
  end-page: 385
  ident: b0095
  article-title: A rapid method for quantitative determination of microtubule protein using DEAE-cellulose filters
  publication-title: Anal. Biochem.
– volume: 4
  start-page: 14
  year: 1991
  end-page: 19
  ident: b0060
  article-title: Arterial blood pressure. Correlation whit erythrocyte count, hematocrit and hemoglobin concentration
  publication-title: Am. J. Hypertens.
– volume: 422
  start-page: 129
  year: 2009
  end-page: 137
  ident: b0080
  article-title: Acetylated tubulin associates with the fifth cytoplasmic domain of Na(+)/K(+)-ATPase: possible anchorage site of microtubules to the plasma membrane
  publication-title: Biochem. J.
– volume: 273
  start-page: 21744
  year: 1998
  end-page: 21751
  ident: b0105
  article-title: Phosphorylation region of the yeast plasma membrane H+-ATPase. Role in protein folding and biogenesis
  publication-title: J. Biol. Chem.
– volume: 269
  start-page: 19659
  year: 1994
  end-page: 19662
  ident: b0165
  article-title: Na
  publication-title: J. Biol. Chem.
– volume: 9
  start-page: 18
  year: 1987
  end-page: 23
  ident: b0175
  article-title: Effects of diltiazem on cation transport across erythrocyte membranes of hypertensive humans
  publication-title: Hypertension
– volume: 19
  start-page: 17
  year: 1978
  end-page: 21
  ident: b0010
  article-title: Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase
  publication-title: Mol. Cell. Biochem.
– volume: 216
  start-page: 85
  year: 2001
  end-page: 92
  ident: b0075
  article-title: Brain plasma membrane Na+, K+-ATPase is inhibited by acetylated tubulin
  publication-title: Mol. Cell. Biochem.
– volume: 226
  start-page: 311
  year: 1985
  end-page: 317
  ident: b0100
  article-title: Release of C-terminal tyrosine from tubulin and microtubules at steady state
  publication-title: Biochem. J.
– volume: 227
  start-page: 680
  year: 1970
  end-page: 685
  ident: b0110
  article-title: Cleavage of structural proteins during the assembly of the head of bacteriophage T4
  publication-title: Nature
– volume: 293
  start-page: 1206
  year: 2007
  end-page: 1215
  ident: b0120
  article-title: Effects of erythrocyte flexibility on microvascular perfusion and oxygenation during acute anemia
  publication-title: Am. J. Physiol. Heart Circ. Physiol.
– volume: 70
  start-page: 8127
  year: 2010
  end-page: 8137
  ident: b0040
  article-title: Epithelial-to-mesenchymal transition promotes tubulin detyrosination and microtentacles that enhance endothelial engagement
  publication-title: Cancer Res.
– volume: 30
  start-page: 1414
  year: 2012
  end-page: 1422
  ident: b0140
  article-title: Involvement of membrane tubulin in erythrocyte deformability and blood pressure
  publication-title: J. Hypertens.
– volume: 63
  start-page: 1046
  year: 1984
  end-page: 1055
  ident: b0145
  article-title: Red cell membrane and cation deficiency in Rh null syndrome
  publication-title: Blood
– volume: 31
  start-page: 205
  year: 1978
  end-page: 210
  ident: b0015
  article-title: Capability of tubulin and microtubules to incorporate and to release tyrosine and phenylalanine and the effect of the incorporation of these amino acids on tubulin assembly
  publication-title: J. Neurochem.
– volume: 44
  start-page: 1203
  year: 2012
  end-page: 1213
  ident: b0135
  article-title: High glucose levels induce inhibition of Na, K-ATPase via stimulation of aldose reductase, formation of microtubules and formation of an acetylated tubulin/Na, K-ATPase complex
  publication-title: Int. J. Biochem. Cell Biol.
– year: 2008
  ident: b0155
  article-title: C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients
  publication-title: Exp. Diab. Res.
– volume: 291
  start-page: 167
  year: 2006
  end-page: 174
  ident: b0055
  article-title: Tubulin must be acetylated in order to form a complex with membrane Na(+), K(+)-ATPase and to inhibit its enzyme activity
  publication-title: Mol. Cell. Biochem.
