Single-molecule imaging and manipulation of biomolecular machines and systems

Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration. We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1862; no. 2; pp. 241 - 252
Main Authors Iino, Ryota, Iida, Tatsuya, Nakamura, Akihiko, Saita, Ei-ichiro, You, Huijuan, Sako, Yasushi
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.02.2018
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration. We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems. Single-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines. Quantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: “What is life?” This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato. •Single-molecule imaging reveals operation mechanisms of motor proteins.•Single-molecule manipulation reveals mechanical properties of motor proteins.•Single-molecule imaging reveals signaling mechanisms of proteins in living cells.
AbstractList Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration.We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems.Single-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines.Quantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: “What is life?” This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration.BACKGROUNDBiological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration.We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems.SCOPE OF REVIEWWe provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems.Single-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines.MAJOR CONCLUSIONSSingle-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines.Quantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: "What is life?" This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.GENERAL SIGNIFICANCEQuantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: "What is life?" This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration. We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems. Single-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines. Quantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: “What is life?” This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato. •Single-molecule imaging reveals operation mechanisms of motor proteins.•Single-molecule manipulation reveals mechanical properties of motor proteins.•Single-molecule imaging reveals signaling mechanisms of proteins in living cells.
Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and migration. We provide an overview of single-molecule imaging methods involving both small and large probes used to monitor the dynamic motions of molecular machines in vitro (purified proteins) and in living cells, and single-molecule manipulation methods used to measure the forces, mechanical properties and responses of biomolecules. We also introduce several examples of single-molecule analysis, focusing primarily on motor proteins and signal transduction systems. Single-molecule analysis is a powerful approach to unveil the operational mechanisms both of individual molecular machines and of systems consisting of many molecular machines. Quantitative, high-resolution single-molecule analyses of biomolecular systems at the various hierarchies of life will help to answer our fundamental question: "What is life?" This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
Author Nakamura, Akihiko
Saita, Ei-ichiro
Iino, Ryota
Sako, Yasushi
Iida, Tatsuya
You, Huijuan
Author_xml – sequence: 1
  givenname: Ryota
  surname: Iino
  fullname: Iino, Ryota
  email: iino@ims.ac.jp
  organization: Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Japan
– sequence: 2
  givenname: Tatsuya
  surname: Iida
  fullname: Iida, Tatsuya
  organization: Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Japan
– sequence: 3
  givenname: Akihiko
  surname: Nakamura
  fullname: Nakamura, Akihiko
  organization: Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Japan
– sequence: 4
  givenname: Ei-ichiro
  surname: Saita
  fullname: Saita, Ei-ichiro
  organization: Information Processing Biology Unit, Okinawa Institute of Science and Technology Graduate University, Japan
