Isoforms of U1-70k control subunit dynamics in the human spliceosomal U1 snRNP

Most human protein-encoding genes contain multiple exons that are spliced together, frequently in alternative arrangements, by the spliceosome. It is established that U1 snRNP is an essential component of the spliceosome, in human consisting of RNA and ten proteins, several of which are post-transla...

Full description

Saved in:
Bibliographic Details
Published inPloS one Vol. 4; no. 9; p. e7202
Main Authors Hernández, Helena, Makarova, Olga V, Makarov, Evgeny M, Morgner, Nina, Muto, Yutaka, Krummel, Daniel Pomeranz, Robinson, Carol V
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 28.09.2009
Public Library of Science (PLoS)
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Most human protein-encoding genes contain multiple exons that are spliced together, frequently in alternative arrangements, by the spliceosome. It is established that U1 snRNP is an essential component of the spliceosome, in human consisting of RNA and ten proteins, several of which are post-translationally modified and exist as multiple isoforms. Unresolved and challenging to investigate are the effects of these post translational modifications on the dynamics, interactions and stability of the particle. Using mass spectrometry we investigate the composition and dynamics of the native human U1 snRNP and compare native and recombinant complexes to isolate the effects of various subunits and isoforms on the overall stability. Our data reveal differential incorporation of four protein isoforms and dynamic interactions of subunits U1-A, U1-C and Sm-B/B'. Results also show that unstructured post-translationally modified C-terminal tails are responsible for the dynamics of Sm-B/B' and U1-C and that their interactions with the Sm core are controlled by binding to different U1-70k isoforms and their phosphorylation status in vivo. These results therefore provide the important functional link between proteomics and structure as well as insight into the dynamic quaternary structure of the native U1 snRNP important for its function.
AbstractList Most human protein-encoding genes contain multiple exons that are spliced together, frequently in alternative arrangements, by the spliceosome. It is established that U1 snRNP is an essential component of the spliceosome, in human consisting of RNA and ten proteins, several of which are post-translationally modified and exist as multiple isoforms. Unresolved and challenging to investigate are the effects of these post translational modifications on the dynamics, interactions and stability of the particle. Using mass spectrometry we investigate the composition and dynamics of the native human U1 snRNP and compare native and recombinant complexes to isolate the effects of various subunits and isoforms on the overall stability. Our data reveal differential incorporation of four protein isoforms and dynamic interactions of subunits U1-A, U1-C and Sm-B/B'. Results also show that unstructured post-translationally modified C-terminal tails are responsible for the dynamics of Sm-B/B' and U1-C and that their interactions with the Sm core are controlled by binding to different U1-70k isoforms and their phosphorylation status in vivo. These results therefore provide the important functional link between proteomics and structure as well as insight into the dynamic quaternary structure of the native U1 snRNP important for its function.
Most human protein-encoding genes contain multiple exons that are spliced together, frequently in alternative arrangements, by the spliceosome. It is established that U1 snRNP is an essential component of the spliceosome, in human consisting of RNA and ten proteins, several of which are post-translationally modified and exist as multiple isoforms. Unresolved and challenging to investigate are the effects of these post translational modifications on the dynamics, interactions and stability of the particle. Using mass spectrometry we investigate the composition and dynamics of the native human U1 snRNP and compare native and recombinant complexes to isolate the effects of various subunits and isoforms on the overall stability. Our data reveal differential incorporation of four protein isoforms and dynamic interactions of subunits U1-A, U1-C and Sm-B/B'. Results also show that unstructured post-translationally modified C-terminal tails are responsible for the dynamics of Sm-B/B' and U1-C and that their interactions with the Sm core are controlled by binding to different U1-70k isoforms and their phosphorylation status in vivo . These results therefore provide the important functional link between proteomics and structure as well as insight into the dynamic quaternary structure of the native U1 snRNP important for its function.
Audience Academic
Author Robinson, Carol V
Makarov, Evgeny M
Morgner, Nina
Krummel, Daniel Pomeranz
Makarova, Olga V
Hernández, Helena
Muto, Yutaka
AuthorAffiliation 3 Division of Bioscience, School of Health and Social Care, Brunel University, Uxbridge, United Kingdom
4 MRC Laboratory of Molecular Biology, Cambridge, United Kingdom
2 Department of Biochemistry, University of Leicester, Leicester, United Kingdom
1 Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
University Paris 7, France
AuthorAffiliation_xml – name: 1 Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