– volume: 177
  start-page: 517
  year: 1988
  end-page: 522
  ident: b0090
  article-title: Relationship between the tyrosination state of tubulin and the activities of tubulin: tyrosine ligase and tubulin carboxypeptidase in rat muscle during development
  publication-title: Eur. J. Biochem.
– volume: 315
  start-page: 183
  year: 1996
  end-page: 187
  ident: b0115
  article-title: Purification of the synaptosomal plasma membrane (Ca2+/Mg2+)-ATPase from pig brain
  publication-title: Biochem. J.
– volume: 72
  start-page: 248
  year: 1976
  end-page: 254
  ident: b0125
  article-title: A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principles of dye-protein binding
  publication-title: Anal. Biochem.
– volume: 4
  start-page: 687
  year: 1988
  end-page: 716
  ident: b0005
  article-title: Structure and utilization of tubulin isotypes
  publication-title: Annu. Rev. Cell Biol.
– volume: 105
  start-page: 251
  year: 1987
  end-page: 264
  ident: b0070
  article-title: Postpolymerization detyrosination of α-tubulin: a mechanism for subcellular differentiation of microtubules
  publication-title: J. Cell Biol.
– volume: 67
  start-page: 3371
  year: 2007
  end-page: 3378
  ident: b0130
  article-title: Parthenolide inhibits tubulin carboxypeptidase activity
  publication-title: Cancer Res.
– volume: 71
  start-page: 511
  year: 2002
  end-page: 535
  ident: b0170
  article-title: Biochemistry of Na, K-ATPase
  publication-title: Annu. Rev. Biochem.
– volume: 109
  start-page: 439
  year: 1980
  end-page: 446
  ident: b0085
  article-title: Total tubulin and its aminoacylated and non-aminoacylated forms during the development of rat brain
  publication-title: Eur. J. Biochem.
– volume: 10
  start-page: 259
  year: 1987
  end-page: 266
  ident: b0050
  article-title: Erythrocyte ghost, Na+, K+-ATPase and blood pressure
  publication-title: Hypertension
– volume: 21
  start-page: 1241
  year: 1973
  end-page: 1251
  ident: b0020
  article-title: Incorporation of phenylalanine as a single unit into rat brain protein: reciprocal inhibition by phenylalanine and tyrosine of their respective incorporations
  publication-title: J. Neurochem.
– volume: 35
  start-page: 15
  year: 2010
  end-page: 22
  ident: b0160
  article-title: Unique post-translational modifications in specialized microtubule architecture
  publication-title: Cell Struct. Funct.
– volume: 9
  start-page: 369
  year: 1979
  end-page: 375
  ident: b0045
  article-title: Abnormal cation composition and transport in erythrocytes from hypertensive patients
  publication-title: Eur. J. Clin. Invest.
– volume: 68
  start-page: 1755
  year: 2011
  end-page: 1768
  ident: b0030
  article-title: Tubulin pools in human erythrocytes: altered distribution in hypertensive patients affects Na(+), K (+)-ATPase activity
  publication-title: Cell. Mol. Life Sci.
– volume: 38
  start-page: 779
  year: 1984
  end-page: 789
  ident: b0025
  article-title: Distinct populations of microtubules: tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo
  publication-title: Cell
– volume: 63
  start-page: 35
  year: 1985
  end-page: 37
  ident: b0150
  article-title: Sodium transport and red cell deformability
  publication-title: Klin. Wochenschr.
– volume: 174
  start-page: 839
  year: 2006
  end-page: 849
  ident: b0035
  article-title: Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends
  publication-title: J. Cell Biol.
– volume: 9
  start-page: 369
  year: 1979
  end-page: 375
  article-title: Abnormal cation composition and transport in erythrocytes from hypertensive patients
  publication-title: Eur. J. Clin. Invest.
– volume: 226
  start-page: 311
  year: 1985
  end-page: 317
  article-title: Release of C-terminal tyrosine from tubulin and microtubules at steady state
  publication-title: Biochem. J.
– volume: 4
  start-page: 687
  year: 1988
  end-page: 716
  article-title: Structure and utilization of tubulin isotypes
  publication-title: Annu. Rev. Cell Biol.
