Switching Muscles On and Off in Steps: The McKillop-Geeves Three-State Model of Muscle Regulation

BJ Classic highlighting the article “Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament.”

Saved in:
Bibliographic Details
Published inBiophysical journal Vol. 112; no. 12; pp. 2459 - 2466
Main Author Lehman, William
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 20.06.2017
Biophysical Society
The Biophysical Society
Subjects
Actin
Actin Cytoskeleton
Actins
Actomyosin
Adenosine triphosphatase
BJ Classics
Calcium-binding protein
Contraction
Filaments
Humans
In vitro testing
Motor task performance
Muscles
Muscular system
Myosin
Myosin ATPase
Myosin Subfragments
Myosins
Proteins
Regulatory proteins
Switches
Switching
Tropomyosin
Troponin
Online AccessGet full text

Cover

Abstract BJ Classic highlighting the article “Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament.”
AbstractList BJ Classic highlighting the article "Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament."
Before the introduction of in vitro motility assays, the actin-activated myosin ATPase was (and still is) commonly used as a benchtop analog of actin-myosin-based contraction. Indeed, actomyosin ATPase activity is Ca^sup 2+^-dependent provided that both tropomyosin and troponin are present in mixtures of purified F-actin and myosin (or when substituting the soluble subfragment-1 (S1) or heavy meromyosin (HMM) motor heads for intact myosin). However, in the early 1970s, Weber, Bremel, and Murray showed that prolonged attachment of myosin on tropomyosin-troponin-regulated thin filaments switches on actomyosin ATPase even at low Ca^sup 2+^ concentration, despite the expectation that ATPase would be inhibited by the regulatory proteins if a strictly binary on-off switching mechanism were in operation. The Murray, Bremel, and Weber work was among the first of several findings to propose that regulation of thin-filament activity is not simply governed by a binary on-off switching mechanism and that a multiple step process may be involved in the myofilament activation.
Author Lehman, William
AuthorAffiliation 1 Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts
AuthorAffiliation_xml – name: 1 Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts
Author_xml – sequence: 1
  givenname: William
  surname: Lehman
  fullname: Lehman, William
  email: wlehman@bu.edu
  organization: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28552313$$D View this record in MEDLINE/PubMed
BookMark eNp9kcGO0zAQhi20iO0uPAAXFIkLl4SxHTsJSEhoBQtiq0q0nC3HmbSOUjvESRFvw7PwZLhqWQEHTj74m1__zHdFLpx3SMhTChkFKl92WT10GQNaZJBnIPgDsqAiZylAKS_IAgBkyvNKXJKrEDoAygTQR-SSlUIwTvmC1OtvdjI767bJcg6mx5CsXKJdk6zaNrEuWU84hFfJZoc_fyzNJ9v3fkhvEQ-R3OxGxHQ96QmTpW-wT3x7jkk-43bu9WS9e0wetroP-OT8XpMv799tbj6kd6vbjzdv71IjcjGlnHNsmaYFSCbbsmqRacZBFxUzNaA0XFesKLWQVV1IljeGC9GwkklTMoqSX5M3p9xhrvfYGHTTqHs1jHavx-_Ka6v-_nF2p7b-oEReVCAgBrw4B4z-64xhUnsbDPa9dujnoGgFPOelKGlEn_-Ddn4eXVwvUrF1LkAeG9ETZUYfwojtfRkK6mhQdSoaVEeDCnIVDcaZZ39ucT_xW1kEXp8AjLc8WBxVMBadwcaOaCbVePuf-F8uqa0v
CitedBy_id crossref_primary_10_1016_j_bbrc_2017_10_161
crossref_primary_10_1007_s10974_019_09515_z
crossref_primary_10_1134_S1990519X1806010X
crossref_primary_10_1085_jgp_201812188
crossref_primary_10_1007_s12551_021_00854_1
crossref_primary_10_1074_jbc_RA120_014713
crossref_primary_10_1085_jgp_202413538
crossref_primary_10_1007_s10974_019_09513_1
crossref_primary_10_1002_2211_5463_12876
crossref_primary_10_1085_jgp_202213274
crossref_primary_10_1016_j_bbrc_2019_05_146
crossref_primary_10_3390_math8071169
crossref_primary_10_1007_s10974_019_09526_w
crossref_primary_10_1016_j_yjmcc_2024_01_004
crossref_primary_10_1016_j_bpj_2017_10_004
crossref_primary_10_1085_jgp_201812198
crossref_primary_10_3389_fphys_2018_00405
crossref_primary_10_1016_j_bpj_2019_11_3396
crossref_primary_10_1007_s10974_019_09501_5
crossref_primary_10_1016_j_abb_2022_109282
crossref_primary_10_1085_jgp_202313387
crossref_primary_10_1038_s41598_023_45037_y
crossref_primary_10_1085_jgp_201912446
crossref_primary_10_3390_ijms19072020
crossref_primary_10_1016_j_bbrc_2019_12_061
Cites_doi 10.1016/j.bbrc.2007.11.130
10.1016/S0006-3495(93)81110-X
10.1016/S0006-3495(98)77581-2
10.1073/pnas.012582499
10.1006/jmbi.1998.1654
10.1038/newbio238097a0
10.1042/bj0640184
10.1016/S0021-9258(17)43316-3
10.1101/SQB.1973.037.01.046
10.1016/S0021-9258(18)93995-5
10.1016/j.abb.2016.02.016
10.1021/bi981603e
10.1042/bj2320343
10.1038/368065a0
10.1007/s10974-008-9157-6
10.1007/BF00818255
10.1016/j.jmb.2009.10.060
10.1038/nature18295
10.1016/S0021-9258(18)34298-4
10.1074/jbc.M003648200
10.1038/nature14033
10.1016/S0006-3495(02)75518-5
10.1038/2001010a0
10.1038/348217a0
10.1016/j.abb.2016.09.008
10.1038/173973a0
10.1038/173971a0
10.1002/jcp.1030290103
10.1016/j.cell.2012.05.037
10.1101/SQB.1973.037.01.037
10.1016/0022-2836(73)90527-5
10.1016/S0006-3495(03)70040-X
10.1021/bi00801a004
10.1152/physrev.1973.53.3.612
10.1042/bj1250085P
10.1085/jgp.59.4.375
10.1016/S0006-3495(02)75519-7
10.1073/pnas.77.12.7209
10.1007/s10974-004-4839-1
10.1016/S0021-9258(18)81304-7
10.1126/science.164.3886.1356
10.1002/bip.22853
10.1016/j.jsb.2006.02.020
10.1016/S0006-3495(03)70041-1
10.1098/rspb.1964.0055
10.1016/j.cub.2016.11.033
10.1016/0022-2836(86)90468-7
10.1006/jmbi.2000.4080
10.1038/newbio236182a0
10.1016/j.bpj.2014.05.044
10.1016/S0006-3495(87)83208-3
10.1101/SQB.1973.037.01.044
10.1016/S0065-3233(04)71005-0
10.1006/jmbi.1996.0800
ContentType Journal Article
Copyright 2017 Biophysical Society
Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Copyright Biophysical Society Jun 20, 2017
2017 Biophysical Society. 2017 Biophysical Society
Copyright_xml – notice: 2017 Biophysical Society
– notice: Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.
– notice: Copyright Biophysical Society Jun 20, 2017
– notice: 2017 Biophysical Society. 2017 Biophysical Society
DBID 6I.
AAFTH
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QO
7QP
7TK
7TM
7U9
8FD
FR3
H94
K9.
