Systematic model reduction captures the dynamics of extrinsic noise in biochemical subnetworks

We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving complex formation and dissociation reactions. We propose the use of model reduction strategies to understand the "extrinsic" sourc...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of chemical physics Vol. 153; no. 2; p. 025101
Main Authors: Bravi, Barbara, Rubin, Katy J, Sollich, Peter
Format: Journal Article
Language:English
Published: United States 14.07.2020
Subjects:
ISSN:1089-7690, 1089-7690
Online Access:Get more information
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving complex formation and dissociation reactions. We propose the use of model reduction strategies to understand the "extrinsic" sources of stochasticity arising from the rest of the network. Our approaches are based on subnetwork dynamical equations derived by projection methods and path integrals. The results provide a principled derivation of different components of the extrinsic noise that is observed experimentally in cellular biochemical reactions, over and above the intrinsic noise from the stochasticity of biochemical events in the subnetwork. We explore several intermediate approximations to assess systematically the relative importance of different extrinsic noise components, including initial transients, long-time plateaus, temporal correlations, multiplicative noise terms, and nonlinear noise propagation. The best approximations achieve excellent accuracy in quantitative tests on a simple protein network and on the epidermal growth factor receptor signaling network.
AbstractList We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving complex formation and dissociation reactions. We propose the use of model reduction strategies to understand the "extrinsic" sources of stochasticity arising from the rest of the network. Our approaches are based on subnetwork dynamical equations derived by projection methods and path integrals. The results provide a principled derivation of different components of the extrinsic noise that is observed experimentally in cellular biochemical reactions, over and above the intrinsic noise from the stochasticity of biochemical events in the subnetwork. We explore several intermediate approximations to assess systematically the relative importance of different extrinsic noise components, including initial transients, long-time plateaus, temporal correlations, multiplicative noise terms, and nonlinear noise propagation. The best approximations achieve excellent accuracy in quantitative tests on a simple protein network and on the epidermal growth factor receptor signaling network.
We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving complex formation and dissociation reactions. We propose the use of model reduction strategies to understand the "extrinsic" sources of stochasticity arising from the rest of the network. Our approaches are based on subnetwork dynamical equations derived by projection methods and path integrals. The results provide a principled derivation of different components of the extrinsic noise that is observed experimentally in cellular biochemical reactions, over and above the intrinsic noise from the stochasticity of biochemical events in the subnetwork. We explore several intermediate approximations to assess systematically the relative importance of different extrinsic noise components, including initial transients, long-time plateaus, temporal correlations, multiplicative noise terms, and nonlinear noise propagation. The best approximations achieve excellent accuracy in quantitative tests on a simple protein network and on the epidermal growth factor receptor signaling network.We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving complex formation and dissociation reactions. We propose the use of model reduction strategies to understand the "extrinsic" sources of stochasticity arising from the rest of the network. Our approaches are based on subnetwork dynamical equations derived by projection methods and path integrals. The results provide a principled derivation of different components of the extrinsic noise that is observed experimentally in cellular biochemical reactions, over and above the intrinsic noise from the stochasticity of biochemical events in the subnetwork. We explore several intermediate approximations to assess systematically the relative importance of different extrinsic noise components, including initial transients, long-time plateaus, temporal correlations, multiplicative noise terms, and nonlinear noise propagation. The best approximations achieve excellent accuracy in quantitative tests on a simple protein network and on the epidermal growth factor receptor signaling network.
Author Sollich, Peter
Rubin, Katy J
Bravi, Barbara
Author_xml – sequence: 1
  givenname: Barbara
  orcidid: 0000000348607584
  surname: Bravi
  fullname: Bravi, Barbara