– sequence: 5
  givenname: Huijuan
  surname: You
  fullname: You, Huijuan
  email: youhuijuan@hust.edu.cn
  organization: School of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, China
– sequence: 6
  givenname: Yasushi
  surname: Sako
  fullname: Sako, Yasushi
  email: sako@riken.jp
  organization: Cellular Informatics Laboratory, RIKEN, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28789884$$D View this record in MEDLINE/PubMed
BookMark eNqFkU9v1DAQxS3Uim4L3wChHLkkjB07cTggoap_kFpxAM6WY48XrxJ7sROkfnvc7vbCgc5lpJnfe4f3zslJiAEJeUehoUC7j7tmHPUWQ8OA9g3IBkC-Ihsqe1ZLgO6EbKAFXnPaiTNynvMOyohBvCZnTPZykJJvyP13H7YT1nOc0KwTVn7W23KqdLDVrIPfr5NefAxVdNXo45HTqTzNLx8wP5H5IS845zfk1Okp49vjviA_r69-XN7Wd99uvl5-uatNO4ilRkFd67BrO86FBGetpm6wlhrh0AjsW0TLR8HcaMqbtwboMEohJXDeUWwvyIeD7z7F3yvmRc0-G5wmHTCuWTFgIHuAgb2I0oH1YuCcQUHfH9F1nNGqfSphpAf1nFYBPh0Ak2LOCZ0yfnlKZ0naT4qCeqxG7dShGvVYjQKpSjVFzP8RP_u_IPt8kGHJ84_HpLLxGAxan9Asykb_f4O_TjiqJA
CitedBy_id crossref_primary_10_1038_s41467_018_06362_3
crossref_primary_10_1038_s41467_024_45570_y
crossref_primary_10_1038_s41598_020_58070_y
crossref_primary_10_1016_j_synbio_2025_02_007
crossref_primary_10_1021_acsphotonics_9b00953
crossref_primary_10_3390_molecules29245828
crossref_primary_10_3390_bios8040100
crossref_primary_10_3390_ijms22105071
crossref_primary_10_1016_j_bpj_2018_11_016
crossref_primary_10_1007_s12551_017_0366_3
crossref_primary_10_1016_j_bbagen_2019_05_005
crossref_primary_10_3389_fphy_2022_855417
Cites_doi 10.1016/j.celrep.2016.07.047
10.1016/j.bbrc.2006.01.126
10.1038/nature04003
10.1016/j.bpj.2013.02.044
10.1016/j.tibs.2016.09.006
10.1038/370621a0
10.1038/nature03528
10.1126/science.1205510
10.1146/annurev.biochem.66.1.717
10.1016/j.bpj.2010.01.011
10.1038/365721a0
10.1038/nature03277
10.1074/jbc.M116.752048
10.2142/biophysico.13.0_1
10.1002/iub.1120
10.1038/35073513
10.1063/1.4813280
10.1074/jbc.M113.506329
10.1038/msb4100100
10.1038/342154a0
10.1073/pnas.1422885112
10.1126/science.271.5250.795
10.1038/nmeth1024
10.1364/OL.19.000780
10.1103/PhysRevLett.104.218103
10.1016/j.bpj.2010.12.3700
10.1021/nl500234t
10.1093/nar/gkw881
10.1073/pnas.0510570103
10.1016/S0006-3495(01)76236-4
10.1038/nature06716
10.1146/annurev.biochem.77.070606.101543
10.1126/science.1208386
10.1074/jbc.M111.262675
10.1016/S0014-5793(97)00359-1
10.1146/annurev-biochem-060713-035546
10.1126/science.1084398
10.1038/ncomms10372
10.1146/annurev.biophys.050708.133751
10.7554/eLife.05413
10.1146/annurev.biochem.72.121801.161737
10.2183/pjab.93.004
10.1016/j.sbi.2015.02.013
10.1016/j.tibs.2015.08.005
10.1038/nature09450
10.1021/cr400344n
10.1038/35004044
10.1364/OE.22.009159
10.1126/science.276.5314.917
10.1038/386299a0
10.1038/nmeth929
10.1073/pnas.0510191103
10.1146/annurev.biophys.36.040306.132700
10.1093/nar/gku581
10.1038/nchembio.443
10.1126/science.1140468
10.1038/nature04268
10.1016/j.tibs.2016.09.010
10.1126/science.1063951
10.1038/ncomms4975
10.7554/eLife.20378
10.1016/j.cell.2007.05.020
10.1017/S0033583510000107
10.1073/pnas.0436796100
10.1038/35051126
10.1016/j.cell.2007.04.038
10.1016/j.jmb.2006.06.016
10.1364/OL.42.000831
10.1016/j.copbio.2010.09.011
10.1016/j.cell.2011.01.033
10.1017/S0033583508004691
10.1126/science.aak9913
10.1016/S0006-3495(02)75672-5
10.1038/nchembio.2028
10.1126/science.276.5315.1109
10.1126/science.1067470
10.1074/jbc.M114.598177
10.1016/j.tibs.2015.11.004
10.1038/ncomms2026
10.1038/nature02212
10.1016/S1097-2765(03)00481-7
10.1016/j.ymeth.2016.06.019
10.1146/annurev.biochem.72.121801.161542
10.1038/ncb1009
10.1038/nmeth.1208
10.1007/978-1-59745-483-4_30
10.1007/s12013-007-0010-0
10.1038/nchembio.232
10.1146/annurev.biophys.36.101106.101451
10.1016/j.molcel.2015.02.033
10.1146/annurev-biophys-051013-022754
10.1038/nmeth.1218
10.1073/pnas.0306713101
10.1146/annurev.biophys.26.1.373
10.1038/330672a0
10.1126/science.1127344
10.1038/368113a0
10.1146/annurev.biophys.37.032807.125908
10.1038/nnano.2016.140
10.1371/journal.pone.0011639
10.1038/ncomms2631
10.1083/jcb.200411005
10.1021/ac502408c
10.1038/nchembio.715
10.1016/j.molcel.2011.01.008
10.1038/nbt927
ContentType Journal Article
Copyright 2017 Elsevier B.V.