– volume: 35
  start-page: 63
  year: 2001
  end-page: 68
  article-title: Hemorreología comparativa. Estudio en diabéticos e hipertensos
  publication-title: Acta Bioquim. Clin. Latinoam.
– volume: 38
  start-page: 779
  year: 1984
  end-page: 789
  article-title: Distinct populations of microtubules: tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo
  publication-title: Cell
– volume: 19
  start-page: 17
  year: 1978
  end-page: 21
  article-title: Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase
  publication-title: Mol. Cell. Biochem.
– volume: 9
  start-page: 18
  year: 1987
  end-page: 23
  article-title: Effects of diltiazem on cation transport across erythrocyte membranes of hypertensive humans
  publication-title: Hypertension
– volume: 109
  start-page: 439
  year: 1980
  end-page: 446
  article-title: Total tubulin and its aminoacylated and non-aminoacylated forms during the development of rat brain
  publication-title: Eur. J. Biochem.
– volume: 291
  start-page: 167
  year: 2006
  end-page: 174
  article-title: Tubulin must be acetylated in order to form a complex with membrane Na(+), K(+)-ATPase and to inhibit its enzyme activity
  publication-title: Mol. Cell. Biochem.
– volume: 35
  start-page: 15
  year: 2010
  end-page: 22
  article-title: Unique post-translational modifications in specialized microtubule architecture
  publication-title: Cell Struct. Funct.
– volume: 72
  start-page: 248
  year: 1976
  end-page: 254
  article-title: A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principles of dye-protein binding
  publication-title: Anal. Biochem.
– volume: 21
  start-page: 1241
  year: 1973
  end-page: 1251
  article-title: Incorporation of phenylalanine as a single unit into rat brain protein: reciprocal inhibition by phenylalanine and tyrosine of their respective incorporations
  publication-title: J. Neurochem.
– volume: 422
  start-page: 129
  year: 2009
  end-page: 137
  article-title: Acetylated tubulin associates with the fifth cytoplasmic domain of Na(+)/K(+)-ATPase: possible anchorage site of microtubules to the plasma membrane
  publication-title: Biochem. J.
– volume: 293
  start-page: 1206
  year: 2007
  end-page: 1215
  article-title: Effects of erythrocyte flexibility on microvascular perfusion and oxygenation during acute anemia
  publication-title: Am. J. Physiol. Heart Circ. Physiol.
– volume: 70
  start-page: 8127
  year: 2010
  end-page: 8137
  article-title: Epithelial-to-mesenchymal transition promotes tubulin detyrosination and microtentacles that enhance endothelial engagement
  publication-title: Cancer Res.
– volume: 105
  start-page: 251
  year: 1987
  end-page: 264
  article-title: Postpolymerization detyrosination of α-tubulin: a mechanism for subcellular differentiation of microtubules
  publication-title: J. Cell Biol.
– volume: 315
  start-page: 183
  year: 1996
  end-page: 187
  article-title: Purification of the synaptosomal plasma membrane (Ca2+/Mg2+)-ATPase from pig brain
  publication-title: Biochem. J.
– volume: 44
  start-page: 1203
  year: 2012
  end-page: 1213
  article-title: High glucose levels induce inhibition of Na, K-ATPase via stimulation of aldose reductase, formation of microtubules and formation of an acetylated tubulin/Na, K-ATPase complex
  publication-title: Int. J. Biochem. Cell Biol.
– volume: 63
  start-page: 35
  year: 1985
  end-page: 37
  article-title: Sodium transport and red cell deformability
  publication-title: Klin. Wochenschr.
– volume: 4
  start-page: 14
  year: 1991
  end-page: 19
  article-title: Arterial blood pressure. Correlation whit erythrocyte count, hematocrit and hemoglobin concentration
  publication-title: Am. J. Hypertens.
– volume: 216
  start-page: 85
  year: 2001
  end-page: 92
  article-title: Brain plasma membrane Na+, K+-ATPase is inhibited by acetylated tubulin
  publication-title: Mol. Cell. Biochem.
– volume: 68
  start-page: 1755
  year: 2011
  end-page: 1768
  article-title: Tubulin pools in human erythrocytes: altered distribution in hypertensive patients affects Na(+), K (+)-ATPase activity
  publication-title: Cell. Mol. Life Sci.
