Spatiotemporal variation of mammalian protein complex stoichiometries

Background Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted...

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Published inGenome Biology Vol. 17; no. 1; p. 47
Main Authors Ori, Alessandro, Iskar, Murat, Buczak, Katarzyna, Kastritis, Panagiotis, Parca, Luca, Andrés-Pons, Amparo, Singer, Stephan, Bork, Peer, Beck, Martin
Format Journal Article
LanguageEnglish
Published London BioMed Central 14.03.2016
Subjects
Acids
Animal Genetics and Genomics
Animals
Bioinformatics
Biomedical and Life Sciences
Cancer
Cell cycle
Cell Lineage - genetics
Chromatin
Chromatin - chemistry
Chromatin - genetics
Datasets
Evolutionary Biology
Gene expression
Genomics
Human Genetics
Humans
Life Sciences
Mammals
Microbial Genetics and Genomics
Multiprotein Complexes - chemistry
Multiprotein Complexes - genetics
neoplasm cells
neoplasms
Plant Genetics and Genomics
Protein expression
Protein Structure, Tertiary
Proteins
proteome
Proteome - genetics
Proteomes
Proteomics
spatial variation
Stem cells
Stoichiometry
temporal variation
Transcription
Transcription, Genetic
Variation
Protein complex
Stoichiometry
Reprogramming
Proteomics
Paralog
Epigenetic
Transport
Cancer
Online AccessGet full text
ISSN1474-760X
1474-7596
1474-760X
DOI10.1186/s13059-016-0912-5

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Abstract Background Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. Results We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. Conclusions Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.
AbstractList Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level.BACKGROUNDRecent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level.We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones.RESULTSWe used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones.Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.CONCLUSIONSOur work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.
Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.
BACKGROUND: Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. RESULTS: We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. CONCLUSIONS: Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.
Background Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. Results We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. Conclusions Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states.
ArticleNumber 47
Author Ori, Alessandro
Buczak, Katarzyna
Kastritis, Panagiotis
Bork, Peer
Parca, Luca
Andrés-Pons, Amparo
Iskar, Murat
Singer, Stephan
Beck, Martin
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/26975353$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1016/j.jmb.2003.10.069
10.1038/nsb1297-973
10.1016/j.molcel.2011.03.026
10.1016/0022-2836(71)90324-X
10.1038/nature13319
10.1186/gb-2013-14-11-r133
10.1038/nprot.2007.406
10.1016/j.devcel.2012.01.005
10.1016/j.cell.2014.02.033
10.1038/msb.2012.44
10.1038/nature04670
10.1007/0-387-29362-0_23
10.1016/j.cell.2011.05.006
10.1016/0022-2836(76)90191-1
10.1016/j.celrep.2014.07.002
10.1111/j.2517-6161.1995.tb02031.x
10.1093/nar/gkr913
10.1038/nature04532
10.1093/nar/gks1193
10.1074/mcp.M111.014050
10.1016/j.cell.2011.03.028
10.1038/msb.2013.4
10.1016/j.cell.2012.11.039
10.1101/gr.073585.107
10.1038/nprot.2010.32
10.1073/pnas.082099299
10.1038/nature13562
10.1016/j.cell.2011.08.044
10.1016/j.cell.2004.12.035
10.1126/scisignal.2003629
10.1038/nprot.2009.97
10.1016/j.cell.2012.08.011
10.1016/j.celrep.2012.10.014
10.1038/nature05186
10.1016/j.cell.2009.01.009
10.1016/j.cell.2013.02.036
10.1093/nar/gkp914
10.1038/ncb2390
10.1016/j.devcel.2011.11.021
10.1093/nar/gku1003
10.1038/nature13302
10.1093/nar/gkn1005
10.1016/j.cell.2007.08.037