Copyright © 2017 Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2017 Elsevier B.V.
– notice: Copyright © 2017 Elsevier B.V. All rights reserved.
DBID AAYXX
CITATION
NPM
7X8
7S9
L.6
DOI 10.1016/j.bbagen.2017.08.008
DatabaseName CrossRef
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitle CrossRef
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList AGRICOLA
MEDLINE - Academic

PubMed
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
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EISSN 1872-8006
EndPage 252
ExternalDocumentID 28789884
10_1016_j_bbagen_2017_08_008
S0304416517302532
Genre Research Support, Non-U.S. Gov't
Journal Article
Review
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
3O-
4.4
457
4G.
53G
5GY
5RE
5VS
7-5
71M
8P~
9JM
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AAXUO
ABEFU
ABFNM
ABGSF
ABMAC
ABUDA
ABXDB
ABYKQ
ACDAQ
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEHWI
AEKER
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
CS3
DOVZS
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OHT
OZT
P-8
P-9
PC.
Q38
R2-
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSU
SSZ
T5K
UQL
WH7
WUQ
XJT
XPP
~G-
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACRPL
ACVFH
ADCNI
ADNMO
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
BNPGV
CITATION
SSH
-~X
.55
.GJ
AAYJJ
ABJNI
AFFNX
AI.
F5P
H~9
K-O
MVM
NPM
RIG
TWZ
UHS
VH1
X7M
Y6R
YYP
ZE2
ZGI
~KM
7X8
7S9
L.6
ID FETCH-LOGICAL-c395t-e51f3fe63644580fdda1f9dd1c5fec5e73eed4b52fbc80f43c019b858804461e3
IEDL.DBID .~1
ISSN 0304-4165
0006-3002
IngestDate Fri Jul 11 07:30:37 EDT 2025
Thu Jul 10 22:32:31 EDT 2025
Mon Jul 21 06:05:21 EDT 2025
Tue Jul 01 00:22:09 EDT 2025
Thu Apr 24 23:06:58 EDT 2025
Fri Feb 23 02:34:15 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 2
Keywords Molecular machines
iSCAT
Single-molecule imaging
STED
AFM
Single-molecule manipulation
ADP
G4
Motor proteins
GFP
Signal transduction
S/N
FCS
ICS
Pi
FRET
TIR
ATP
Language English
License Copyright © 2017 Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c395t-e51f3fe63644580fdda1f9dd1c5fec5e73eed4b52fbc80f43c019b858804461e3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
PMID 28789884
PQID 1927594420
PQPubID 23479
PageCount 12
ParticipantIDs proquest_miscellaneous_2020870092
proquest_miscellaneous_1927594420
pubmed_primary_28789884
crossref_citationtrail_10_1016_j_bbagen_2017_08_008
crossref_primary_10_1016_j_bbagen_2017_08_008
elsevier_sciencedirect_doi_10_1016_j_bbagen_2017_08_008
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate February 2018
2018-02-00
20180201
PublicationDateYYYYMMDD 2018-02-01
PublicationDate_xml – month: 02
  year: 2018
  text: February 2018
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta
PublicationYear 2018
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References You, Lattmann, Rhodes, Yan (bb0390) 2017; 45