P64
7X8
5PM
DOI 10.1016/j.bpj.2017.04.053
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Biotechnology Research Abstracts
Calcium & Calcified Tissue Abstracts
Neurosciences Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Technology Research Database
Engineering Research Database
AIDS and Cancer Research Abstracts
ProQuest Health & Medical Complete (Alumni)
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Virology and AIDS Abstracts
Biotechnology Research Abstracts
Technology Research Database
Nucleic Acids Abstracts
AIDS and Cancer Research Abstracts
ProQuest Health & Medical Complete (Alumni)
Engineering Research Database
Calcium & Calcified Tissue Abstracts
Neurosciences Abstracts
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic


MEDLINE
Virology and AIDS Abstracts
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 Biology
EISSN 1542-0086
EndPage 2466
ExternalDocumentID 10_1016_j_bpj_2017_04_053
28552313
S0006349517305076
Genre Comment
Journal Article
Feature
GrantInformation_xml – fundername: NHLBI NIH HHS
  grantid: R37 HL036153
GroupedDBID ---
-DZ
-~X
.55
0R~
23N
2WC
4.4
457
5GY
5RE
62-
6I.
6J9
AACTN
AAEDW
AAFTH
AAIAV
AAKRW
AALRI
AAUCE
AAVLU
AAXJY
AAXUO
ABJNI
ABMAC
ABMWF
ABVKL
ACBEA
ACGFO
ACGFS
ACGOD
ACIWK
ACNCT
ACPRK
ADBBV
ADEZE
ADJPV
AENEX
AEXQZ
AFRAH
AFTJW
AGKMS
AHMBA
AHPSJ
AITUG
ALKID
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
AOIJS
AYCSE
AZFZN
BAWUL
CS3
D0L
DIK
DU5
E3Z
EBS
EJD
F5P
FCP
FDB
FRP
HYE
IH2
IXB
JIG
KQ8
L7B
M41
N9A
NCXOZ
O-L
O9-
OK1
P2P
RCE
RIG
RNS
ROL
RPM
RWL
SES
SSZ
TAE
TBP
TN5
WH7
WOQ
WOW
WQ6
X7M
YNY
YWH
ZA5
~02
0SF
AAEDT
AAMRU
ADVLN
AKAPO
AKRWK
ALIPV
CGR
CUY
CVF
ECM
EIF
NPM
--K
.GJ
3O-
3V.
53G
6TJ
7X2
7X7
88A
88E
88I
8AF
8AO
8FE
8FG
8FH
8FI
8FJ
8G5
8R4
8R5
AAIKJ
AAQXK
AAYXX
ABUWG
ACRPL
ADMUD
ADNMO
AFKRA
AGHFR
AI.
ARAPS
ASPBG
ATCPS
AVWKF
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
BPHCQ
BVXVI
CCPQU
CITATION
DWQXO
FEDTE
FGOYB
FYUFA
G-2
GNUQQ
GUQSH
GX1
H13
HCIFZ
HMCUK
HVGLF
HX~
HZ~
LK8
M0K
M0L
M1P
M2O
M2P
M2Q
M7P
MVM
OZT
P62
PQQKQ
PRG
PROAC
PSQYO
Q2X
R2-
S0X
UKHRP
UKR
VH1
YYP
ZGI
ZXP
~KM
7QO
7QP
7TK
7TM
7U9
8FD
FR3
H94
K9.
P64
7X8
5PM
ID FETCH-LOGICAL-c545t-333ef2a170626f89fe2a230a792cb0e6c3a9278a569b7624dc355d2826c821e63
IEDL.DBID RPM
ISSN 0006-3495
IngestDate Tue Sep 17 20:52:39 EDT 2024
Fri Oct 25 07:17:28 EDT 2024
Thu Oct 10 20:30:26 EDT 2024
Fri Dec 06 02:36:22 EST 2024
Sat Sep 28 08:46:35 EDT 2024
Fri Feb 23 02:27:08 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 12
Language English
License This article is made available under the Elsevier license.
Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c545t-333ef2a170626f89fe2a230a792cb0e6c3a9278a569b7624dc355d2826c821e63
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Commentary-1
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S0006349517305076
PMID 28552313
PQID 1923045066
PQPubID 7454
PageCount 8
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5479050
proquest_miscellaneous_1903438581
proquest_journals_1923045066
crossref_primary_10_1016_j_bpj_2017_04_053
pubmed_primary_28552313
elsevier_sciencedirect_doi_10_1016_j_bpj_2017_04_053
PublicationCentury 2000
PublicationDate 2017-06-20
PublicationDateYYYYMMDD 2017-06-20
PublicationDate_xml – month: 06
  year: 2017
  text: 2017-06-20
  day: 20
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: New York
PublicationTitle Biophysical journal
PublicationTitleAlternate Biophys J
PublicationYear 2017
Publisher Elsevier Inc
Biophysical Society
The Biophysical Society
Publisher_xml – name: Elsevier Inc
– name: Biophysical Society
– name: The Biophysical Society
References Bremel, Murray, Weber (bib26) 1972; 37
McKillop, Geeves (bib23) 1993; 65
Giese (bib3) 1963
Heilbrunn, Wiercinski (bib10) 1947; 29
Huxley (bib16) 1971; 11
Lehman, Craig, Vibert (bib54) 1994; 368
Holmes (bib51) 1995; 68
Geeves, Conibear (bib40) 1998; 75
Poole, Lorenz, Holmes (bib42) 2006; 155
Lehrer, Morris (bib29) 1982; 257
Geeves (bib36) 2012; vol. 4
Li, Holmes, Fischer (bib61) 2010; 395
Huxley (bib17) 1971; 125
Moore, Campbell, Lehman (bib34) 2016; 594
Rynkiewicz, Fischer, Lehman (bib58) 2016; 609
Geeves, Goody, Gutfreund (bib38) 1984; 5
Carlson, Doyle (bib49) 2002; 99
Huxley (bib7) 1969; 164
Vibert, Haselgrove, Poulsen (bib22) 1972; 236
Geeves, Holmes (bib8) 2005; 71
Lymn, Taylor (bib6) 1971; 10
Geeves (bib9) 2016; 105
Ebashi (bib14) 1963; 200
Lehman, Hatch, Craig (bib50) 2000; 302
Scheer (bib4) 1963
Huxley (bib19) 2008; 369
Holmes, Lehman (bib56) 2008; 29
Chalovich, Yan, Chen (bib55) 2002; 82
Phillips, Fillers, Cohen (bib37) 1986; 192
von der Ecken, Heissler, Raunser (bib45) 2016; 534
Smith, Maytum, Geeves (bib60) 2003; 84
Li, Rieck, Dong (bib32) 2014; 107
Maytum, Lehrer, Geeves (bib48) 1999; 38
Lehrer, Geeves (bib30) 1998; 277
Milligan, Whittaker, Safer (bib53) 1990; 348
Poole, Holmes, Lorenz (bib52) 1995; 68
Huxley, Niedergerke (bib2) 1954; 173
Parry, Squire (bib21) 1973; 75
Ostap, Franzini-Armstrong, Szent-Györgyi (bib24) 2004; 25
Weber, Herz (bib12) 1963; 238
Haselgrove (bib20) 1972; 37
Lehrer, Morris (bib33) 1984; 259
Tobacman, Butters (bib35) 2000; 275
Huxley, Hanson (bib1) 1954; 173
Huxley (bib18) 1972; 37
Weber, Murray (bib27) 1973; 53
Geeves, Halsall (bib46) 1987; 52
Smith, Geeves (bib59) 2003; 84
Grey, Perry (bib11) 1956; 64
Bremel, Weber (bib25) 1972; 238
Banga (bib5) 1942; 1
Geeves, Lehrer (bib31) 2002; 82
Behrmann, Müller, Raunser (bib43) 2012; 150
Trybus, Taylor (bib47) 1980; 77
Gunning, Hardeman (bib57) 2017; 27
Hanson, Lowy (bib15) 1964; 160
Criddle, Geeves, Jeffries (bib39) 1985; 232
von der Ecken, Müller, Raunser (bib44) 2015; 519
Weber, Winicur (bib13) 1961; 236
Lehman, Szent-Györgyi (bib28) 1972; 59
Vibert, Craig, Lehman (bib41) 1997; 266
9571024 - J Mol Biol. 1998 Apr 17;277(5):1081-9
14005435 - J Biol Chem. 1961 Dec;236:3198-202
13363825 - Biochem J. 1956 Sep;64(1):184-92