10.1021/ja026939x
10.1093/bioinformatics/bth114
10.1093/nar/gku1081
10.1038/msb.2011.81
10.1093/nar/gkt1196
10.1093/biostatistics/4.2.249
10.1126/science.1105103
10.1093/nar/gkq1218
10.1021/ci4005332
10.1016/B978-0-12-417160-2.00006-0
10.1038/nbt.1862
10.1038/msb.2011.82
10.1073/pnas.0812889106
10.1021/pr9009854
10.1038/nature11247
10.1186/1471-2148-8-337
10.1021/ja00214a001
ContentType Journal Article
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2016. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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Issue 1
Keywords Protein complex
Stoichiometry
Reprogramming
Proteomics
Paralog
Epigenetic
Transport
Cancer
Language English
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References D Szklarczyk (912_CR59) 2015; 43
PL Kastritis (912_CR55) 2014; 54
PV Luc (912_CR37) 2004; 20
TL Lenstra (912_CR9) 2011; 42
Y Benjamini (912_CR46) 1995; 57
S Pu (912_CR38) 2009; 37
J Hansson (912_CR12) 2012; 2
M Wilhelm (912_CR1) 2014; 509
R Szklarczyk (912_CR34) 2008; 8
MS Kim (912_CR2) 2014; 509
SJ Vries de (912_CR50) 2010; 5
J Janin (912_CR47) 1997; 4
C Kadoch (912_CR24) 2013; 153
T Barrett (912_CR43) 2013; 41
JM Polo (912_CR22) 2012; 151
A Ori (912_CR10) 2013; 9
JR Wisniewski (912_CR30) 2012; 8
P Flicek (912_CR40) 2014; 42
BP Lewis (912_CR56) 2005; 120
MA D’Angelo (912_CR21) 2012; 22
CS Yang (912_CR29) 2014; 8
NJ Krogan (912_CR4) 2006; 440
JI Wu (912_CR26) 2009; 136
GK Smyth (912_CR45) 2005
G Zanetti (912_CR33) 2012; 14
M Beck (912_CR16) 2011; 7
B Lee (912_CR48) 1971; 55
S Durinck (912_CR41) 2009; 4
A Ruepp (912_CR14) 2010; 38
RA Irizarry (912_CR44) 2003; 4
J Fernandez-Recio (912_CR53) 2004; 335
PL Kastritis (912_CR51) 2010; 9
J Parenteau (912_CR36) 2011; 147
T Geiger (912_CR13) 2012; 11
PC Havugimana (912_CR5) 2012; 150
S Komili (912_CR35) 2007; 131
L Pan (912_CR23) 2014; 514
AT Brunger (912_CR54) 2007; 2
AC Gavin (912_CR3) 2006; 440
M Kapushesky (912_CR42) 2012; 40
N Nagaraj (912_CR17) 2011; 7
A Ori (912_CR57) 2014; 122
L Ho (912_CR27) 2009; 106
PJ Rugg-Gunn (912_CR32) 2012; 22
AJ Vilella (912_CR39) 2009; 19
A Vinayagam (912_CR15) 2013; 6
ENCODE Project Consortium (912_CR31) 2012; 489
MG Kearse (912_CR20) 2011; 39
P Minguez (912_CR60) 2015; 43
A Malovannaya (912_CR6) 2011; 145
C Dominguez (912_CR25) 2003; 125
N Kondrashov (912_CR19) 2011; 145
U Lichtenberg de (912_CR7) 2005; 307
C Chothia (912_CR49) 1976; 105
R Tibshirani (912_CR58) 2002; 99
C Jüschke (912_CR11) 2013; 14
D Subramanyam (912_CR28) 2011; 29
LJ Jensen (912_CR8) 2006; 443
G-W Li (912_CR18) 2014; 157
W Jorgensen (912_CR52) 1988; 110
26975421 - Genome Biol. 2016;17:48
References_xml – volume: 335
  start-page: 843
  year: 2004
  ident: 912_CR53
  publication-title: J Mol Biol.
  doi: 10.1016/j.jmb.2003.10.069
– volume: 4
  start-page: 973
  year: 1997
  ident: 912_CR47
  publication-title: Nat Struct Biol.
  doi: 10.1038/nsb1297-973
– volume: 42
  start-page: 536
  year: 2011
  ident: 912_CR9
  publication-title: Mol Cell.
  doi: 10.1016/j.molcel.2011.03.026
– volume: 55
  start-page: 379
  year: 1971
  ident: 912_CR48
  publication-title: J Mol Biol.
  doi: 10.1016/0022-2836(71)90324-X
– volume: 509
  start-page: 582
  year: 2014
  ident: 912_CR1
  publication-title: Nature.
  doi: 10.1038/nature13319
– volume: 14
  start-page: r133
  year: 2013
  ident: 912_CR11
  publication-title: Genome Biol.
  doi: 10.1186/gb-2013-14-11-r133
– volume: 2
  start-page: 2728
  year: 2007
  ident: 912_CR54
  publication-title: Nat Protoc
  doi: 10.1038/nprot.2007.406
– volume: 22
  start-page: 887
  year: 2012
  ident: 912_CR32
  publication-title: Dev Cell.
  doi: 10.1016/j.devcel.2012.01.005
– volume: 157
  start-page: 624
  year: 2014
  ident: 912_CR18
  publication-title: Cell.