Larson, Landick, Block (bb0010) 2011; 41
Carter, Cross (bb0285) 2005; 435
Pyle (bb0355) 2008; 37
Igarashi, Uchihashi, Koivula, Wada, Kimura, Okamoto, Penttila, Ando, Samejima (bb0125) 2011; 333
Jarmoskaite, Russell (bb0350) 2014; 83
Yanagida, Ishii (bb0015) 2017; 93
Smith, Cui, Bustamante (bb0335) 1996; 271
Levi, Gratton (bb0445) 2007; 48
Iwane, Funatsu, Harada, Tokunaga, Ohara, Morimoto, Yanagida (bb0160) 1997; 407
Kodera, Yamamoto, Ishikawa, Ando (bb0250) 2010; 468
Rodriguez, Campbell, Lin, Lin, Miyawaki, Palmer, Shu, Zhang, Tsien (bb0165) 2017; 42
Tran, Schilling, Wirbelauer, Hess, Nagamine (bb0400) 2004; 13
Ortega Arroyo, Andrecka, Spillane, Billington, Takagi, Sellers, Kukura (bb0505) 2014; 14
Iino, Ueno, Minagawa, Suzuki, Murata (bb0115) 2015; 31
Toprak, Selvin (bb0180) 2007; 36
Andrecka, Ortega Arroyo, Takagi, de Wit, Fineberg, MacKinnon, Young, Sellers, Kukura (bb0510) 2015; 4
Imamura, Nakano, Noji, Muneyuki, Ohkuma, Yoshida, Yokoyama (bb0100) 2003; 100
Hell, Wichmann (bb0520) 1994; 19
Lin, Chang, Hsieh (bb0515) 2014; 22
Gao, Nienhaus (bb0425) 2017; 42
Iino, Noji (bb0095) 2013; 65
Alivisatos (bb0195) 2004; 22
Nakamura, Hibino, Yanagida, Sako (bb0480) 2016; 13
Ueno, Minagawa, Hara, Rahman, Yamato, Muneyuki, Noji, Murata, Iino (bb0120) 2014; 289
Sako, Minoghchi, Yanagida (bb0490) 2000; 2
Wen, Lancaster, Hodges, Zeri, Yoshimura, Noller, Bustamante, Tinoco (bb0030) 2008; 452
Bustamante, Chemla, Forde, Izhaky (bb0145) 2004; 73
Yodh, Schlierf, Ha (bb0375) 2010; 43
Hibino, Shibata, Yanagida, Sako (bb0485) 2011; 286
Iino, Koyama, Kusumi (bb0495) 2001; 80
Abrahams, Leslie, Lutter, Walker (bb0235) 1994; 370
Nakada, Ritchie, Oba, Nakamura, Hotta, Iino, Kasai, Yamaguchi, Fujiwara, Kusumi (bb0455) 2003; 5
Woodside, Block (bb0380) 2014; 43
Kubitscheck, Grunwald, Hoekstra, Rohleder, Kues, Siebrasse, Peters (bb0470) 2005; 168
Hodeib, Raj, Manosas, Zhang, Bagchi, Ducos, Allemand, Bensimon, Croquette (bb0370) 2016; 105
Arata, Hiroshima, Pack, Ramanujam, Motegi, Nakazato, Shindo, Wiseman, Sawa, Kobayashi, Brandao, Shibata, Sako (bb0460) 2016; 16
Saxton, Jacobson (bb0185) 1997; 26
Houdusse, Sweeney (bb0230) 2016; 41
Teng, Ishitsuka, Ren, Youn, Deng, Ge, Belmont, Selvin (bb0440) 2016; 5
Fukuda, Uchihashi, Iino, Okazaki, Yoshida, Igarashi, Ando (bb0135) 2013; 84
Paschal, King, Moss, Collins, Vallee, Witman (bb0060) 1987; 330
Shiroguchi, Kinosita (bb0245) 2007; 316
Dessinges, Lionnet, Xi, Bensimon, Croquette (bb0360) 2004; 101
Roy, Hohng, Ha (bb0190) 2008; 5
Boehr, Nussinov, Wright (bb0270) 2009; 5
Johnson, Bai, Smith, Patel, Wang (bb0365) 2007; 129
Nakamura, Tasaki, Ishiwata, Yamamoto, Okuni, Visootsat, Maximilien, Noji, Uchiyama, Samejima, Igarashi, Iino (bb0130) 2016; 291
Ulbrich, Isacoff (bb0500) 2007; 4
Noji, Yasuda, Yoshida, Kinosita (bb0090) 1997; 386