2234090 - Nature. 1990 Nov 15;348(6298):217-21
13999360 - J Biol Chem. 1963 Feb;238:599-605
19116763 - J Muscle Res Cell Motil. 2008;29(6-8):213-9
27061920 - Biopolymers. 2016 Aug;105(8):483-91
14097720 - Nature. 1963 Dec 7;200:1010
27324845 - Nature. 2016 Jun 30;534(7609):724-8
5144244 - Biochem J. 1971 Dec;125(4):85P
13165697 - Nature. 1954 May 22;173(4412):971-3
4503735 - Nat New Biol. 1972 Apr 12;236(67):182-3
19883661 - J Mol Biol. 2010 Jan 15;395(2):327-39
4261616 - Nat New Biol. 1972 Jul 26;238(82):97-101
6938966 - Proc Natl Acad Sci U S A. 1980 Dec;77(12):7209-13
4260494 - J Gen Physiol. 1972 Apr;59(4):375-87
10864931 - J Biol Chem. 2000 Sep 8;275(36):27587-93
9054965 - J Mol Biol. 1997 Feb 14;266(1):8-14
8218897 - Biophys J. 1993 Aug;65(2):693-701
6123507 - J Biol Chem. 1982 Jul 25;257(14):8073-80
4181952 - Science. 1969 Jun 20;164(3886):1356-65
3911945 - Biochem J. 1985 Dec 1;232(2):343-9
22817895 - Cell. 2012 Jul 20;150(2):327-38
3663829 - Biophys J. 1987 Aug;52(2):215-20
13165698 - Nature. 1954 May 22;173(4412):973-6
7787068 - Biophys J. 1995 Apr;68(4 Suppl):2S-5S; discussion 6S-7S
8107884 - Nature. 1994 Mar 3;368(6466):65-7
11898795 - Biophys J. 2002 Mar;82(3):1677-81
16230112 - Adv Protein Chem. 2005;71:161-93
9894007 - Biochemistry. 1999 Jan 19;38(3):1102-10
27663225 - Arch Biochem Biophys. 2016 Nov 1;609:51-58
3820299 - J Mol Biol. 1986 Nov 5;192(1):111-31
12719245 - Biophys J. 2003 May;84(5):3155-67
4577547 - Physiol Rev. 1973 Jul;53(3):612-73
6237117 - J Muscle Res Cell Motil. 1984 Aug;5(4):351-61
28073025 - Curr Biol. 2017 Jan 9;27(1):R8-R13
10986121 - J Mol Biol. 2000 Sep 22;302(3):593-606
20285919 - J Cell Comp Physiol. 1947 Feb;29(1):15-32
25470062 - Nature. 2015 Mar 5;519(7541):114-7
9675193 - Biophys J. 1998 Aug;75(2):926-37
4258719 - Biochemistry. 1971 Dec 7;10(25):4617-24
26891592 - Arch Biochem Biophys. 2016 Mar 15;594:8-17
14218067 - Proc R Soc Lond B Biol Sci. 1964 Oct 27;160:449-60
16793285 - J Struct Biol. 2006 Aug;155(2):273-84
25099807 - Biophys J. 2014 Aug 5;107(3):682-93
16106534 - J Muscle Res Cell Motil. 2004;25(6):483-7
6230348 - J Biol Chem. 1984 Feb 25;259(4):2070-2
4713300 - J Mol Biol. 1973 Mar 25;75(1):33-55
12719246 - Biophys J. 2003 May;84(5):3168-80
11875207 - Proc Natl Acad Sci U S A. 2002 Feb 19;99 Suppl 1:2538-45
18070595 - Biochem Biophys Res Commun. 2008 Apr 25;369(1):34-42
Lymn (10.1016/j.bpj.2017.04.053_bib6) 1971; 10
Holmes (10.1016/j.bpj.2017.04.053_bib56) 2008; 29
Huxley (10.1016/j.bpj.2017.04.053_bib19) 2008; 369
Geeves (10.1016/j.bpj.2017.04.053_bib31) 2002; 82
Lehrer (10.1016/j.bpj.2017.04.053_bib33) 1984; 259
Giese (10.1016/j.bpj.2017.04.053_bib3) 1963
Vibert (10.1016/j.bpj.2017.04.053_bib41) 1997; 266
Ostap (10.1016/j.bpj.2017.04.053_bib24) 2004; 25
Heilbrunn (10.1016/j.bpj.2017.04.053_bib10) 1947; 29
Vibert (10.1016/j.bpj.2017.04.053_bib22) 1972; 236
Huxley (10.1016/j.bpj.2017.04.053_bib7) 1969; 164
Weber (10.1016/j.bpj.2017.04.053_bib12) 1963; 238
Moore (10.1016/j.bpj.2017.04.053_bib34) 2016; 594
Trybus (10.1016/j.bpj.2017.04.053_bib47) 1980; 77
Geeves (10.1016/j.bpj.2017.04.053_bib8) 2005; 71
Behrmann (10.1016/j.bpj.2017.04.053_bib43) 2012; 150
Huxley (10.1016/j.bpj.2017.04.053_bib17) 1971; 125
Bremel (10.1016/j.bpj.2017.04.053_bib26) 1972; 37
Huxley (10.1016/j.bpj.2017.04.053_bib1) 1954; 173
Huxley (10.1016/j.bpj.2017.04.053_bib16) 1971; 11
Poole (10.1016/j.bpj.2017.04.053_bib42) 2006; 155
Li (10.1016/j.bpj.2017.04.053_bib32) 2014; 107
von der Ecken (10.1016/j.bpj.2017.04.053_bib45) 2016; 534
Poole (10.1016/j.bpj.2017.04.053_bib52) 1995; 68
Milligan (10.1016/j.bpj.2017.04.053_bib53) 1990; 348
Scheer (10.1016/j.bpj.2017.04.053_bib4) 1963
Lehman (10.1016/j.bpj.2017.04.053_bib54) 1994; 368
Smith (10.1016/j.bpj.2017.04.053_bib59) 2003; 84
Geeves (10.1016/j.bpj.2017.04.053_bib46) 1987; 52
Weber (10.1016/j.bpj.2017.04.053_bib13) 1961; 236
Phillips (10.1016/j.bpj.2017.04.053_bib37) 1986; 192
Holmes (10.1016/j.bpj.2017.04.053_bib51) 1995; 68
Huxley (10.1016/j.bpj.2017.04.053_bib2) 1954; 173
Lehrer (10.1016/j.bpj.2017.04.053_bib29) 1982; 257
von der Ecken (10.1016/j.bpj.2017.04.053_bib44) 2015; 519
Maytum (10.1016/j.bpj.2017.04.053_bib48) 1999; 38
Haselgrove (10.1016/j.bpj.2017.04.053_bib20) 1972; 37
Geeves (10.1016/j.bpj.2017.04.053_bib9) 2016; 105
Lehrer (10.1016/j.bpj.2017.04.053_bib30) 1998; 277
Gunning (10.1016/j.bpj.2017.04.053_bib57) 2017; 27
McKillop (10.1016/j.bpj.2017.04.053_bib23) 1993; 65
Geeves (10.1016/j.bpj.2017.04.053_bib38) 1984; 5
Rynkiewicz (10.1016/j.bpj.2017.04.053_bib58) 2016; 609
Grey (10.1016/j.bpj.2017.04.053_bib11) 1956; 64
Criddle (10.1016/j.bpj.2017.04.053_bib39) 1985; 232
Ebashi (10.1016/j.bpj.2017.04.053_bib14) 1963; 200
Hanson (10.1016/j.bpj.2017.04.053_bib15) 1964; 160
Geeves (10.1016/j.bpj.2017.04.053_bib40) 1998; 75
Lehman (10.1016/j.bpj.2017.04.053_bib50) 2000; 302
Geeves (10.1016/j.bpj.2017.04.053_bib36) 2012; vol. 4
Carlson (10.1016/j.bpj.2017.04.053_bib49) 2002; 99
Lehman (10.1016/j.bpj.2017.04.053_bib28) 1972; 59
Huxley (10.1016/j.bpj.2017.04.053_bib18) 1972; 37
Parry (10.1016/j.bpj.2017.04.053_bib21) 1973; 75
Chalovich (10.1016/j.bpj.2017.04.053_bib55) 2002; 82
Bremel (10.1016/j.bpj.2017.04.053_bib25) 1972; 238
Weber (10.1016/j.bpj.2017.04.053_bib27) 1973; 53
Tobacman (10.1016/j.bpj.2017.04.053_bib35) 2000; 275
Li (10.1016/j.bpj.2017.04.053_bib61) 2010; 395
Smith (10.1016/j.bpj.2017.04.053_bib60) 2003; 84
Banga (10.1016/j.bpj.2017.04.053_bib5) 1942; 1
References_xml – volume: 257
  start-page: 8073
  year: 1982
  end-page: 8080
  ident: bib29
  article-title: Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Morris
– volume: 259
  start-page: 2070
  year: 1984
  end-page: 2072
  ident: bib33
  article-title: Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Morris
– volume: 368
  start-page: 65
  year: 1994
  end-page: 67
  ident: bib54