– name: 3 Division of Bioscience, School of Health and Social Care, Brunel University, Uxbridge, United Kingdom
– name: 2 Department of Biochemistry, University of Leicester, Leicester, United Kingdom
– name: 4 MRC Laboratory of Molecular Biology, Cambridge, United Kingdom
– name: University Paris 7, France
Author_xml – sequence: 1
  givenname: Helena
  surname: Hernández
  fullname: Hernández, Helena
  organization: Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
– sequence: 2
  givenname: Olga V
  surname: Makarova
  fullname: Makarova, Olga V
– sequence: 3
  givenname: Evgeny M
  surname: Makarov
  fullname: Makarov, Evgeny M
– sequence: 4
  givenname: Nina
  surname: Morgner
  fullname: Morgner, Nina
– sequence: 5
  givenname: Yutaka
  surname: Muto
  fullname: Muto, Yutaka
– sequence: 6
  givenname: Daniel Pomeranz
  surname: Krummel
  fullname: Krummel, Daniel Pomeranz
– sequence: 7
  givenname: Carol V
  surname: Robinson
  fullname: Robinson, Carol V
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19784376$$D View this record in MEDLINE/PubMed
BookMark eNqNkluP0zAQhSO0iL3AP0AQCQnEQ4pviZsXpNWKS6XVLlpYXi3HnrQujl0yCWL_PS4N0CIeUB4STb5zxp45p9lRiAGy7DElM8olfbWOYx-0n21SeUYIkYywe9kJrTkrKkb40d73cXaKuCak5POqepAd01rOBZfVSXa1wNjGvsM8tvktLST5kpsYhj76HMdmDG7I7V3QnTOYu5APK8hXY6dDjhvvDESMnfZJmWO4ufrwMLvfao_waHqfZbdv33y6eF9cXr9bXJxfFkayeigEMwIYECu41ZzRyjJSGqgBrOFlKVjZMLBApLCcU962zFR1YxsJBGxran6WPd35bnxENY0CFWU1Y0wSIROx2BE26rXa9K7T_Z2K2qmfhdgvle4HZzwoqcu54Q2RphWC1I2mwpLUrDSkrDno5PV66jY2XToipPlof2B6-Ce4lVrGb4pJIQmdJ4MXk0Efv46Ag-ocGvBeB4gjKskFqXhaYCKf_UX--3KzHbXU6fwutDG1NemxkBaVAtG6VD8Xks3LJOJJ8PJAsF0xfB-WekRUi483_89efz5kn--xK9B-WGH04-BiwENQ7EDTR8Qe2t_To0Rt8_zrnmqbZzXlOcme7E_-j2gKMP8BS8nyAg
CitedBy_id crossref_primary_10_1093_nar_gkr1056
crossref_primary_10_1016_j_sbi_2011_08_002
crossref_primary_10_1016_j_sbi_2011_12_003
crossref_primary_10_1073_pnas_1106261108
crossref_primary_10_1073_pnas_2018251118
crossref_primary_10_1038_onc_2012_38
crossref_primary_10_1021_acs_analchem_0c05373
crossref_primary_10_1038_nmeth0210_157
crossref_primary_10_1016_j_jprot_2012_04_030
crossref_primary_10_1016_j_molcel_2019_08_007
crossref_primary_10_1016_j_sbi_2016_09_008
crossref_primary_10_1074_mcp_R111_014027
crossref_primary_10_1073_pnas_2315259121
crossref_primary_10_1016_j_str_2010_08_006
crossref_primary_10_1016_j_str_2010_11_009
crossref_primary_10_1021_ac300056a
crossref_primary_10_1126_science_1210148
crossref_primary_10_1021_acs_chemrev_1c00696
crossref_primary_10_1016_j_jprot_2020_103799
crossref_primary_10_1016_j_chroma_2011_05_094
crossref_primary_10_1016_j_bbagen_2017_09_019
crossref_primary_10_1093_nar_gkac636
crossref_primary_10_3109_10409238_2011_559451
crossref_primary_10_1016_j_cplett_2011_11_014
crossref_primary_10_1080_15476286_2021_1872963
crossref_primary_10_1016_j_trechm_2021_03_007
crossref_primary_10_1016_j_molcel_2013_08_020
crossref_primary_10_1002_pro_2661
crossref_primary_10_1007_s00425_023_04132_0
crossref_primary_10_1042_BST20210325
crossref_primary_10_1002_wrna_1257
crossref_primary_10_1007_s12127_013_0121_9
crossref_primary_10_1261_rna_037044_112
crossref_primary_10_3390_cryst11080948
crossref_primary_10_1002_pmic_201000287
crossref_primary_10_1146_annurev_physchem_040214_121732
crossref_primary_10_1016_j_tibs_2010_04_007
crossref_primary_10_1111_j_1742_4658_2011_08460_x
Cites_doi 10.1093/nass/1.1.275
10.1017/S135583820101442X
10.1073/pnas.95.18.10602
10.1101/sqb.2006.71.001
10.1073/pnas.0800406105
10.1002/j.1460-2075.1989.tb08563.x
10.1016/j.jasms.2008.05.018
10.1128/MCB.19.10.6554
10.1261/rna.2136103
10.1016/j.cell.2006.09.026
10.1038/nature01031
10.1016/j.molcel.2006.11.019
10.1016/S0021-9258(18)42475-1
10.1016/S0092-8674(00)80550-4
10.1371/journal.pbio.0040267
10.1016/S1097-2765(03)00270-3
10.1016/j.cell.2009.02.009
10.1038/nprot.2007.73
10.1016/j.molcel.2006.12.019
10.1038/nature07851
10.1074/jbc.273.32.20629
10.1074/jbc.M000300200
10.1038/sj.embor.embor863
10.1146/annurev.biophys.35.040405.101953
10.1002/j.1460-2075.1993.tb05689.x
10.1016/0092-8674(86)90072-3
10.1074/jbc.M409587200
10.1073/pnas.0805139105
10.1002/j.1460-2075.1994.tb06729.x
10.1096/fasebj.14.2.231
10.1021/ja061468q
10.1093/nar/24.23.4614
10.1016/0378-1119(91)90069-N
10.1016/j.cell.2006.10.037
10.1016/S0968-0004(00)01604-2
10.1093/nar/15.24.10373
10.1093/nar/8.18.4143
10.1038/sj.embor.7400702
10.1074/jbc.M208966200
10.1021/pr070152u
10.1016/j.jmb.2004.04.078
10.1016/j.bbrc.2004.08.107
10.1101/gad.11.3.334
10.1038/363283a0
10.1093/nar/gkn658
10.1038/sj.cdd.4402312
10.1016/0092-8674(90)90021-6
10.1016/0092-8674(89)90175-X
10.1073/pnas.0801313105
10.1021/ac0110552
10.1021/ar700218q
10.1016/j.str.2008.10.012
10.1016/j.autrev.2005.02.003
10.1021/ja0211508
10.1093/nar/11.5.1475
10.1002/j.1460-2075.1996.tb00579.x
10.1038/nbt1240
10.1038/nature06942
ContentType Journal Article
Copyright COPYRIGHT 2009 Public Library of Science
2009 Hernández et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Hernández et al. 2009
Copyright_xml – notice: COPYRIGHT 2009 Public Library of Science
– notice: 2009 Hernández et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: Hernández et al. 2009
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
IOV
ISR
3V.
7QG
7QL
7QO
7RV
7SN
7SS
7T5
7TG
7TM
7U9
7X2
7X7
7XB
88E
8AO
8C1
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABJCF
ABUWG
AFKRA
ARAPS
ATCPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
D1I
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
KB.
KB0
KL.