– volume: 31
  start-page: 205
  year: 1978
  end-page: 210
  article-title: Capability of tubulin and microtubules to incorporate and to release tyrosine and phenylalanine and the effect of the incorporation of these amino acids on tubulin assembly
  publication-title: J. Neurochem.
– volume: 50
  start-page: 373
  year: 1972
  end-page: 385
  article-title: A rapid method for quantitative determination of microtubule protein using DEAE-cellulose filters
  publication-title: Anal. Biochem.
– year: 2008
  article-title: C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients
  publication-title: Exp. Diab. Res.
– volume: 177
  start-page: 517
  year: 1988
  end-page: 522
  article-title: Relationship between the tyrosination state of tubulin and the activities of tubulin: tyrosine ligase and tubulin carboxypeptidase in rat muscle during development
  publication-title: Eur. J. Biochem.
– volume: 63
  start-page: 1046
  year: 1984
  end-page: 1055
  article-title: Red cell membrane and cation deficiency in Rh null syndrome
  publication-title: Blood
– volume: 269
  start-page: 19659
  year: 1994
  end-page: 19662
  article-title: Na , K -ATPase
  publication-title: J. Biol. Chem.
– volume: 10
  start-page: 259
  year: 1987
  end-page: 266
  article-title: Erythrocyte ghost, Na+, K+-ATPase and blood pressure
  publication-title: Hypertension
– volume: 174
  start-page: 839
  year: 2006
  end-page: 849
  article-title: Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends
  publication-title: J. Cell Biol.
– volume: 273
  start-page: 21744
  year: 1998
  end-page: 21751
  article-title: Phosphorylation region of the yeast plasma membrane H+-ATPase. Role in protein folding and biogenesis
  publication-title: J. Biol. Chem.
– volume: 227
  start-page: 680
  year: 1970
  end-page: 685
  article-title: Cleavage of structural proteins during the assembly of the head of bacteriophage T4
  publication-title: Nature
– volume: 71
  start-page: 511
  year: 2002
  end-page: 535
  article-title: Biochemistry of Na, K-ATPase
  publication-title: Annu. Rev. Biochem.
– volume: 67
  start-page: 3371
  year: 2007
  end-page: 3378
  article-title: Parthenolide inhibits tubulin carboxypeptidase activity
  publication-title: Cancer Res.
– volume: 30
  start-page: 1414
  year: 2012
  end-page: 1422
  article-title: Involvement of membrane tubulin in erythrocyte deformability and blood pressure
  publication-title: J. Hypertens.
– ident: e_1_2_6_30_1
  doi: 10.1182/blood.V63.5.1046.1046
– ident: e_1_2_6_29_1
  doi: 10.1097/HJH.0b013e328353b19a
– ident: e_1_2_6_15_1
  doi: 10.1083/jcb.105.1.251
– ident: e_1_2_6_21_1
  doi: 10.1042/bj2260311
– ident: e_1_2_6_35_1
  doi: 10.1146/annurev.biochem.71.102201.141218
– ident: e_1_2_6_25_1
  doi: 10.1152/ajpheart.00109.2007
– ident: e_1_2_6_10_1
  doi: 10.1111/j.1365-2362.1979.tb00898.x
– ident: e_1_2_6_24_1
  doi: 10.1042/bj3150183
– ident: e_1_2_6_20_1
  doi: 10.1016/0003-2697(72)90046-2
– ident: e_1_2_6_23_1
  doi: 10.1111/j.1462-5822.2007.00901.x
– ident: e_1_2_6_6_1
  doi: 10.1016/0092-8674(84)90273-3
– ident: e_1_2_6_13_1
  doi: 10.1093/ajh/4.1.14
– ident: e_1_2_6_27_1
  doi: 10.1158/0008-5472.CAN-06-3732
– ident: e_1_2_6_19_1
  doi: 10.1111/j.1432-1033.1988.tb14402.x
– ident: e_1_2_6_34_1
  doi: 10.1016/S0021-9258(17)32067-7
– ident: e_1_2_6_17_1
  doi: 10.1042/BJ20082410
– ident: e_1_2_6_26_1
  doi: 10.1016/0003-2697(76)90527-3
– volume: 63
  start-page: 35
  year: 1985
  ident: e_1_2_6_31_1
  article-title: Sodium transport and red cell deformability
  publication-title: Klin. Wochenschr.