  organization: Institute of Theoretical Physics, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland
– sequence: 2
  givenname: Katy J
  surname: Rubin
  fullname: Rubin, Katy J
  organization: Department of Mathematics, King's College London, Strand, London WC2R 2LS, United Kingdom
– sequence: 3
  givenname: Peter
  orcidid: 0000000301697893
  surname: Sollich
  fullname: Sollich, Peter
  organization: Department of Mathematics, King's College London, Strand, London WC2R 2LS, United Kingdom
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32668933$$D View this record in MEDLINE/PubMed
BookMark eNpN0DtPwzAUBWALFdEHDPwB5JElxa848YgqXlIlBjoTOfa1akjsEjuC_nsiARLTPcN3znCXaBZiAIQuKVlTIvlNuSaE1JyIE7SgpFZFJRWZ_ctztEzpbUK0YuIMzTmTslacL9DryzFl6HX2BvfRQocHsKPJPgZs9CGPAySc94DtMejem4Sjw_CVBx_SVAnRJ8A-4NZHs4cJ6A6nsQ2QP-Pwns7RqdNdgovfu0K7-7vd5rHYPj88bW63hRG0zoWwxFWO2xIq7jTnyqjSVqCksYQaJYy2QhPpSg3OUUpapiThVW1kKyvp2Apd_8wehvgxQspN75OBrtMB4pgaJpgQgvGSTPTql45tD7Y5DL7Xw7H5ewn7BkXMZWk
CitedBy_id crossref_primary_10_1088_2632_2153_ad9194
crossref_primary_10_1088_1751_8121_acfd6a
ContentType Journal Article
DBID CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1063/5.0008304
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList MEDLINE
MEDLINE - Academic
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: 7X8
  name: MEDLINE - Academic
  url: https://search.proquest.com/medline
  sourceTypes: Aggregation Database
DeliveryMethod no_fulltext_linktorsrc
Discipline Chemistry
Physics
EISSN 1089-7690
ExternalDocumentID 32668933
Genre Journal Article
GroupedDBID ---
-DZ
-ET
-~X
123
1UP
2-P
29K
4.4
53G
5VS
85S
AAAAW
AABDS
AAPUP
AAYIH
ABJGX
ABPPZ
ABZEH
ACBRY
ACLYJ
ACNCT
ACZLF
ADCTM
ADMLS
AEJMO
AENEX
AFATG
AFHCQ
AGKCL
AGLKD
AGMXG
AGTJO
AHSDT
AJJCW
AJQPL
ALEPV
ALMA_UNASSIGNED_HOLDINGS
AQWKA
ATXIE
AWQPM
BDMKI
BPZLN
CGR
CS3
CUY
CVF
D-I
DU5
EBS
ECM
EIF
F5P
FDOHQ
FFFMQ
HAM
M6X
M71
M73
N9A
NPM
NPSNA
O-B
P2P
RIP
RNS
RQS
TN5
TWZ
UPT
WH7
YQT
YZZ
~02
7X8
AAGWI
ABUFD
ID FETCH-LOGICAL-c418t-4d0f7f3d5e73fa339c95d7e96cd01c94cad4a06f5aeff110b2960378c6b676f2
IEDL.DBID 7X8
ISICitedReferencesCount 4
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000551898100001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 1089-7690
IngestDate Sun Nov 09 09:28:36 EST 2025
Thu Apr 03 06:57:29 EDT 2025
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 2
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c418t-4d0f7f3d5e73fa339c95d7e96cd01c94cad4a06f5aeff110b2960378c6b676f2
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000000348607584
0000000301697893
OpenAccessLink https://aip.scitation.org/doi/pdf/10.1063/5.0008304
PMID 32668933
PQID 2424442350
PQPubID 23479
ParticipantIDs proquest_miscellaneous_2424442350
pubmed_primary_32668933
PublicationCentury 2000
PublicationDate 2020-Jul-14
20200714
PublicationDateYYYYMMDD 2020-07-14
PublicationDate_xml – month: 07
  year: 2020
  text: 2020-Jul-14
  day: 14
PublicationDecade 2020
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle The Journal of chemical physics
PublicationTitleAlternate J Chem Phys
PublicationYear 2020
SSID ssj0001724
Score 2.3569741
Snippet We consider the general problem of describing the dynamics of subnetworks of larger biochemical reaction networks, e.g., protein interaction networks involving...
SourceID proquest
pubmed
SourceType Aggregation Database
Index Database
StartPage 025101
SubjectTerms ErbB Receptors - chemistry
ErbB Receptors - metabolism
Models, Biological
Protein Interaction Maps
Stochastic Processes
Title Systematic model reduction captures the dynamics of extrinsic noise in biochemical subnetworks
URI https://www.ncbi.nlm.nih.gov/pubmed/32668933
https://www.proquest.com/docview/2424442350
Volume 153
WOSCitedRecordID wos000551898100001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV05T8MwFLaAgmDhKFe5ZCTWiMR27GRCqKJioapEh05UPqUsSalbfj_POeiEhMSSLVFiv7z3vcPfh9ADgDZBuY0jQ7QNCYqNAGWQSKlEJMYwxeNGbEKMx9lslk_agptvxyo7n1g7alPpUCN_DMcYGMT-NH5afEZBNSp0V1sJjW3UowBlglWL2YYtHIIzawbs80hAGtgxC3H6GCopgD5qfbZfkGUdYUZH_323Y3TYYkv83BjDCdqyZR_tDztJtz7aq-c9tT9FH-8_DM64FsPBy8DhGnYJa7kIbQWPARti0yjWe1w5DH58WZTwAFxWhbe4KLEqguJWTTmA_VqVzVC5P0PT0ct0-Bq1UguRZkm2ipiJnXDUpFZQJynNdZ4aYXOuTZzonGlpmIy5S6V1DhCDIpD5UJFprrjgjpyjnbIq7SXCEP5trmJjJSAHQrSiTvE04EhJiMroAN13aziHrw_tCVnaau3nm1UcoItmI-aLhnJjDiCTA7KiV3-4-xodkJAUB_ZLdoN6Dv5je4t29deq8Mu72kTgOp68fQOCO8dE
linkProvider ProQuest
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=Systematic+model+reduction+captures+the+dynamics+of+extrinsic+noise+in+biochemical+subnetworks&rft.jtitle=The+Journal+of+chemical+physics&rft.au=Bravi%2C+Barbara&rft.au=Rubin%2C+Katy+J&rft.au=Sollich%2C+Peter&rft.date=2020-07-14&rft.eissn=1089-7690&rft.volume=153&rft.issue=2&rft.spage=025101&rft_id=info:doi/10.1063%2F5.0008304&rft_id=info%3Apmid%2F32668933&rft_id=info%3Apmid%2F32668933&rft.externalDocID=32668933
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1089-7690&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1089-7690&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1089-7690&client=summon