L6V
LK8
M0K
M0S
M1P
M7N
M7P
M7S
NAPCQ
P5Z
P62
P64
PATMY
PDBOC
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
PTHSS
PYCSY
RC3
7X8
5PM
DOA
DOI 10.1371/journal.pone.0007202
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Opposing Viewpoints Resource Center
Science in Context
ProQuest Central (Corporate)
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Biotechnology Research Abstracts
ProQuest Nursing & Allied Health Database
Ecology Abstracts
Entomology Abstracts (Full archive)
Immunology Abstracts
Meteorological & Geoastrophysical Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Agricultural Science Collection
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Public Health Database (Proquest)
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Materials Science & Engineering Collection
ProQuest Central (Alumni)
ProQuest Central
Advanced Technologies & Aerospace Collection
Agricultural & Environmental Science Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
ProQuest Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Materials Science Collection
ProQuest Central Korea
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Materials Science Database
Nursing & Allied Health Database (Alumni Edition)
Meteorological & Geoastrophysical Abstracts - Academic
ProQuest Engineering Collection
Biological Sciences
Agriculture Science Database
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Database
Engineering Database
Nursing & Allied Health Premium
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Environmental Science Database
Materials Science Collection
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Engineering Collection
Environmental Science Collection
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Agricultural Science Database
Publicly Available Content Database
ProQuest Central Student
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
ProQuest Central China
Environmental Sciences and Pollution Management
Health Research Premium Collection
Meteorological & Geoastrophysical Abstracts
Natural Science Collection
Biological Science Collection
ProQuest Medical Library (Alumni)
Engineering Collection
Advanced Technologies & Aerospace Collection
Engineering Database
Virology and AIDS Abstracts
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Agricultural Science Collection
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Environmental Science Collection
Entomology Abstracts
Nursing & Allied Health Premium
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Environmental Science Database
ProQuest Nursing & Allied Health Source (Alumni)
Engineering Research Database
ProQuest One Academic
Meteorological & Geoastrophysical Abstracts - Academic
Technology Collection
Technology Research Database
Materials Science Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
Genetics Abstracts
ProQuest Engineering Collection
Biotechnology Research Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Agricultural & Environmental Science Collection
AIDS and Cancer Research Abstracts
Materials Science Database
ProQuest Materials Science Collection
ProQuest Public Health
ProQuest Nursing & Allied Health Source
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Animal Behavior Abstracts
Materials Science & Engineering Collection
Immunology Abstracts
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList Agricultural Science Database



MEDLINE


Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  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: 3
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 4
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
DocumentTitleAlternate Subunit Dynamics of U1snRNP
EISSN 1932-6203
Editor Mayer, Claudine
Editor_xml – sequence: 1
  givenname: Claudine
  surname: Mayer
  fullname: Mayer, Claudine
EndPage e7202
ExternalDocumentID 1292227047
oai_doaj_org_article_7a58c3b07cf4409ba14d0db75c0593ea
2897684561
A472859223
10_1371_journal_pone_0007202
19784376
Genre Research Support, Non-U.S. Gov't
Journal Article
GrantInformation_xml – fundername: Biotechnology and Biological Sciences Research Council
– fundername: Biotechnology and Biological Sciences Research Council
  grantid: BB/C004272/1
– fundername: Medical Research Council
  grantid: MC_U105184330
GroupedDBID ---
123
29O
2WC
3V.
53G
5VS
7RV
7X2
7X7
7XC
88E
8AO
8C1
8CJ
8FE
8FG
8FH
8FI
8FJ
A8Z
AAFWJ
ABDBF
ABIVO
ABJCF
ABUWG
ACGFO
ACIHN
ACIWK
ACPRK
ADBBV
ADRAZ
AEAQA
AENEX
AFKRA
AFRAH
AHMBA
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
APEBS
ARAPS
ATCPS
BAWUL
BBNVY
BBORY
BCNDV
BENPR
BGLVJ
BHPHI
BKEYQ
BPHCQ
BVXVI
BWKFM
CCPQU
CGR
CS3
CUY
CVF
D1I
D1J
D1K
DIK
DU5
E3Z
EAP
EAS
EBD
ECM
EIF
EMOBN
ESTFP
ESX
EX3
F5P
FPL
FYUFA
GROUPED_DOAJ
GX1
HCIFZ
HH5
HMCUK
HYE
IAO
IEA
IHR
IHW
INH
INR
IOV
IPY
ISE
ISR
ITC
K6-
KB.
KQ8
L6V
LK5
LK8
M0K
M1P
M48
M7P
M7R
M7S
M~E
NAPCQ
NPM
O5R
O5S
OK1
P2P
P62
PATMY
PDBOC
PIMPY
PQQKQ
PROAC
PSQYO
PTHSS
PYCSY
RNS
RPM
SV3
TR2
UKHRP
WOQ
WOW
~02
~KM
AAYXX
CITATION
AFPKN
7QG
7QL
7QO
7SN
7SS
7T5
7TG
7TM
7U9
7XB
8FD
8FK
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
KL.
M7N
P64
PQEST
PQUKI
PRINS
RC3
7X8
5PM
-
02
AAPBV
ABPTK
ADACO
BBAFP
KM
ID FETCH-LOGICAL-c729t-42c4e2e0d43da3216d205ce9eedc355425b2ede074d3313ff2c69bdb7e0edfc93
IEDL.DBID RPM
ISSN 1932-6203
IngestDate Fri Nov 26 17:12:29 EST 2021
Tue Oct 22 15:15:53 EDT 2024
Tue Sep 17 21:23:21 EDT 2024
Sat Oct 26 00:09:36 EDT 2024
Thu Oct 10 16:46:54 EDT 2024
Wed Nov 13 00:55:10 EST 2024
Thu Aug 01 19:23:33 EDT 2024
Thu Aug 01 19:41:50 EDT 2024
Tue Aug 20 22:14:44 EDT 2024
Thu Nov 21 21:19:12 EST 2024
Wed Oct 16 00:48:31 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 9
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
Creative Commons Attribution License
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c729t-42c4e2e0d43da3216d205ce9eedc355425b2ede074d3313ff2c69bdb7e0edfc93
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Conceived and designed the experiments: HH OM EM CVR. Performed the experiments: HH OM EM. Analyzed the data: HH NM CVR. Contributed reagents/materials/analysis tools: HH OM EM YM DPK. Wrote the paper: HH DPK CVR.