Ritter, Veith, Veenendaal, Siebrasse, Kubitscheck (bb0540) 2010; 5
Sako (bb0415) 2006; 2
Finer, Simmons, Spudich (bb0040) 1994; 368
Howard, Hudspeth, Vale (bb0050) 1989; 342
Ueno, Nishikawa, Iino, Tabata, Sakakihara, Yanagida, Noji (bb0205) 2010; 98
Bustamante, Cheng, Mejia (bb0035) 2011; 144
Abbondanzieri, Greenleaf, Shaevitz, Landick, Block (bb0025) 2005; 438
Shibata, Hibino, Mashimo, Yanagida, Sako (bb0450) 2006; 342
Gosse, Croquette (bb0325) 2002; 82
Sako, Yanagida (bb0405) 2003
Chen, Fu, Zhu, Cong, Nakamura, Yan (bb0330) 2011; 100
Isojima, Iino, Niitani, Noji, Tomishige (bb0215) 2016; 12
Sowa, Rowe, Leake, Yakushi, Homma, Ishijima, Berry (bb0255) 2005; 437
Saita, Suzuki, Kinosita, Yoshida (bb0320) 2015; 112
Watanabe, Iino, Noji (bb0305) 2010; 6
Yildiz, Forkey, McKinney, Ha, Goldman, Selvin (bb0175) 2003; 300
Boyer (bb0085) 1997; 66
Cotter, Stransky, McGuire, Forgac (bb0105) 2015; 40
Yasuda, Noji, Yoshida, Kinosita, Itoh (bb0310) 2001; 410
Karagiannis, Ishii, Yanagida (bb0045) 2014; 114
Ueda, Sako, Tanaka, Devreotes, Yanagida (bb0020) 2001; 294
Watanabe, Mitchison (bb0465) 2002; 295
Efros, Nesbitt (bb0200) 2016; 11
Rondelez, Tresset, Nakashima, Kato-Yamada, Fujita, Takeuchi, Noji (bb0280) 2005; 433
Svoboda, Schmidt, Schnapp, Block (bb0055) 1993; 365
Igarashi, Uchihashi, Uchiyama, Sugimoto, Wada, Suzuki, Sakuda, Ando, Watanabe, Samejima (bb0140) 2014; 5
Rief, Gautel, Oesterhelt, Fernandez, Gaub (bb0340) 1997; 276
Joo, Balci, Ishitsuka, Buranachai, Ha (bb0150) 2008; 77
Axelrod (bb0170) 2013; 104
Liu, Lavis, Betzig (bb0420) 2015; 58
Balzarotti, Eilers, Gwosch, Gynna, Westphal, Stefani, Elf, Hell (bb0535) 2017; 355
Berg (bb0075) 2003; 72
Hinner, Johnsson (bb0430) 2010; 21
Astumian (bb0265) 1997; 276
Sweeney, Houdusse (bb0225) 2010; 39
Uchihashi, Iino, Ando, Noji (bb0240) 2011; 333
Hayashi, Ueno, Iino, Noji (bb0220) 2010; 104
Minagawa, Ueno, Hara, Ishizuka-Katsura, Ohsawa, Terada, Shirouzu, Yokoyama, Yamato, Muneyuki, Noji, Murata, Iino (bb0110) 2013; 288
Watanabe, Okuno, Sakakihara, Shimabukuro, Iino, Yoshida, Noji (bb0295) 2011; 8
Harada, Ohara, Takatsuki, Itoh, Shimamoto, Kinosita (bb0070) 2001; 409
Hibino, Hiroshima, Takahashi, Sako (bb0410) 2009; 544
Steven, Baumeister, Johnson, Perham (bb0005) 2016
Marsden, Nardelli, Linder, McCarthy (bb0385) 2006; 361
Neuman, Nagy (bb0345) 2008; 5
Itoh, Takahashi, Adachi, Noji, Yasuda, Yoshida, Kinosita (bb0275) 2004; 427
Adachi, Oiwa, Yoshida, Nishizaka, Kinosita (bb0300) 2012; 3
Adachi, Oiwa, Nishizaka, Furuike, Noji, Itoh, Yoshida, Kinosita (bb0315) 2007; 130
Bhabha, Johnson, Schroeder, Vale (bb0065) 2016; 41
Kollmannsperger, Sharei, Raulf, Heilemann, Langer, Jensen, Wieneke, Tampe (bb0435) 2016; 7
Betzig, Patterson, Sougrat, Lindwasser, Olenych, Bonifacino, Davidson, Lippincott-Schwartz, Hess (bb0525) 2006; 313