– ident: e_1_2_6_12_1
  doi: 10.1007/s11010-006-9212-9
– ident: e_1_2_6_2_1
  doi: 10.1146/annurev.cb.04.110188.003351
– ident: e_1_2_6_7_1
  doi: 10.1007/s00018-010-0549-6
– ident: e_1_2_6_4_1
  doi: 10.1111/j.1471-4159.1978.tb12449.x
– ident: e_1_2_6_18_1
  doi: 10.1111/j.1432-1033.1980.tb04813.x
– ident: e_1_2_6_33_1
  doi: 10.1247/csf.09027
– ident: e_1_2_6_28_1
  doi: 10.1016/j.biocel.2012.04.011
– ident: e_1_2_6_3_1
  doi: 10.1007/BF00231230
– ident: e_1_2_6_9_1
  doi: 10.1158/0008-5472.CAN-09-4613
– ident: e_1_2_6_22_1
  doi: 10.1074/jbc.273.34.21744
– ident: e_1_2_6_32_1
  doi: 10.1155/2008/730594
– ident: e_1_2_6_16_1
  doi: 10.1023/A:1011029125228
– ident: e_1_2_6_36_1
  doi: 10.1161/01.HYP.9.1.18
– ident: e_1_2_6_5_1
  doi: 10.1111/j.1471-4159.1973.tb07578.x
– ident: e_1_2_6_8_1
  doi: 10.1083/jcb.200512058
– ident: e_1_2_6_11_1
  doi: 10.1161/01.HYP.10.3.259
– volume: 35
  start-page: 63
  year: 2001
  ident: e_1_2_6_14_1
  article-title: Hemorreología comparativa. Estudio en diabéticos e hipertensos
  publication-title: Acta Bioquim. Clin. Latinoam.
SSID ssj0001819
Score 2.2406833
Snippet •Detyrosinated tubulin is able to inhibit the NKA activity.•Erythrocytes of hypertensive subjects have a reduced content and activity of TTL.•GluTub levels and...
Formation of tubulin/Na+,K+‐ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that...
Formation of tubulin/Na + ,K + ‐ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here...
Formation of tubulin/Na(+),K(+)-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here...
Formation of tubulin/Na+,K+-ATPase (NKA) complex in erythrocytes of hypertensive subjects results in a 50% reduction in NKA activity. We demonstrate here that...
SourceID proquest
pubmed
crossref
wiley
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 364
SubjectTerms acetylated tubulin
AcTub
Adult
Detyrosinated tubulin
enzyme activity
Erythrocyte deformability
Erythrocyte Deformability - genetics
erythrocytes
Erythrocytes - enzymology
Erythrocytes - pathology
Female
GluTub
Human erythrocytes
Humans
Hypertension
Hypertension - genetics
Hypertension - metabolism
Hypertension - pathology
Male
Middle Aged
Na+,K+-ATPase
NKA
PAGE
phenylmethylsulfonyl fluoride
PMSF
polyacrylamide gel electrophoresis
sodium-potassium-exchanging ATPase
Sodium-Potassium-Exchanging ATPase - genetics
Sodium-Potassium-Exchanging ATPase - metabolism
TTCP
TTL
tubulin
Tubulin - metabolism
tubulin tyrosine carboxypeptidase
tubulin tyrosine ligase
tyrosinated tubulin
tyrosine
Tyrosine - metabolism
TyrTub
Title Effects of detyrosinated tubulin on Na+,K+-ATPase activity and erythrocyte function in hypertensive subjects