Current address: Department of Biochemistry, Brandeis University, Waltham, Massachusetts, United States of America
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2747018/
PMID 19784376
PQID 1292227047
PQPubID 1436336
PageCount e7202
ParticipantIDs plos_journals_1292227047
doaj_primary_oai_doaj_org_article_7a58c3b07cf4409ba14d0db75c0593ea
pubmedcentral_primary_oai_pubmedcentral_nih_gov_2747018
proquest_miscellaneous_734063202
proquest_journals_1292227047
gale_infotracacademiconefile_A472859223
gale_incontextgauss_ISR_A472859223
gale_incontextgauss_IOV_A472859223
gale_healthsolutions_A472859223
crossref_primary_10_1371_journal_pone_0007202
pubmed_primary_19784376
PublicationCentury 2000
PublicationDate 2009-09-28
PublicationDateYYYYMMDD 2009-09-28
PublicationDate_xml – month: 09
  year: 2009
  text: 2009-09-28
  day: 28
PublicationDecade 2000
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: San Francisco
– name: San Francisco, USA
PublicationTitle PloS one
PublicationTitleAlternate PLoS One
PublicationYear 2009
Publisher Public Library of Science
Public Library of Science (PLoS)
Publisher_xml – name: Public Library of Science
– name: Public Library of Science (PLoS)
References MS Jurica (ref2) 2003; 12
VA Raker (ref52) 1999; 19
A van Dam (ref19) 1989; 8
MT Bedford (ref50) 1998; 95
H Brahms (ref40) 2001; 7
M Sharon (ref25) 2006; 4
M Sharon (ref31) 2009; 17
SB Patel (ref8) 2008; 36
JD Dignam (ref57) 1983; 11
W Cao (ref11) 1998; 273
D Cheng (ref13) 2007; 25
CW Smith (ref55) 2000; 25
Y Muto (ref30) 2001; Suppl
SH Xiao (ref10) 1997; 11
Z Zhou (ref1) 2002; 419
DA Pomeranz Krummel (ref17) 2009; 458
F Sobott (ref58) 2002; 74
JC Jurchen (ref34) 2003; 125
MC Wahl (ref3) 2009; 136
C Uetrecht (ref29) 2008; 105
JV Olsen (ref42) 2006; 127
J Hamm (ref5) 1990; 62
N Dephoure (ref46) 2008; 105
J Tazi (ref12) 1993; 363
Q Liu (ref27) 2006; 127
IA Kaltashov (ref47) 2008; 19
G Donmez (ref56) 2007; 25
TB Miranda (ref39) 2004; 323
H Hernandez (ref24) 2006; 7
LR Yu (ref43) 2007; 6
D Hof (ref22) 2005; 4
H Hernández (ref35) 2006; 7
H Brahms (ref41) 2000; 275
C Kambach (ref18) 1999; 96
IW Mattaj (ref4) 1986; 46
C Schmauss (ref9) 1992; 267
M Zhou (ref26) 2008; 105
EO Hochleitner (ref38) 2005; 280
J Dieker (ref45) 2008; 15
Y Muto (ref51) 2004; 341
CL Hanson (ref36) 2003; 278
J Mouaikel (ref54) 2003; 4
DJ Battle (ref53) 2006; 71
CC Query (ref23) 1989; 57
CL Will (ref15) 1996; 24
C Branlant (ref33) 1980; 8
ED Levy (ref48) 2008; 453
TS McConnell (ref32) 2003; 9
SA Beausoleil (ref44) 2006; 24
RL Nelissen (ref14) 1994; 13
H Hernandez (ref59) 2007; 2
H Stark (ref16) 2006; 35
RA Spritz (ref21) 1987; 15
BK Kay (ref49) 2000; 14
U Fischer (ref6) 1993; 12
T Taverner (ref28) 2008; 41
JL Chu (ref20) 1991; 97
VA Raker (ref7) 1996; 15
AR McKay (ref37) 2006; 128
References_xml – volume: Suppl
  start-page: 275
  year: 2001
  ident: ref30
  article-title: Reconstitution of the spliceosomal U1 snRNP from all recombinant subunits and its characterisation by ionspray Q-tof mass-spectrometry.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nass/1.1.275
  contributor:
    fullname: Y Muto
– volume: 7
  start-page: 1531
  year: 2001
  ident: ref40
  article-title: Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.
  publication-title: Rna
  doi: 10.1017/S135583820101442X
  contributor:
    fullname: H Brahms
– volume: 95
  start-page: 10602
  year: 1998
  ident: ref50
  article-title: WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.95.18.10602
  contributor:
    fullname: MT Bedford
– volume: 71
  start-page: 313
  year: 2006
  ident: ref53
  article-title: The SMN complex: an assembly machine for RNPs.
  publication-title: Cold Spring Harb Symp Quant Biol
  doi: 10.1101/sqb.2006.71.001
  contributor:
    fullname: DJ Battle
– volume: 105
  start-page: 9216
  year: 2008
  ident: ref29
  article-title: High-resolution mass spectrometry of viral assemblies: molecular composition and stability of dimorphic hepatitis B virus capsids.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0800406105
  contributor:
    fullname: C Uetrecht
– volume: 8
  start-page: 3853
  year: 1989
  ident: ref19
  article-title: Cloned human snRNP proteins B and B' differ only in their carboxy-terminal part.
  publication-title: Embo J
  doi: 10.1002/j.1460-2075.1989.tb08563.x
  contributor:
    fullname: A van Dam
– volume: 19
  start-page: 1239
  year: 2008
  ident: ref47
  article-title: Do ionic charges in ESI MS provide useful information on macromolecular structure?
  publication-title: J Am Soc Mass Spectrom
  doi: 10.1016/j.jasms.2008.05.018
  contributor:
    fullname: IA Kaltashov
– volume: 19
  start-page: 6554
  year: 1999
  ident: ref52
  article-title: Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner.
  publication-title: Mol Cell Biol
  doi: 10.1128/MCB.19.10.6554
  contributor:
    fullname: VA Raker
– volume: 9
  start-page: 193
  year: 2003
  ident: ref32
  article-title: Assembly of the U1 snRNP involves interactions with the backbone of the terminal stem of U1 snRNA.
  publication-title: RNA
  doi: 10.1261/rna.2136103
  contributor:
    fullname: TS McConnell
– volume: 127
  start-page: 635
  year: 2006
  ident: ref42
  article-title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
  publication-title: Cell
  doi: 10.1016/j.cell.2006.09.026
  contributor:
    fullname: JV Olsen
– volume: 419
  start-page: 182
  year: 2002
  ident: ref1
  article-title: Comprehensive proteomic analysis of the human spliceosome.
  publication-title: Nature
  doi: 10.1038/nature01031
  contributor:
    fullname: Z Zhou
– volume: 25
  start-page: 71
  year: 2007
  ident: ref13
  article-title: The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2006.11.019
  contributor:
    fullname: D Cheng
– volume: 267
  start-page: 8521
  year: 1992
  ident: ref9
  article-title: The gene encoding the small nuclear ribonucleoprotein-associated protein N is expressed at high levels in neurons.