  article-title: Ca
  publication-title: Nature
  contributor:
    fullname: Vibert
– volume: 27
  start-page: R8
  year: 2017
  end-page: R13
  ident: bib57
  article-title: Tropomyosins
  publication-title: Curr. Biol.
  contributor:
    fullname: Hardeman
– volume: 160
  start-page: 449
  year: 1964
  end-page: 460
  ident: bib15
  article-title: The structure of actin filaments and the origin of the axial periodicity in the I-substance of vertebrate striated muscle
  publication-title: Proc. R. Soc. Lond. B Biol. Sci.
  contributor:
    fullname: Lowy
– volume: 75
  start-page: 33
  year: 1973
  end-page: 55
  ident: bib21
  article-title: Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Squire
– volume: 84
  start-page: 3155
  year: 2003
  end-page: 3167
  ident: bib60
  article-title: Cooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems
  publication-title: Biophys. J.
  contributor:
    fullname: Geeves
– volume: 37
  start-page: 341
  year: 1972
  end-page: 352
  ident: bib20
  article-title: X-ray evidence for a conformational change in actin-containing filaments of vertebrate striated muscle
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  contributor:
    fullname: Haselgrove
– volume: 107
  start-page: 682
  year: 2014
  end-page: 693
  ident: bib32
  article-title: In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation
  publication-title: Biophys. J.
  contributor:
    fullname: Dong
– volume: 71
  start-page: 161
  year: 2005
  end-page: 193
  ident: bib8
  article-title: The molecular mechanism of muscle contraction
  publication-title: Adv. Protein Chem.
  contributor:
    fullname: Holmes
– volume: 75
  start-page: 926
  year: 1998
  end-page: 937
  ident: bib40
  article-title: Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin
  publication-title: Biophys. J.
  contributor:
    fullname: Conibear
– volume: 275
  start-page: 27587
  year: 2000
  end-page: 27593
  ident: bib35
  article-title: A new model of cooperative myosin-thin filament binding
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Butters
– year: 1963
  ident: bib3
  article-title: Cell Physiology
  contributor:
    fullname: Giese
– volume: 65
  start-page: 693
  year: 1993
  end-page: 701
  ident: bib23
  article-title: Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
  publication-title: Biophys. J.
  contributor:
    fullname: Geeves
– volume: 11
  start-page: 235a
  year: 1971
  ident: bib16
  article-title: Cross-bridge movement and filament overlap
  publication-title: Biophys. J.
  contributor:
    fullname: Huxley
– volume: 82
  start-page: 1679
  year: 2002
  end-page: 1681
  ident: bib55
  article-title: Response to the letter by Geeves and Lehrer
  publication-title: Biophys. J.
  contributor:
    fullname: Chen
– volume: 38
  start-page: 1102
  year: 1999
  end-page: 1110
  ident: bib48
  article-title: Cooperativity and switching within the three-state model of muscle regulation
  publication-title: Biochemistry
  contributor:
    fullname: Geeves
– volume: 232
  start-page: 343
  year: 1985
  end-page: 349
  ident: bib39
  article-title: The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin
  publication-title: Biochem. J.
  contributor:
    fullname: Jeffries
– volume: 77
  start-page: 7209
  year: 1980
  end-page: 7213
  ident: bib47
  article-title: Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Taylor
– volume: 395
  start-page: 327
  year: 2010
  end-page: 339
  ident: bib61
  article-title: The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Fischer
– volume: 609
  start-page: 51
  year: 2016
  end-page: 58
  ident: bib58
  article-title: The propensity for tropomyosin twisting in the presence and absence of F-actin
  publication-title: Arch. Biochem. Biophys.
  contributor:
    fullname: Lehman
– volume: 369
  start-page: 34
  year: 2008
  end-page: 42
  ident: bib19
  article-title: Memories of early work on muscle contraction and regulation in the 1950’s and 1960’s
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Huxley
– volume: 534
  start-page: 724
  year: 2016
  end-page: 728
  ident: bib45
  article-title: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
  publication-title: Nature
  contributor:
    fullname: Raunser
– volume: 68
  start-page: 2S
  year: 1995
  end-page: 5S
  ident: bib51
  article-title: The actomyosin interaction and its control by tropomyosin
  publication-title: Biophys. J.
  contributor:
    fullname: Holmes
– volume: 53
  start-page: 612
  year: 1973
  end-page: 673
  ident: bib27
  article-title: Molecular control mechanisms in muscle contraction
  publication-title: Physiol. Rev.
  contributor:
    fullname: Murray
– volume: vol. 4
  start-page: 251
  year: 2012
  end-page: 267
  ident: bib36
  article-title: Thin filament regulation
  publication-title: Comprehensive Biophysics
  contributor:
    fullname: Geeves
– volume: 236
  start-page: 182
  year: 1972
  end-page: 183
  ident: bib22
  article-title: Structural changes in actin-containing filaments of muscle
  publication-title: Nat. New Biol.
  contributor:
    fullname: Poulsen
– volume: 519
  start-page: 114
  year: 2015
  end-page: 117
  ident: bib44
  article-title: Structure of the F-actin-tropomyosin complex
  publication-title: Nature
  contributor:
    fullname: Raunser
– volume: 37
  start-page: 361
  year: 1972
  end-page: 376
  ident: bib18
  article-title: Structural changes in actin- and myosin-containing filaments during contraction
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  contributor:
    fullname: Huxley
– volume: 84
  start-page: 3168
  year: 2003
  end-page: 3180
  ident: bib59
  article-title: Cooperative regulation of myosin-actin interactions by a continuous flexible chain II: actin-tropomyosin-troponin and regulation by calcium
  publication-title: Biophys. J.