  doi: 10.1016/j.cell.2014.02.033
– volume: 8
  start-page: 611
  year: 2012
  ident: 912_CR30
  publication-title: Mol Syst Biol.
  doi: 10.1038/msb.2012.44
– volume: 440
  start-page: 637
  year: 2006
  ident: 912_CR4
  publication-title: Nature.
  doi: 10.1038/nature04670
– start-page: 397
  volume-title: Bioinformatics and Computational Biology Solutions Using R and Bioconductor
  year: 2005
  ident: 912_CR45
  doi: 10.1007/0-387-29362-0_23
– volume: 145
  start-page: 787
  year: 2011
  ident: 912_CR6
  publication-title: Cell.
  doi: 10.1016/j.cell.2011.05.006
– volume: 105
  start-page: 1
  year: 1976
  ident: 912_CR49
  publication-title: J Mol Biol.
  doi: 10.1016/0022-2836(76)90191-1
– volume: 8
  start-page: 327
  year: 2014
  ident: 912_CR29
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.07.002
– volume: 57
  start-page: 289
  year: 1995
  ident: 912_CR46
  publication-title: J R Stat Soc Ser B Methodol.
  doi: 10.1111/j.2517-6161.1995.tb02031.x
– volume: 40
  start-page: D1077
  year: 2012
  ident: 912_CR42
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkr913
– volume: 440
  start-page: 631
  year: 2006
  ident: 912_CR3
  publication-title: Nature.
  doi: 10.1038/nature04532
– volume: 41
  start-page: D991
  year: 2013
  ident: 912_CR43
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gks1193
– volume: 11
  start-page: M111.014050
  year: 2012
  ident: 912_CR13
  publication-title: Mol Cell Proteomics.
  doi: 10.1074/mcp.M111.014050
– volume: 145
  start-page: 383
  year: 2011
  ident: 912_CR19
  publication-title: Cell.
  doi: 10.1016/j.cell.2011.03.028
– volume: 9
  start-page: 648
  year: 2013
  ident: 912_CR10
  publication-title: Mol Syst Biol.
  doi: 10.1038/msb.2013.4
– volume: 151
  start-page: 1617
  year: 2012
  ident: 912_CR22
  publication-title: Cell.
  doi: 10.1016/j.cell.2012.11.039
– volume: 19
  start-page: 327
  year: 2009
  ident: 912_CR39
  publication-title: Genome Res.
  doi: 10.1101/gr.073585.107
– volume: 5
  start-page: 883
  year: 2010
  ident: 912_CR50
  publication-title: Nat Protoc.
  doi: 10.1038/nprot.2010.32
– volume: 99
  start-page: 6567
  year: 2002
  ident: 912_CR58
  publication-title: Proc Natl Acad Sci U S A.
  doi: 10.1073/pnas.082099299
– volume: 514
  start-page: 233
  year: 2014
  ident: 912_CR23
  publication-title: Nature.
  doi: 10.1038/nature13562
– volume: 147
  start-page: 320
  year: 2011
  ident: 912_CR36
  publication-title: Cell.
  doi: 10.1016/j.cell.2011.08.044
– volume: 120
  start-page: 15
  year: 2005
  ident: 912_CR56
  publication-title: Cell.
  doi: 10.1016/j.cell.2004.12.035
– volume: 6
  start-page: rs5
  year: 2013
  ident: 912_CR15
  publication-title: Sci Signal
  doi: 10.1126/scisignal.2003629
– volume: 4
  start-page: 1184
  year: 2009
  ident: 912_CR41
  publication-title: Nat Protoc.
  doi: 10.1038/nprot.2009.97
– volume: 150
  start-page: 1068
  year: 2012
  ident: 912_CR5
  publication-title: Cell.
  doi: 10.1016/j.cell.2012.08.011
– volume: 2
  start-page: 1579
  year: 2012
  ident: 912_CR12
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2012.10.014
– volume: 443
  start-page: 594
  year: 2006
  ident: 912_CR8
  publication-title: Nature.
  doi: 10.1038/nature05186
– volume: 136
  start-page: 200
  year: 2009
  ident: 912_CR26
  publication-title: Cell.
  doi: 10.1016/j.cell.2009.01.009
– volume: 153
  start-page: 71
  year: 2013
  ident: 912_CR24
  publication-title: Cell.
  doi: 10.1016/j.cell.2013.02.036
– volume: 38
  start-page: D497
  year: 2010
  ident: 912_CR14
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkp914
– volume: 14
  start-page: 20
  year: 2012
  ident: 912_CR33
  publication-title: Nat Cell Biol.