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)42475-1
  contributor:
    fullname: C Schmauss
– volume: 96
  start-page: 375
  year: 1999
  ident: ref18
  article-title: Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs.
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80550-4
  contributor:
    fullname: C Kambach
– volume: 4
  start-page: 1314
  year: 2006
  ident: ref25
  article-title: Structural organization of the 19S proteasome lid: Insights from MS of intact complexes.
  publication-title: PLoS Biol
  doi: 10.1371/journal.pbio.0040267
  contributor:
    fullname: M Sharon
– volume: 12
  start-page: 5
  year: 2003
  ident: ref2
  article-title: Pre-mRNA splicing: awash in a sea of proteins.
  publication-title: Mol Cell
  doi: 10.1016/S1097-2765(03)00270-3
  contributor:
    fullname: MS Jurica
– volume: 136
  start-page: 701
  year: 2009
  ident: ref3
  article-title: The spliceosome: design principles of a dynamic RNP machine.
  publication-title: Cell
  doi: 10.1016/j.cell.2009.02.009
  contributor:
    fullname: MC Wahl
– volume: 2
  start-page: 715
  year: 2007
  ident: ref59
  article-title: Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry.
  publication-title: Nat Protoc
  doi: 10.1038/nprot.2007.73
  contributor:
    fullname: H Hernandez
– volume: 25
  start-page: 399
  year: 2007
  ident: ref56
  article-title: The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes.
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2006.12.019
  contributor:
    fullname: G Donmez
– volume: 458
  start-page: 475
  year: 2009
  ident: ref17
  article-title: Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.
  publication-title: Nature
  doi: 10.1038/nature07851
  contributor:
    fullname: DA Pomeranz Krummel
– volume: 273
  start-page: 20629
  year: 1998
  ident: ref11
  article-title: A serine/arginine-rich domain in the human U1 70 k protein is necessary and sufficient for ASF/SF2 binding.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.273.32.20629
  contributor:
    fullname: W Cao
– volume: 275
  start-page: 17122
  year: 2000
  ident: ref41
  article-title: The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M000300200
  contributor:
    fullname: H Brahms
– volume: 4
  start-page: 616
  year: 2003
  ident: ref54
  article-title: Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron.
  publication-title: EMBO Rep
  doi: 10.1038/sj.embor.embor863
  contributor:
    fullname: J Mouaikel
– volume: 35
  start-page: 435
  year: 2006
  ident: ref16
  article-title: Cryo-electron microscopy of spliceosomal components.
  publication-title: Annu Rev Biophys Biomol Struct
  doi: 10.1146/annurev.biophys.35.040405.101953
  contributor:
    fullname: H Stark
– volume: 12
  start-page: 573
  year: 1993
  ident: ref6
  article-title: Nucleo-cytoplasmic transport of U snRNPs: definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap.
  publication-title: Embo J
  doi: 10.1002/j.1460-2075.1993.tb05689.x
  contributor:
    fullname: U Fischer
– volume: 46
  start-page: 905
  year: 1986
  ident: ref4
  article-title: Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding.
  publication-title: Cell
  doi: 10.1016/0092-8674(86)90072-3
  contributor:
    fullname: IW Mattaj
– volume: 280
  start-page: 2536
  year: 2005
  ident: ref38
  article-title: Protein stoichiometry of a multiprotein complex, the human spliceosomal U1 small nuclear ribonucleoprotein: absolute quantification using isotope-coded tags and mass spectrometry.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M409587200
  contributor:
    fullname: EO Hochleitner
– volume: 105
  start-page: 10762
  year: 2008
  ident: ref46
  article-title: A quantitative atlas of mitotic phosphorylation.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0805139105
  contributor:
    fullname: N Dephoure
– volume: 13
  start-page: 4113
  year: 1994
  ident: ref14
  article-title: The association of the U1-specific 70 K and C proteins with U1 snRNPs is mediated in part by common U snRNP proteins.
  publication-title: Embo J
  doi: 10.1002/j.1460-2075.1994.tb06729.x
  contributor:
    fullname: RL Nelissen
– volume: 14
  start-page: 231
  year: 2000
  ident: ref49
  article-title: The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.
  publication-title: FASEB J
  doi: 10.1096/fasebj.14.2.231
  contributor:
    fullname: BK Kay
– volume: 128
  start-page: 11433
  year: 2006
  ident: ref37
  article-title: Mass Measurements of Increased Accuracy Resolve Heterogeneous Populations of Intact Ribosomes.
  publication-title: J Am Chem Soc
  doi: 10.1021/ja061468q
  contributor:
    fullname: AR McKay
– volume: 24
  start-page: 4614
  year: 1996
  ident: ref15
  article-title: In vitro reconstitution of mammalian U1 snRNPs active in splicing: the U1-C protein enhances the formation of early (E) spliceosomal complexes.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/24.23.4614
  contributor:
    fullname: CL Will
– volume: 97
  start-page: 311
  year: 1991
  ident: ref20
  article-title: The small nuclear ribonucleoproteins, SmB and B', are products of a single gene.
  publication-title: Gene
  doi: 10.1016/0378-1119(91)90069-N
  contributor:
    fullname: JL Chu
– volume: 127
  start-page: 1223
  year: 2006
  ident: ref27
  article-title: Reconstitution, activities, and structure of the eukaryotic RNA exosome.
  publication-title: Cell
  doi: 10.1016/j.cell.2006.10.037
  contributor:
    fullname: Q Liu
– volume: 25
  start-page: 381
  year: 2000
  ident: ref55
  article-title: Alternative pre-mRNA splicing: the logic of combinatorial control.
  publication-title: Trends Biochem Sci
  doi: 10.1016/S0968-0004(00)01604-2
  contributor:
    fullname: CW Smith
– volume: 15
  start-page: 10373
  year: 1987
  ident: ref21
  article-title: The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/15.24.10373
  contributor:
    fullname: RA Spritz
– volume: 8
  start-page: 4143
  year: 1980
  ident: ref33
  article-title: Nucleotide sequences of nuclear U1A RNAs from chicken, rat and man.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/8.18.4143
  contributor:
    fullname: C Branlant
– volume: 7
  start-page: 605
  year: 2006
  ident: ref35
  article-title: Subunit architecture of multimeric complexes isolated directly from cells.
  publication-title: EMBO Reports
  doi: 10.1038/sj.embor.7400702
  contributor:
    fullname: H Hernández
– volume: 278
  start-page: 1259
  year: 2003
  ident: ref36
  article-title: Dissociation of intact Escherichia coli ribosomes in a mass spectrometer. Evidence for conformational change in a ribosome elongation factor G complex.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M208966200
  contributor:
    fullname: CL Hanson
– volume: 6
  start-page: 4150
  year: 2007
  ident: ref43
  article-title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.
  publication-title: J Proteome Res
  doi: 10.1021/pr070152u
  contributor:
    fullname: LR Yu
– volume: 341
  start-page: 185
  year: 2004
  ident: ref51
  article-title: The structure and biochemical properties of the human spliceosomal protein U1C.