  contributor:
    fullname: Geeves
– volume: 236
  start-page: 3198
  year: 1961
  end-page: 3202
  ident: bib13
  article-title: The role of calcium in the superprecipitation of actomyosin
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Winicur
– volume: 302
  start-page: 593
  year: 2000
  end-page: 606
  ident: bib50
  article-title: Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Craig
– volume: 52
  start-page: 215
  year: 1987
  end-page: 220
  ident: bib46
  article-title: Two-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actin
  publication-title: Biophys. J.
  contributor:
    fullname: Halsall
– volume: 266
  start-page: 8
  year: 1997
  end-page: 14
  ident: bib41
  article-title: Steric-model for activation of muscle thin filaments
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Lehman
– volume: 25
  start-page: 483
  year: 2004
  end-page: 487
  ident: bib24
  article-title: Fifty important papers in the history of muscle contraction and myosin motility
  publication-title: J. Muscle Res. Cell Motil.
  contributor:
    fullname: Szent-Györgyi
– volume: 277
  start-page: 1081
  year: 1998
  end-page: 1089
  ident: bib30
  article-title: The muscle thin filament as a classical cooperative/allosteric regulatory system
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Geeves
– volume: 105
  start-page: 483
  year: 2016
  end-page: 491
  ident: bib9
  article-title: Review: the ATPase mechanism of myosin and actomyosin
  publication-title: Biopolymers
  contributor:
    fullname: Geeves
– volume: 68
  start-page: 348s
  year: 1995
  ident: bib52
  article-title: Control of the actomyosin ATPase
  publication-title: Biophys. J.
  contributor:
    fullname: Lorenz
– volume: 5
  start-page: 351
  year: 1984
  end-page: 361
  ident: bib38
  article-title: Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle
  publication-title: J. Muscle Res. Cell Motil.
  contributor:
    fullname: Gutfreund
– volume: 348
  start-page: 217
  year: 1990
  end-page: 221
  ident: bib53
  article-title: Molecular structure of F-actin and location of surface binding sites
  publication-title: Nature
  contributor:
    fullname: Safer
– volume: 64
  start-page: 184
  year: 1956
  end-page: 192
  ident: bib11
  article-title: A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphatase
  publication-title: Biochem. J.
  contributor:
    fullname: Perry
– volume: 173
  start-page: 973
  year: 1954
  end-page: 976
  ident: bib1
  article-title: Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
  publication-title: Nature
  contributor:
    fullname: Hanson
– volume: 37
  start-page: 267
  year: 1972
  end-page: 275
  ident: bib26
  article-title: Manifestations of cooperative behavior in the regulated actin filament during actin-activated ATP hydrolysis in the presence of calcium
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  contributor:
    fullname: Weber
– volume: 164
  start-page: 1356
  year: 1969
  end-page: 1365
  ident: bib7
  article-title: The mechanism of muscular contraction
  publication-title: Science
  contributor:
    fullname: Huxley
– volume: 29
  start-page: 213
  year: 2008
  end-page: 219
  ident: bib56
  article-title: Gestalt-binding of tropomyosin to actin filaments
  publication-title: J. Muscle Res. Cell Motil.
  contributor:
    fullname: Lehman
– year: 1963
  ident: bib4
  article-title: Animal Physiology
  contributor:
    fullname: Scheer
– volume: 192
  start-page: 111
  year: 1986
  end-page: 131
  ident: bib37
  article-title: Tropomyosin crystal structure and muscle regulation
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Cohen
– volume: 99
  start-page: 2538
  year: 2002
  end-page: 2545
  ident: bib49
  article-title: Complexity and robustness
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Doyle
– volume: 125
  start-page: 85P
  year: 1971
  ident: bib17
  article-title: Structural changes during muscle contraction
  publication-title: Biochem. J.
  contributor:
    fullname: Huxley
– volume: 200
  start-page: 1010
  year: 1963
  ident: bib14
  article-title: Third component participating in the superprecipitation of “Natural Actomyosin”
  publication-title: Nature
  contributor:
    fullname: Ebashi
– volume: 10
  start-page: 4617
  year: 1971
  end-page: 4624
  ident: bib6
  article-title: Mechanism of adenosine triphosphate hydrolysis by actomyosin
  publication-title: Biochemistry
  contributor:
    fullname: Taylor
– volume: 238
  start-page: 599
  year: 1963
  end-page: 605
  ident: bib12
  article-title: The binding of calcium to actomyosin systems in relation to their biological activity
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Herz
– volume: 150
  start-page: 327
  year: 2012
  end-page: 338
  ident: bib43
  article-title: Structure of the rigor actin-tropomyosin-myosin complex
  publication-title: Cell
  contributor:
    fullname: Raunser
– volume: 29
  start-page: 15
  year: 1947
  end-page: 32
  ident: bib10
  article-title: The action of various cations on muscle protoplasm
  publication-title: J. Cell. Comp. Physiol.
  contributor:
    fullname: Wiercinski
– volume: 82
  start-page: 1677
  year: 2002
  end-page: 1681
  ident: bib31
  article-title: Modeling thin filament cooperativity
  publication-title: Biophys. J.
  contributor:
    fullname: Lehrer
– volume: 238
  start-page: 97
  year: 1972
  end-page: 101
  ident: bib25
  article-title: Cooperation within actin filament in vertebrate skeletal muscle
  publication-title: Nat. New Biol.
  contributor:
    fullname: Weber
– volume: 594
  start-page: 8
  year: 2016
  end-page: 17
  ident: bib34
  article-title: Structural determinants of muscle thin filament cooperativity
  publication-title: Arch. Biochem. Biophys.
  contributor:
    fullname: Lehman
– volume: 173
  start-page: 971
  year: 1954
  end-page: 973
  ident: bib2
  article-title: Structural changes in muscle during contraction; interference microscopy of living muscle fibres
  publication-title: Nature
  contributor:
    fullname: Niedergerke
– volume: 1
  start-page: 5
  year: 1942
  end-page: 15
  ident: bib5
  article-title: The phosphatase activity of myosin
  publication-title: Stud. Inst. Med. Chem. Univ. Szeged
  contributor:
    fullname: Banga
– volume: 155
  start-page: 273
  year: 2006
  end-page: 284
  ident: bib42
  article-title: A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle x-ray fibre diagrams from non-overlap muscle
  publication-title: J. Struct. Biol.
  contributor:
    fullname: Holmes
– volume: 59
  start-page: 375
  year: 1972
  end-page: 387
  ident: bib28
  article-title: Activation of the adenosine triphosphatase of actomyosin by tropomyosin
  publication-title: J. Gen. Physiol.
  contributor:
    fullname: Szent-Györgyi
– volume: 1
  start-page: 5
  year: 1942
  ident: 10.1016/j.bpj.2017.04.053_bib5
  article-title: The phosphatase activity of myosin
  publication-title: Stud. Inst. Med. Chem. Univ. Szeged
  contributor:
    fullname: Banga
– volume: 369
  start-page: 34
  year: 2008
  ident: 10.1016/j.bpj.2017.04.053_bib19
  article-title: Memories of early work on muscle contraction and regulation in the 1950’s and 1960’s
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2007.11.130
  contributor:
    fullname: Huxley
– volume: 65
  start-page: 693
  year: 1993
  ident: 10.1016/j.bpj.2017.04.053_bib23
  article-title: Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(93)81110-X
  contributor:
    fullname: McKillop
– volume: 75
  start-page: 926
  year: 1998
  ident: 10.1016/j.bpj.2017.04.053_bib40
  article-title: Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(98)77581-2
  contributor:
    fullname: Geeves
– volume: 11
  start-page: 235a
  year: 1971
  ident: 10.1016/j.bpj.2017.04.053_bib16
  article-title: Cross-bridge movement and filament overlap
  publication-title: Biophys. J.