URI https://dx.doi.org/10.1016/j.febslet.2014.12.022
https://onlinelibrary.wiley.com/doi/abs/10.1016%2Fj.febslet.2014.12.022
https://www.ncbi.nlm.nih.gov/pubmed/25541490
https://www.proquest.com/docview/1652399605
https://www.proquest.com/docview/1673380407
https://www.proquest.com/docview/2000210377
Volume 589
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3da9swEBddx9hextbuI_sIGoy9dE5sS5bsRyc0lIWVMVqWNyFZEk3pnBI7D3nZ3747f2SU0nXszdg6I99J9-X76Qj5CDZHGC1NII3jAefMBjpiIvCZC4tMRzxp2gF9PRUn5_zLIlnskWmPhcGyyk73tzq90dbdnXHHzfH1cokYX3xTxiBEwOJCBPwynjYgvsVkp43BgrUucMQDHP0HxTO-HHlnKmAPVnjxJisYx3fZp9v-5013trFHs2fkaedI0ryd63Oy58oDcpiXEET_3NJPtCntbHLmB-TRpL96PO0bvB2Sq_bk4oquPLWu3sJ8lkDuLK03BgvU6aqkp_ro8_woyM--gbmjiILAZhNUl5a69RabLBTb2lE0jyhiClQXENquu8J4Wm0MZnqqF-R8dnw2PQm65gtBIVKGSUYZm9Q6ERlhhI-klEwzWRTMc2FkYjJgWgL-Q1qkJoSHznu4zdJYu8TpkL0k--WqdK8JFdqCm5NF2riQ29im1oc-M0kW2lj4LB0Q3rNcFd3J5Ngg40r1JWiXqpOUQkmpKFYgqQEZ7ciu26M57iNIe3mqG2tMgfm4j_RDL38FUsKfKrp0q02lIpEgPBiiwr-NkYyloC7l3WMQMhUjaBPGvGoX2O6rIOzjEMmGA5I3K-7fPlfNjifxrV3y5v-Z8JY8QZljAoqF78h-vd649-CS1WZIHox-RUPyMJ9__zEfNjvwNySLMzw
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnR3LbtswTOg6DN1l2No9sqcGDLt0TmxLluRjGjTI1jbYIQV6EyRLQlN0TpE4h1z27SP9aFEUXYfdDJk0JFIUHyZFQr6AzhHWSBtJ63nEOXORSZiIQu7jIjcJz-p2QCdTMTnlP86ysy0y6mphMK2yPfubM70-rduRQUvNwdV8jjW--KWcgYuAyYXqEXnMQXxROvu_b_I8QIU1NnDCIwS_KeMZXPSDtyugD6Z48TosmKb3Kai7Buhte7ZWSOPn5FlrSdJhM9kXZMuXu2RvWIIX_WtDv9I6t7MOmu-SJwfd086o6_C2Ry6bq4tXdBGo89UG5jMHdO9otbaYoU4XJZ2a_W9H-9Fw9hP0HcUyCOw2QU3pqF9usMtCsak8Rf2IPKaAdQ6-7bLNjKertcVQz-olOR0fzkaTqO2-EBVCMYwyytQq50VihRUhkVIyw2RRsMCFlZnNgWgZGBCqUDaGlz4EGGYqNT7zJmavyHa5KP0bQoVxYOfkibE-5i51yoU45DbLY5eKkKse4R3JddFeTY4dMi51l4N2oVtOaeSUTlINnOqR_jXaVXM3x0MIquOnvrXJNOiPh1A_d_zXwCX8q2JKv1ivdCIyrA8Gt_BvMJIxBeelvB8Ga6ZSrNoEmNfNBrteFfh9HFzZuEeG9Y77t-Xq8eFBekdM3v4_ET6Rncns5Fgff58evSNPkf8YjWLxe7JdLdf-A9hnlf1Yy98fmLAzrQ
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=Effects+of+detyrosinated+tubulin+on+Na%2B%2CK%2B%E2%80%90ATPase+activity+and+erythrocyte+function+in+hypertensive+subjects&rft.jtitle=FEBS+letters&rft.au=Amaiden%2C+Marina+R.&rft.au=Santander%2C+Ver%C3%B3nica+S.&rft.au=Monesterolo%2C+Noelia+E.&rft.au=Nigra%2C+Ayelen+D.&rft.date=2015-01-30&rft.issn=0014-5793&rft.eissn=1873-3468&rft.volume=589&rft.issue=3&rft.spage=364&rft.epage=373&rft_id=info:doi/10.1016%2Fj.febslet.2014.12.022&rft.externalDBID=10.1016%252Fj.febslet.2014.12.022&rft.externalDocID=FEB2S0014579314009028
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0014-5793&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0014-5793&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0014-5793&client=summon