  doi: 10.1038/ncb2390
– volume: 22
  start-page: 446
  year: 2012
  ident: 912_CR21
  publication-title: Dev Cell.
  doi: 10.1016/j.devcel.2011.11.021
– volume: 43
  start-page: D447
  year: 2015
  ident: 912_CR59
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku1003
– volume: 509
  start-page: 575
  year: 2014
  ident: 912_CR2
  publication-title: Nature.
  doi: 10.1038/nature13302
– volume: 37
  start-page: 825
  year: 2009
  ident: 912_CR38
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkn1005
– volume: 131
  start-page: 557
  year: 2007
  ident: 912_CR35
  publication-title: Cell.
  doi: 10.1016/j.cell.2007.08.037
– volume: 125
  start-page: 1731
  year: 2003
  ident: 912_CR25
  publication-title: J Am Chem Soc.
  doi: 10.1021/ja026939x
– volume: 20
  start-page: 1413
  year: 2004
  ident: 912_CR37
  publication-title: Bioinformatics.
  doi: 10.1093/bioinformatics/bth114
– volume: 43
  start-page: D494
  year: 2015
  ident: 912_CR60
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku1081
– volume: 7
  start-page: 548
  year: 2011
  ident: 912_CR17
  publication-title: Mol Syst Biol.
  doi: 10.1038/msb.2011.81
– volume: 42
  start-page: D749
  year: 2014
  ident: 912_CR40
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkt1196
– volume: 4
  start-page: 249
  year: 2003
  ident: 912_CR44
  publication-title: Biostatistics.
  doi: 10.1093/biostatistics/4.2.249
– volume: 307
  start-page: 724
  year: 2005
  ident: 912_CR7
  publication-title: Science.
  doi: 10.1126/science.1105103
– volume: 39
  start-page: 2701
  year: 2011
  ident: 912_CR20
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkq1218
– volume: 54
  start-page: 826
  year: 2014
  ident: 912_CR55
  publication-title: J Chem Inf Model.
  doi: 10.1021/ci4005332
– volume: 122
  start-page: 117
  year: 2014
  ident: 912_CR57
  publication-title: Methods Cell Biol.
  doi: 10.1016/B978-0-12-417160-2.00006-0
– volume: 29
  start-page: 443
  year: 2011
  ident: 912_CR28
  publication-title: Nat Biotechnol.
  doi: 10.1038/nbt.1862
– volume: 7
  start-page: 549
  year: 2011
  ident: 912_CR16
  publication-title: Mol Syst Biol.
  doi: 10.1038/msb.2011.82
– volume: 106
  start-page: 5181
  year: 2009
  ident: 912_CR27
  publication-title: Proc Natl Acad Sci U S A.
  doi: 10.1073/pnas.0812889106
– volume: 9
  start-page: 2216
  year: 2010
  ident: 912_CR51
  publication-title: J Proteome Res.
  doi: 10.1021/pr9009854
– volume: 489
  start-page: 57
  year: 2012
  ident: 912_CR31
  publication-title: Nature
  doi: 10.1038/nature11247
– volume: 8
  start-page: 337
  year: 2008
  ident: 912_CR34
  publication-title: BMC Evol Biol.
  doi: 10.1186/1471-2148-8-337
– volume: 110
  start-page: 1657
  year: 1988
  ident: 912_CR52
  publication-title: J Am Chem Soc.
  doi: 10.1021/ja00214a001
– reference: 26975421 - Genome Biol. 2016;17:48
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Snippet Background Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so...
Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly...
Background Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so...
BACKGROUND: Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so...
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StartPage 47
SubjectTerms Acids
Animal Genetics and Genomics
Animals
Bioinformatics
Biomedical and Life Sciences
Cancer
Cell cycle
Cell Lineage - genetics
Chromatin
Chromatin - chemistry
Chromatin - genetics
Datasets
Evolutionary Biology
Gene expression
Genomics
Human Genetics
Humans
Life Sciences
Mammals
Microbial Genetics and Genomics
Multiprotein Complexes - chemistry
Multiprotein Complexes - genetics
neoplasm cells
neoplasms
Plant Genetics and Genomics
Protein expression
Protein Structure, Tertiary
Proteins
proteome
Proteome - genetics
Proteomes
Proteomics
spatial variation
Stem cells
Stoichiometry
temporal variation
Transcription
Transcription, Genetic
Variation
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Title Spatiotemporal variation of mammalian protein complex stoichiometries
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