  contributor:
    fullname: Huxley
– volume: 99
  start-page: 2538
  issue: Suppl 1
  year: 2002
  ident: 10.1016/j.bpj.2017.04.053_bib49
  article-title: Complexity and robustness
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.012582499
  contributor:
    fullname: Carlson
– volume: 277
  start-page: 1081
  year: 1998
  ident: 10.1016/j.bpj.2017.04.053_bib30
  article-title: The muscle thin filament as a classical cooperative/allosteric regulatory system
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1998.1654
  contributor:
    fullname: Lehrer
– volume: 238
  start-page: 97
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib25
  article-title: Cooperation within actin filament in vertebrate skeletal muscle
  publication-title: Nat. New Biol.
  doi: 10.1038/newbio238097a0
  contributor:
    fullname: Bremel
– volume: 64
  start-page: 184
  year: 1956
  ident: 10.1016/j.bpj.2017.04.053_bib11
  article-title: A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphatase
  publication-title: Biochem. J.
  doi: 10.1042/bj0640184
  contributor:
    fullname: Grey
– volume: 259
  start-page: 2070
  year: 1984
  ident: 10.1016/j.bpj.2017.04.053_bib33
  article-title: Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)43316-3
  contributor:
    fullname: Lehrer
– volume: 37
  start-page: 361
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib18
  article-title: Structural changes in actin- and myosin-containing filaments during contraction
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  doi: 10.1101/SQB.1973.037.01.046
  contributor:
    fullname: Huxley
– volume: 236
  start-page: 3198
  year: 1961
  ident: 10.1016/j.bpj.2017.04.053_bib13
  article-title: The role of calcium in the superprecipitation of actomyosin
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)93995-5
  contributor:
    fullname: Weber
– volume: 594
  start-page: 8
  year: 2016
  ident: 10.1016/j.bpj.2017.04.053_bib34
  article-title: Structural determinants of muscle thin filament cooperativity
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2016.02.016
  contributor:
    fullname: Moore
– volume: 38
  start-page: 1102
  year: 1999
  ident: 10.1016/j.bpj.2017.04.053_bib48
  article-title: Cooperativity and switching within the three-state model of muscle regulation
  publication-title: Biochemistry
  doi: 10.1021/bi981603e
  contributor:
    fullname: Maytum
– volume: 232
  start-page: 343
  year: 1985
  ident: 10.1016/j.bpj.2017.04.053_bib39
  article-title: The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin
  publication-title: Biochem. J.
  doi: 10.1042/bj2320343
  contributor:
    fullname: Criddle
– year: 1963
  ident: 10.1016/j.bpj.2017.04.053_bib4
  contributor:
    fullname: Scheer
– volume: 68
  start-page: 2S
  issue: 4, Suppl
  year: 1995
  ident: 10.1016/j.bpj.2017.04.053_bib51
  article-title: The actomyosin interaction and its control by tropomyosin
  publication-title: Biophys. J.
  contributor:
    fullname: Holmes
– volume: 368
  start-page: 65
  year: 1994
  ident: 10.1016/j.bpj.2017.04.053_bib54
  article-title: Ca2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
  publication-title: Nature
  doi: 10.1038/368065a0
  contributor:
    fullname: Lehman
– volume: 29
  start-page: 213
  year: 2008
  ident: 10.1016/j.bpj.2017.04.053_bib56
  article-title: Gestalt-binding of tropomyosin to actin filaments
  publication-title: J. Muscle Res. Cell Motil.
  doi: 10.1007/s10974-008-9157-6
  contributor:
    fullname: Holmes
– volume: 5
  start-page: 351
  year: 1984
  ident: 10.1016/j.bpj.2017.04.053_bib38
  article-title: Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle
  publication-title: J. Muscle Res. Cell Motil.
  doi: 10.1007/BF00818255
  contributor:
    fullname: Geeves
– volume: 395
  start-page: 327
  year: 2010
  ident: 10.1016/j.bpj.2017.04.053_bib61
  article-title: The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.10.060
  contributor:
    fullname: Li
– volume: 534
  start-page: 724
  year: 2016
  ident: 10.1016/j.bpj.2017.04.053_bib45
  article-title: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
  publication-title: Nature
  doi: 10.1038/nature18295
  contributor:
    fullname: von der Ecken
– volume: 257
  start-page: 8073
  year: 1982
  ident: 10.1016/j.bpj.2017.04.053_bib29
  article-title: Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)34298-4
  contributor:
    fullname: Lehrer
– volume: 275
  start-page: 27587
  year: 2000
  ident: 10.1016/j.bpj.2017.04.053_bib35
  article-title: A new model of cooperative myosin-thin filament binding
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M003648200
  contributor:
    fullname: Tobacman
– volume: 519
  start-page: 114
  year: 2015
  ident: 10.1016/j.bpj.2017.04.053_bib44
  article-title: Structure of the F-actin-tropomyosin complex
  publication-title: Nature
  doi: 10.1038/nature14033
  contributor:
    fullname: von der Ecken
– volume: 82
  start-page: 1677
  year: 2002
  ident: 10.1016/j.bpj.2017.04.053_bib31
  article-title: Modeling thin filament cooperativity
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(02)75518-5
  contributor:
    fullname: Geeves
– volume: 200
  start-page: 1010
  year: 1963
  ident: 10.1016/j.bpj.2017.04.053_bib14
  article-title: Third component participating in the superprecipitation of “Natural Actomyosin”
  publication-title: Nature
  doi: 10.1038/2001010a0
  contributor:
    fullname: Ebashi
– volume: 348
  start-page: 217
  year: 1990
  ident: 10.1016/j.bpj.2017.04.053_bib53
  article-title: Molecular structure of F-actin and location of surface binding sites
  publication-title: Nature
  doi: 10.1038/348217a0
  contributor:
    fullname: Milligan
– volume: 609
  start-page: 51
  year: 2016
  ident: 10.1016/j.bpj.2017.04.053_bib58
  article-title: The propensity for tropomyosin twisting in the presence and absence of F-actin
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2016.09.008
  contributor:
    fullname: Rynkiewicz
– volume: 173
  start-page: 973
  year: 1954
  ident: 10.1016/j.bpj.2017.04.053_bib1
  article-title: Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
  publication-title: Nature
  doi: 10.1038/173973a0
  contributor:
    fullname: Huxley
– volume: 173
  start-page: 971
  year: 1954
  ident: 10.1016/j.bpj.2017.04.053_bib2
  article-title: Structural changes in muscle during contraction; interference microscopy of living muscle fibres
  publication-title: Nature
  doi: 10.1038/173971a0
  contributor:
    fullname: Huxley
– volume: 29
  start-page: 15
  year: 1947
  ident: 10.1016/j.bpj.2017.04.053_bib10
  article-title: The action of various cations on muscle protoplasm
  publication-title: J. Cell. Comp. Physiol.