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2004.04.078
  contributor:
    fullname: Y Muto
– volume: 323
  start-page: 382
  year: 2004
  ident: ref39
  article-title: Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus.
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/j.bbrc.2004.08.107
  contributor:
    fullname: TB Miranda
– volume: 11
  start-page: 334
  year: 1997
  ident: ref10
  article-title: Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing.
  publication-title: Genes Dev
  doi: 10.1101/gad.11.3.334
  contributor:
    fullname: SH Xiao
– volume: 363
  start-page: 283
  year: 1993
  ident: ref12
  article-title: Thiophosphorylation of U1-70K protein inhibits pre-mRNA splicing.
  publication-title: Nature
  doi: 10.1038/363283a0
  contributor:
    fullname: J Tazi
– volume: 36
  start-page: 6482
  year: 2008
  ident: ref8
  article-title: The assembly of a spliceosomal small nuclear ribonucleoprotein particle.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/gkn658
  contributor:
    fullname: SB Patel
– volume: 15
  start-page: 793
  year: 2008
  ident: ref45
  article-title: Apoptosis-linked changes in the phosphorylation status and subcellular localization of the spliceosomal autoantigen U1-70K.
  publication-title: Cell Death Differ
  doi: 10.1038/sj.cdd.4402312
  contributor:
    fullname: J Dieker
– volume: 62
  start-page: 569
  year: 1990
  ident: ref5
  article-title: The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal.
  publication-title: Cell
  doi: 10.1016/0092-8674(90)90021-6
  contributor:
    fullname: J Hamm
– volume: 57
  start-page: 89
  year: 1989
  ident: ref23
  article-title: A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70 K U1 snRNP protein.
  publication-title: Cell
  doi: 10.1016/0092-8674(89)90175-X
  contributor:
    fullname: CC Query
– volume: 105
  start-page: 18139
  year: 2008
  ident: ref26
  article-title: Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0801313105
  contributor:
    fullname: M Zhou
– volume: 74
  start-page: 1402
  year: 2002
  ident: ref58
  article-title: A Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies.
  publication-title: Anal Chem
  doi: 10.1021/ac0110552
  contributor:
    fullname: F Sobott
– volume: 41
  start-page: 617
  year: 2008
  ident: ref28
  article-title: Subunit architecture of intact protein complexes from mass spectrometry and homology modeling.
  publication-title: Acc Chem Res
  doi: 10.1021/ar700218q
  contributor:
    fullname: T Taverner
– volume: 17
  start-page: 31
  year: 2009
  ident: ref31
  article-title: Symmetrical Modularity of the COP9 Signalosome Complex Suggests its Multifunctionality.
  publication-title: Structure
  doi: 10.1016/j.str.2008.10.012
  contributor:
    fullname: M Sharon
– volume: 4
  start-page: 380
  year: 2005
  ident: ref22
  article-title: Apoptotic modifications affect the autoreactivity of the U1 snRNP autoantigen.
  publication-title: Autoimmun Rev
  doi: 10.1016/j.autrev.2005.02.003
  contributor:
    fullname: D Hof
– volume: 125
  start-page: 2817
  year: 2003
  ident: ref34
  article-title: Origin of Asymmetric Charge Partitioning in the Dissociation of Gas-Phase Protein Homodimers.
  publication-title: J Am Chem Soc
  doi: 10.1021/ja0211508
  contributor:
    fullname: JC Jurchen
– volume: 7
  start-page: 605
  year: 2006
  ident: ref24
  article-title: Subunit architecture of multimeric complexes isolated directly from cells.
  publication-title: EMBO Rep
  doi: 10.1038/sj.embor.7400702
  contributor:
    fullname: H Hernandez
– volume: 11
  start-page: 1475
  year: 1983
  ident: ref57
  article-title: Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei.
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/11.5.1475
  contributor:
    fullname: JD Dignam
– volume: 15
  start-page: 2256
  year: 1996
  ident: ref7
  article-title: The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro.
  publication-title: Embo J
  doi: 10.1002/j.1460-2075.1996.tb00579.x
  contributor:
    fullname: VA Raker
– volume: 24
  start-page: 1285
  year: 2006
  ident: ref44
  article-title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
  publication-title: Nat Biotechnol
  doi: 10.1038/nbt1240
  contributor:
    fullname: SA Beausoleil
– volume: 453
  start-page: 1262
  year: 2008
  ident: ref48
  article-title: Assembly reflects evolution of protein complexes.
  publication-title: Nature
  doi: 10.1038/nature06942
  contributor:
    fullname: ED Levy
SSID ssj0053866
Score 2.2077267
Snippet Most human protein-encoding genes contain multiple exons that are spliced together, frequently in alternative arrangements, by the spliceosome. It is...
SourceID plos
doaj
pubmedcentral
proquest
gale
crossref
pubmed
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
StartPage e7202
SubjectTerms Biochemistry
Biochemistry/Experimental Biophysical Methods
Biochemistry/Macromolecular Assemblies and Machines
Biochemistry/RNA Structure
Catalysis
Dynamic stability
Dynamics
Exons
HeLa Cells
Humans
Isoforms
Laboratories
Mass spectrometry
Mass Spectrometry - methods
Mass spectroscopy
Molecular biology
Molecular Conformation
Phosphorylation
Post-translation
Post-translational modifications
Protein Isoforms
Protein Processing, Post-Translational
Protein structure
Protein Structure, Quaternary
Proteins
Proteomics
Proteomics - methods
Quaternary
Quaternary structure
Recombinant Proteins - chemistry
Ribonucleic acid
Ribonucleoprotein, U1 Small Nuclear - chemistry
Ribonucleoprotein, U1 Small Nuclear - metabolism
Ribonucleoproteins (small nuclear)
RNA
RNA - metabolism
RNA, Small Nuclear - metabolism
Scientific imaging
Spectrometry, Mass, Electrospray Ionization - methods
Spliceosomes - metabolism
Trends
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Nb9QwELXQnrggylcDBSyEBBxCHduJk2NBVC0SCyos6s3yV6ACkhXe_f_MxN6liyrBgVu0HmmTN574OeN5Q8hT7k1jjeBl51tfSmsFXGHOVTpYXmQfuoCFwu_mzclCvj2vzy-1-sIzYUkeOAF3qEzdOmGZcr2EvYg1lfTMW1U7bEYXEjVifLOZSu9giOKmyYVyQlWH2S8vl-MQULFQ8fwZZbMQTXr927fybPl9jFdRzj9PTl5aio5vkhuZQ9KjdO975FoYbpG9HKWRPs9S0i9uk_lpHJGVRjr2dFGVin2j-XA6jWu7hnimPvWkj_RioMAG6dS1j0bMa4cxjj_gnxYVjcPZ_MMdsjh-8-n1SZk7KJQOSPOqlNzJwAPzUnhwSNV4zmqH-HuHRIPXlgcfgEZ4ISrR99w1nUXFZRZ87zpxl8wGwGyf0Jr1sF1rW5RslY3xLbfcsL43UjSiqk1Byg2cepmEMvSULVOwwUi4aIRfZ_gL8gox39qizPX0AzhfZ-frvzm_II_RYzrVjG6DVR9JhcJ8QH0K8mSyQKmLAc_SfDHrGPXp-8__YPTxbMfoWTbqR_C9M7l-AZ4JJbR2LPdxAm0eO2rgVFhyzKQqyMFmUl09TLfDEOaYuzFDGNdRKwHMS0y43UtT8DfKnWolrBMFUTuTcwfa3ZHh4uukJI6fJFjV3v8fvnhArqdMW1fy9oDMVj_X4SEQtpV9NMXmL55iPhY
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Technology Collection
  dbid: 8FG
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Lb9QwELZguXBBlFcDBSyEBBxCE9uJkxMqhaVFYkEti3qzHD_aCkiWevf_M5M4WxZViNtqPVKSGY_9eR6fCXnOrC4bzVla28qmomk4_MKcqzCwvQjvaoeNwp9m5cFcfDwpTmLALcSyynFN7Bdq2xmMke_CvoRtm5mQbxa_Urw1CrOr8QqN6-RGzmSJJX3V9MO4EoMvl2Vsl-My343Web3oWoe8hZLFYMq4HfWs_eu1ebL40YWrgOff9ZN_bEjT2-RWRJJ0bzD9Frnm2jtkK_pqoC8jofSru2R2GDrEpoF2ns7zVGbf6f5Qok5h4ViBV9N3w830gZ63FDAh7YP79Biz264L3U940jynoT2afblH5tP3X_cP0niPQmoAOi9TwYxwzGVWcAtmyUvLssKgFaxBuMGKhjnrAExYznPuPTNl3SDvcuasNzW_TyYt6Gyb0CLzcGirKiRuFaW2FWuYzrzXgpc8L3RC0lGdajHQZag-ZybhmDHoRaH6VVR_Qt6izteySHbd_9FdnKroO0rqojK8yaTxAo6jjc6FzeD1CoP3ETp46FO0mBo6R9cuq_aERHo-AEAJedZLIOFFixU1p3oVgjr8_O0_hI6PNoReRCHfge2Njl0M8E1IpLUhuY0TaPzsoC5ncEJ2xkl19TBdD4OzYwZHt65bBSU54C_e6-3BMAUvtVzLSsBukRC5MTk3VLs50p6f9XziGJjI8urhv9_qEbk5ZNLqlFU7ZLK8WLnHAMiWzZPe634DHTU0jw
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3fb9MwELam8sILYvxaYICFkICHTI7txMkDQmMwbUgraCNob5ZjO2NiJKVuJfjvuUvSQlCR9lbFlyY-3_k-5-zvCHnOnckqI3hcuNzFsqoE_MKcq7QQXmTtC48HhU-m2VEpP5yn51tkVbN1UGDYuLTDelLl_Grv549fb8DhX3dVG1Syumlv1jYe-QgVR3bJGxxiI27yOpHrvAJ4d5e9RNQSZ5yJ4TDd__5lFKw6Tv_1zD2ZXbVhEyz9d3flX-Hq8Da5NeBMut8bxjbZ8s0dsj14cqAvB7rpV3fJ9Di0iFwDbWtaJrFi3-hBv4GdwrSyBJ-n7_q69YFeNhQQI-0-_dMzzH37NrTf4UllQkNzOv10j5SH7z8fHMVDlYXYArBexJJb6blnTgoHg5ZkjrPU4hg5i2CEpxX3zgPUcEIkoq65zYoKWZmZd7UtxH0yaUBnO4SmrIYlXZ4jravMjMt5xQ2rayNFJpLURCReqVPPejIN3WXUFCxCer1oVL8e1B-Rt6jztSxSYXcX2vmFHjxLK5PmVlRM2VrCYrUyiXQMXi-1WK3Qw0Of4ojp_lzp2qH1vlRI3gfwKCLPOgmkw2hwv82FWYagjz9-uYbQ2elI6MUgVLcw9tYMZxygT0izNZLcQQNadTtowF14LJlJFZHdlVFtbqbrZpgKML9jGt8ug1YC0Jno9PagN8E_Wi5ULiGWRESNjHOk2nFLc_m1YxvHzxYsyR9ep_-PyM0-21bEPN8lk8V86R8DaFtUTzo__A2qLz5G
  priority: 102
  providerName: Scholars Portal
Title Isoforms of U1-70k control subunit dynamics in the human spliceosomal U1 snRNP