  doi: 10.1002/jcp.1030290103
  contributor:
    fullname: Heilbrunn
– volume: 150
  start-page: 327
  year: 2012
  ident: 10.1016/j.bpj.2017.04.053_bib43
  article-title: Structure of the rigor actin-tropomyosin-myosin complex
  publication-title: Cell
  doi: 10.1016/j.cell.2012.05.037
  contributor:
    fullname: Behrmann
– volume: 37
  start-page: 267
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib26
  article-title: Manifestations of cooperative behavior in the regulated actin filament during actin-activated ATP hydrolysis in the presence of calcium
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  doi: 10.1101/SQB.1973.037.01.037
  contributor:
    fullname: Bremel
– volume: 75
  start-page: 33
  year: 1973
  ident: 10.1016/j.bpj.2017.04.053_bib21
  article-title: Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(73)90527-5
  contributor:
    fullname: Parry
– volume: 84
  start-page: 3155
  year: 2003
  ident: 10.1016/j.bpj.2017.04.053_bib60
  article-title: Cooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(03)70040-X
  contributor:
    fullname: Smith
– volume: 10
  start-page: 4617
  year: 1971
  ident: 10.1016/j.bpj.2017.04.053_bib6
  article-title: Mechanism of adenosine triphosphate hydrolysis by actomyosin
  publication-title: Biochemistry
  doi: 10.1021/bi00801a004
  contributor:
    fullname: Lymn
– volume: 53
  start-page: 612
  year: 1973
  ident: 10.1016/j.bpj.2017.04.053_bib27
  article-title: Molecular control mechanisms in muscle contraction
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.1973.53.3.612
  contributor:
    fullname: Weber
– volume: 125
  start-page: 85P
  year: 1971
  ident: 10.1016/j.bpj.2017.04.053_bib17
  article-title: Structural changes during muscle contraction
  publication-title: Biochem. J.
  doi: 10.1042/bj1250085P
  contributor:
    fullname: Huxley
– year: 1963
  ident: 10.1016/j.bpj.2017.04.053_bib3
  contributor:
    fullname: Giese
– volume: 59
  start-page: 375
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib28
  article-title: Activation of the adenosine triphosphatase of actomyosin by tropomyosin
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.59.4.375
  contributor:
    fullname: Lehman
– volume: 82
  start-page: 1679
  year: 2002
  ident: 10.1016/j.bpj.2017.04.053_bib55
  article-title: Response to the letter by Geeves and Lehrer
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(02)75519-7
  contributor:
    fullname: Chalovich
– volume: 77
  start-page: 7209
  year: 1980
  ident: 10.1016/j.bpj.2017.04.053_bib47
  article-title: Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.77.12.7209
  contributor:
    fullname: Trybus
– volume: 25
  start-page: 483
  year: 2004
  ident: 10.1016/j.bpj.2017.04.053_bib24
  article-title: Fifty important papers in the history of muscle contraction and myosin motility
  publication-title: J. Muscle Res. Cell Motil.
  doi: 10.1007/s10974-004-4839-1
  contributor:
    fullname: Ostap
– volume: 238
  start-page: 599
  year: 1963
  ident: 10.1016/j.bpj.2017.04.053_bib12
  article-title: The binding of calcium to actomyosin systems in relation to their biological activity
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)81304-7
  contributor:
    fullname: Weber
– volume: 164
  start-page: 1356
  year: 1969
  ident: 10.1016/j.bpj.2017.04.053_bib7
  article-title: The mechanism of muscular contraction
  publication-title: Science
  doi: 10.1126/science.164.3886.1356
  contributor:
    fullname: Huxley
– volume: 105
  start-page: 483
  year: 2016
  ident: 10.1016/j.bpj.2017.04.053_bib9
  article-title: Review: the ATPase mechanism of myosin and actomyosin
  publication-title: Biopolymers
  doi: 10.1002/bip.22853
  contributor:
    fullname: Geeves
– volume: 155
  start-page: 273
  year: 2006
  ident: 10.1016/j.bpj.2017.04.053_bib42
  article-title: A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle x-ray fibre diagrams from non-overlap muscle
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2006.02.020
  contributor:
    fullname: Poole
– volume: 84
  start-page: 3168
  year: 2003
  ident: 10.1016/j.bpj.2017.04.053_bib59
  article-title: Cooperative regulation of myosin-actin interactions by a continuous flexible chain II: actin-tropomyosin-troponin and regulation by calcium
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(03)70041-1
  contributor:
    fullname: Smith
– volume: 160
  start-page: 449
  year: 1964
  ident: 10.1016/j.bpj.2017.04.053_bib15
  article-title: The structure of actin filaments and the origin of the axial periodicity in the I-substance of vertebrate striated muscle
  publication-title: Proc. R. Soc. Lond. B Biol. Sci.
  doi: 10.1098/rspb.1964.0055
  contributor:
    fullname: Hanson
– volume: 27
  start-page: R8
  year: 2017
  ident: 10.1016/j.bpj.2017.04.053_bib57
  article-title: Tropomyosins
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2016.11.033
  contributor:
    fullname: Gunning
– volume: 192
  start-page: 111
  year: 1986
  ident: 10.1016/j.bpj.2017.04.053_bib37
  article-title: Tropomyosin crystal structure and muscle regulation
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(86)90468-7
  contributor:
    fullname: Phillips
– volume: 302
  start-page: 593
  year: 2000
  ident: 10.1016/j.bpj.2017.04.053_bib50
  article-title: Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2000.4080
  contributor:
    fullname: Lehman
– volume: 68
  start-page: 348s
  year: 1995
  ident: 10.1016/j.bpj.2017.04.053_bib52
  article-title: Control of the actomyosin ATPase
  publication-title: Biophys. J.
  contributor:
    fullname: Poole
– volume: 236
  start-page: 182
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib22
  article-title: Structural changes in actin-containing filaments of muscle
  publication-title: Nat. New Biol.
  doi: 10.1038/newbio236182a0
  contributor:
    fullname: Vibert
– volume: 107
  start-page: 682
  year: 2014
  ident: 10.1016/j.bpj.2017.04.053_bib32
  article-title: In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2014.05.044
  contributor:
    fullname: Li
– volume: vol. 4
  start-page: 251
  year: 2012
  ident: 10.1016/j.bpj.2017.04.053_bib36
  article-title: Thin filament regulation
  contributor:
    fullname: Geeves
– volume: 52
  start-page: 215
  year: 1987
  ident: 10.1016/j.bpj.2017.04.053_bib46
  article-title: Two-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actin
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(87)83208-3
  contributor:
    fullname: Geeves
– volume: 37
  start-page: 341
  year: 1972
  ident: 10.1016/j.bpj.2017.04.053_bib20
  article-title: X-ray evidence for a conformational change in actin-containing filaments of vertebrate striated muscle
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  doi: 10.1101/SQB.1973.037.01.044
  contributor:
    fullname: Haselgrove
– volume: 71
  start-page: 161
  year: 2005
  ident: 10.1016/j.bpj.2017.04.053_bib8
  article-title: The molecular mechanism of muscle contraction
  publication-title: Adv. Protein Chem.
  doi: 10.1016/S0065-3233(04)71005-0
  contributor:
    fullname: Geeves
– volume: 266
  start-page: 8
  year: 1997
  ident: 10.1016/j.bpj.2017.04.053_bib41
  article-title: Steric-model for activation of muscle thin filaments
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1996.0800
  contributor:
    fullname: Vibert
SSID ssj0012501
Score 2.4252758
Snippet BJ Classic highlighting the article “Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament.”
BJ Classic highlighting the article "Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament."
Before the introduction of in vitro motility assays, the actin-activated myosin ATPase was (and still is) commonly used as a benchtop analog of...