URI https://www.ncbi.nlm.nih.gov/pubmed/19784376
https://www.proquest.com/docview/1292227047
https://search.proquest.com/docview/734063202
https://pubmed.ncbi.nlm.nih.gov/PMC2747018
https://doaj.org/article/7a58c3b07cf4409ba14d0db75c0593ea
http://dx.doi.org/10.1371/journal.pone.0007202
Volume 4
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwELa28sILYvxaYBQLIQEPaZPYidPHraxsSC1VR1HfrMR2too1qZb2_-fOccqK9oB4saL6qiR3Pvu7-O4zIR8inSV5xiJ_oFPt8zxncIV7rlzB8sILMzBYKDyeJBdz_m0RLw5I3NbC2KR9lS975e2qVy5vbG7leqX6bZ5YfzoeYiQVhGn_kBzC8tuG6M30Cw6cJK5Gjomw70zSW1elQbJCAdG-ZQoVKWfINHJvObKs_bu5ubO-reqHgOff-ZP3FqTRU_LEIUl62jzxETkw5TNy5Hy1pp8cofTn52RyWVeITWtaFXQe-iL4RYdNijqFiWMLXk2_NCfT13RZUsCE1H7cp1e4u22qulrBneYhrcvZZPqCzEfnP4YXvjtHwVcAnTc-jxQ3kQk0ZxrMEiY6CmKFVtAK4UYU55HRBsCEZixkRRGpZJAj73JgdKEG7CXplKC-Y0LjoICgLU2RuJUnmU6jPMqCosg4S1gYZx7xW3XKdUOXIe2emYAwo9GLREtIZwmPnKHOd7JIdm1_qO6upTO5FFmcKpYHQhUcwtE8C7kO4PFihecRGrjpO7SYbCpHdy4rT7lAej4AQB55byWQ8KLEjJrrbFvX8vL7z38QuprtCX10QkUFtleZq2KAd0IirT3JYxxA7WvXEpAVFh4HXHjkpB1UD3fTXTc4O-7gZKWptrUUDPAXs3p71QzBP1p2A9ojYm9w7ql2vwfcy_KJO3d6_d__fEMeN5tsAz9KT0hnc7c1bwGrbfIueOhCQJsOQ2xHX7vk0dn5ZDrr2q8f0I552rUe_BvwskOe
link.rule.ids 230,314,727,780,784,864,885,2102,2221,12056,12223,12765,21388,24318,27924,27925,31719,31720,33266,33267,33373,33374,33744,33745,43310,43579,43600,43805,53791,53793,73745,74014,74035,74302
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwELege4CXifG1wmAWQgIewhLbiZMntI1NK2xl6la0N8uxnTEBSZnb_5-7xOkomhBvVX1Skvvy-c73O0JeM6uzUnMWFTa3kShLDr-w5ioMbC-icoXDRuGTcXY0FZ8u0ouQcPPhWmXvE1tHbRuDOfId2JewbTMW8sPsV4RTo7C6GkZo3CVriJyeDsja3sH4dNL7YrDmLAsNc1wmO0E-72dN7RC5ULKQTuk3pBa3f-mdB7Mfjb8t9Pz7BuUfW9LhA7IeYkm62wl_g9xx9UOyEazV07cBUvrdIzIe-QajU0-bik6TSMbf6X53SZ2C61iAXdOP3Wx6T69qClEhbdP79Azr267xzU940jShvp6MTx-T6eHB-f5RFCYpRAaC53kkmBGOudgKbkEwSWZZnBqUgzUYcLC0ZM46CCcs5wmvKmayokTk5djZyhT8CRnUwLNNQtO4gmNbniN0q8i0zVnJdFxVWvCMJ6kekqhnp5p1gBmqrZpJOGh0fFHIfhXYPyR7yPMlLcJdt38015cqWI-SOs0NL2NpKgEH0lInwsbweqnBiYQOHrqNElNd7-jSaNWukAjQByHQkLxqKRDyosY7NZd64b0affn6H0RnkxWiN4GoakD2Roc-BvgmhNJaodxEBeo_26sbHR6SrV6pbl-my2Uwd6zh6No1C68khwiMt3x72qngDZcLmQvYL4ZErijnCmtXV-qrby2iOKYm4iR_9u-32ib3js5PjtXxaPz5Obnf1dWKiOVbZDC_XrgXEJ7Ny5fBBn8D5mA44A
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Zb9NAEF5BKiFeKspVQ6ErhAQ8mNi76-sJ9YoajhClBPVtZe9RKsAO3eT_M2OvU4IqxFuUHcn23Luz8w0hL5ku06rkLCx0rkNRVRx-Yc1VKAgvwprCYKPwp0l6Ohfvz5Nzf__J-WuVvU9sHbVuFJ6RDyEuYdtmJLKh9dcipsejd4tfIU6QwkqrH6dxm2xBVIzYgGwdnkyms94vg2WnqW-e41k89LJ6u2hqgyiGGfNHK31wajH81556sPjRuJvS0L9vU_4Rnkb3yLbPK-lBpwg75Jap75Mdb7mOvvbw0m8ekMnYNZipOtpYOo_DLPpOj7oL6xTcyApsnB53c-odvawpZIi0PeqnZ1jrNo1rfsKT5jF19WwyfUjmo5MvR6ehn6oQKkikl6FgShhmIi24BiHFqWZRolAmWmHywZKKGW0gtdCcx9xaptKiQhTmyGirCv6IDGrg2S6hSWRhC5fnCOMq0lLnrGJlZG0peMrjpAxI2LNTLjrwDNlW0DLYdHR8kch-6dkfkEPk-ZoWoa_bP5qrC-ktSWZlkiteRZmyAjanVRkLHcHrJQqnExp46D5KTHZ9pGsDlgciQ7A-SIcC8qKlQPiLGhXpolw5J8efv_4H0dlsg-iVJ7INyF6VvqcBvglhtTYod1GB-s928lqfA7LXK9XNy3S9DKaP9ZyyNs3KyYxDNsZbvj3uVPCay0WWC4gdAck2lHODtZsr9eW3Fl0cjymiOH_y77faJ3fA_OTH8eTDU3K3K7EVIcv3yGB5tTLPIFNbVs-9Cf4GodU9DQ
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=Isoforms+of+U1-70k+Control+Subunit+Dynamics+in+the+Human+Spliceosomal+U1+snRNP&rft.jtitle=PloS+one&rft.au=Hern%C3%A1ndez%2C+Helena&rft.au=Makarova%2C+Olga+V&rft.au=Makarov%2C+Evgeny+M&rft.au=Morgner%2C+Nina&rft.date=2009-09-28&rft.pub=Public+Library+of+Science&rft.issn=1932-6203&rft.eissn=1932-6203&rft.volume=4&rft.issue=9&rft.spage=e7202&rft_id=info:doi/10.1371%2Fjournal.pone.0007202&rft.externalDBID=ISR&rft.externalDocID=A472859223
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1932-6203&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1932-6203&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1932-6203&client=summon