SourceID pubmedcentral
proquest
crossref
pubmed
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 2459
SubjectTerms Actin
Actin Cytoskeleton
Actins
Actomyosin
Adenosine triphosphatase
BJ Classics
Calcium-binding protein
Contraction
Filaments
Humans
In vitro testing
Motor task performance
Muscles
Muscular system
Myosin
Myosin ATPase
Myosin Subfragments
Myosins
Proteins
Regulatory proteins
Switches
Switching
Tropomyosin
Troponin
SummonAdditionalLinks – databaseName: Open Access: Elsevier Open Archive Journals
  dbid: ABVKL
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3bbtQwEB2VVki8IO4sFGQknpCsZn3JhbdSUSrKUgla1DfLcSZqqlV2xe624m_4Fr6MmcRZsSB44DGJbSVnJuNj-XgG4KUtCHpfWVkl1kqDRSnLLElkoU0olUJUGZ9GnnxMj87M-3N7vgUHw1kYllXG2N_H9C5axzt7Ec29edPwGV-aXonfj8lJidWkN2CHc5mTa-_sv_ly_GG9mUCzfCycl0ruMGxudjKvcn7JAq-sS3hq9d-mpz_p5-8qyl-mpcM7cDvySbHfv_Jd2ML2HtzsK0x-uw_l5-tm2cklxWS1YAWcOGmFbytxUteiaQWrvBavBXnLj--TcNxMp7O5fId4RS1Pyc4oOzoquGbaVMzqOIz41NewJ6s-gLPDt6cHRzKWVZCB6NJSaq2xVp7z5qi0zosalaeFiM8KFcoE06B9obLcE5QlhUpTBeIkFS3N0pCrMab6IWy3sxYfg0BCP9A4tSeaoLHIc1qe6GCy1NqgsB7BqwFNN--zZ7hBVnbpCHrH0LvEOIJ-BGbA2224gKPo_q9uu4NtXPz_Fo55K5FV4lMjeLF-TH8Ob4f4FmcrbpNow_ui4xE86k25fkmVW1qhj2nwbMPI6waclXvzSdtcdNm5reGcZ8mT__uap3CLr1iMppJd2F5-XeEzoj3L8nl06592ev8u
  priority: 102
  providerName: Elsevier
Title Switching Muscles On and Off in Steps: The McKillop-Geeves Three-State Model of Muscle Regulation
URI https://dx.doi.org/10.1016/j.bpj.2017.04.053
https://www.ncbi.nlm.nih.gov/pubmed/28552313
https://www.proquest.com/docview/1923045066
https://search.proquest.com/docview/1903438581
https://pubmed.ncbi.nlm.nih.gov/PMC5479050
Volume 112
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LbxMxEB41RUhcEO8ulMhInJDcbPzYB7e2ohRKKIIW5WbZXq_YKnUikoD4N_wWfhnj3XVEQXDg7Idsz9jzjebzDMBTWeLR60rSKpWSClcaavI0pSUX1jDmHMvDb-TJ2-z4XLyeyukWyPgXpiXtW9Ps-dnlnm8-tdzKxaUdRZ7Y6N3kUIqQViodDWCA5je66H3oAG16XyYvoxzhfwxltqQus7gIdK68TW8qQxEdVkj0xcb8b3bpT9z5O33yF3t0dAtu9kCS7HcLvg1bzt-B611pyW93wXz42qxaniSZrJdhS-TUE-0rclrXpPEk0LuWzwmqyY_vE3vSzGbzBX3p3BfseYYCdrTFoSQUS5uRed1PQ953xetRnPfg_OjF2eEx7espUIs4aUU5565mOiTMYVldlLVjGj0QnZfMmtRlluuS5YWWWWnwjRSVRTBSoU-W2YKNXcbvw7afe7cDxCEwszhPrREfcFcWBfol3Io8k9IyVyfwLJ6mWnRpM1Tkk10olIIKUlCpUCiFBEQ8b9Xb_c6eK3zW_zVsN8pG9RdvqQJgRZSKQCqBJ5tmvDIhDqK9m69Dn5SLEBAdJ_CgE-VmkVEdEsivCHnTIaTjvtqCWtqm5e618uF_j3wEN8L2AhGNpbuwvfq8do8R8qzMEK7tH3w8eTOEwavpwbBV-J8YoADz
link.rule.ids 230,314,727,780,784,885,3506,27569,27924,27925,45663,45874,53791,53793
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9NAEB6VIgQXVN6hpSwSJ6RVnX3Z7o1WtCltWglSKbfVer0WriInapIi_g2_hV_GjB8RAdFDr971yp6ZnflW8-0MwHudouhdrnkeac1VSDOexVHEU6l8JkQIIqbbyMNzM7hUn8d6vAGH3V0YolW2vr_x6bW3bp_stdLcm5Ul3fHF8Ir4vo9GiqjG3IP7SicxFdA_GR-sUgkY49u2eYbT9C61WZO8stkV0bviutyplv8LTv-Cz785lH8EpaMteNyiSfax-eAnsBGqp_Cg6S_54xlkX7-Xi5osyYbLOfHf2EXFXJWzi6JgZcWI4zXfZ2grv34O_Wk5mUxn_DiEG5w5Qi0HXoNRRh3TJmxatMuwL00He9Tpc7g8-jQ6HPC2qQL3CJYWXEoZCuGoao4wRZIWQTg8hrg4FT6LgvHSpSJOnDZpho5S5R4RSY4HM-MT0Q9GvoDNalqFV8ACyt7jOoVDkCBDmiR4OJFexUZrL0LRgw-dNO2sqZ1hO1LZlUXRWxK9jZRF0fdAdfK2awZg0bff9tpOpxvb7r65JdSKUBXRVA_erYZx31AyxFVhuqQ5kVSUFe334GWjytVHikTj-byPi8drSl5NoJrc6yNV-a2uza0VVTyLXt_tb97Cw8FoeGbPTs5Pt-ERjRAtTUQ7sLm4XoY3CIAW2W5t4L8Bn-YBCA
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbhQxEC1BEIgLYqdDACNxQnKmx0sv3FBgCIRJIkik3CzbbYuOJp5WZgbE3_AtfBnlXkYJCA6c7bZsv7Lrlfy6CuCFLHHrdSVplUpJhSsNNXma0pILaxhzjuXxb-TpfrZ7LD6cyJMLpb5a0b419XaYnW2H-kurrWzO7GjQiY0OpztSxLRS6aip_OgqXJMcjWwI1PsHBPTsfbG8jHIMAoYHzVbaZZrTKOrK2ySnMpbSYYXEiGzM_-ad_mSfv4soL3ilyW241dNJ8rqb9h244sJduN4VmPx-D8znb_WyVUuS6WoRF0YOAtGhIgfekzqQKPJavCJoLD9_TO1ePZvNG_rOua_Y8whhdrRloySWTJuRue-HIZ-6EvYI6n04nrw92tmlfVUFapEtLSnn3HmmY9oclvmi9I5pjEN0XjJrUpdZrkuWF1pmpcGbUlQWKUmFkVlmCzZ2GX8AG2Ee3CMgDumZxXG8RpbAXVkUGJ1wK_JMSsucT-DlsJuq6ZJnqEFVdqoQBRVRUKlQiEICYthv1Xv_zqsrvNz_9dnWgI3qj99CRdqKXBXpVALP1814cOJriA5uvop9Ui7is-g4gYcdlOtJDuaQQH4J5HWHmJT7cgvaapucu7fNzf_-8hncOHwzUR_f7-89hptxpVGZxtIt2Fier9wT5EBL87S19l9j3gLE
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=Switching+Muscles+On+and+Off+in+Steps%3A+The+McKillop-Geeves+Three-State+Model+of+Muscle+Regulation&rft.jtitle=Biophysical+journal&rft.au=Lehman%2C+William&rft.date=2017-06-20&rft.pub=Biophysical+Society&rft.issn=0006-3495&rft.eissn=1542-0086&rft.volume=112&rft.issue=12&rft.spage=2459&rft_id=info:doi/10.1016%2Fj.bpj.2017.04.053&rft.externalDBID=HAS_PDF_LINK
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3495&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3495&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3495&client=summon