Vazquez, Matsuoka, Sellers, Yanagida, Ueda, Devreotes (bb0475) 2006; 103
Enoki, Iino, Niitani, Minagawa, Tomishige, Noji (bb0210) 2015; 87
Rust, Bates, Zhuang (bb0530) 2006; 3
Watanabe, Tabata, Iino, Ueno, Iwamoto, Oiki, Noji (bb0260) 2013; 4
Gebhardt, Clemen, Jaud, Rief (bb0290) 2006; 103
You, Zeng, Xu, Lim, Efremov, Phan, Yan (bb0395) 2014; 42
Greenleaf, Woodside, Block (bb0155) 2007; 36
Sowa, Berry (bb0080) 2008; 41
Minagawa (10.1016/j.bbagen.2017.08.008_bb0110) 2013; 288
Sowa (10.1016/j.bbagen.2017.08.008_bb0255) 2005; 437
Igarashi (10.1016/j.bbagen.2017.08.008_bb0140) 2014; 5
Watanabe (10.1016/j.bbagen.2017.08.008_bb0295) 2011; 8
Carter (10.1016/j.bbagen.2017.08.008_bb0285) 2005; 435
Watanabe (10.1016/j.bbagen.2017.08.008_bb0260) 2013; 4
Iino (10.1016/j.bbagen.2017.08.008_bb0095) 2013; 65
Steven (10.1016/j.bbagen.2017.08.008_bb0005) 2016
Hell (10.1016/j.bbagen.2017.08.008_bb0520) 1994; 19
Jarmoskaite (10.1016/j.bbagen.2017.08.008_bb0350) 2014; 83
Imamura (10.1016/j.bbagen.2017.08.008_bb0100) 2003; 100
Adachi (10.1016/j.bbagen.2017.08.008_bb0315) 2007; 130
Iino (10.1016/j.bbagen.2017.08.008_bb0115) 2015; 31
Rust (10.1016/j.bbagen.2017.08.008_bb0530) 2006; 3
Hibino (10.1016/j.bbagen.2017.08.008_bb0485) 2011; 286
Woodside (10.1016/j.bbagen.2017.08.008_bb0380) 2014; 43
Arata (10.1016/j.bbagen.2017.08.008_bb0460) 2016; 16
Gao (10.1016/j.bbagen.2017.08.008_bb0425) 2017; 42
Sowa (10.1016/j.bbagen.2017.08.008_bb0080) 2008; 41
Isojima (10.1016/j.bbagen.2017.08.008_bb0215) 2016; 12
Liu (10.1016/j.bbagen.2017.08.008_bb0420) 2015; 58
Sako (10.1016/j.bbagen.2017.08.008_bb0405) 2003
Sako (10.1016/j.bbagen.2017.08.008_bb0490) 2000; 2
Andrecka (10.1016/j.bbagen.2017.08.008_bb0510) 2015; 4
Bhabha (10.1016/j.bbagen.2017.08.008_bb0065) 2016; 41
Sweeney (10.1016/j.bbagen.2017.08.008_bb0225) 2010; 39
Saita (10.1016/j.bbagen.2017.08.008_bb0320) 2015; 112
Saxton (10.1016/j.bbagen.2017.08.008_bb0185) 1997; 26
Wen (10.1016/j.bbagen.2017.08.008_bb0030) 2008; 452
Berg (10.1016/j.bbagen.2017.08.008_bb0075) 2003; 72
Adachi (10.1016/j.bbagen.2017.08.008_bb0300) 2012; 3
Betzig (10.1016/j.bbagen.2017.08.008_bb0525) 2006; 313
Levi (10.1016/j.bbagen.2017.08.008_bb0445) 2007; 48
Ulbrich (10.1016/j.bbagen.2017.08.008_bb0500) 2007; 4
Greenleaf (10.1016/j.bbagen.2017.08.008_bb0155) 2007; 36
Uchihashi (10.1016/j.bbagen.2017.08.008_bb0240) 2011; 333
Nakamura (10.1016/j.bbagen.2017.08.008_bb0480) 2016; 13
Iwane (10.1016/j.bbagen.2017.08.008_bb0160) 1997; 407
Tran (10.1016/j.bbagen.2017.08.008_bb0400) 2004; 13
Hayashi (10.1016/j.bbagen.2017.08.008_bb0220) 2010; 104
Igarashi (10.1016/j.bbagen.2017.08.008_bb0125) 2011; 333
Smith (10.1016/j.bbagen.2017.08.008_bb0335) 1996; 271
Finer (10.1016/j.bbagen.2017.08.008_bb0040) 1994; 368
Yodh (10.1016/j.bbagen.2017.08.008_bb0375) 2010; 43
Chen (10.1016/j.bbagen.2017.08.008_bb0330) 2011; 100
Vazquez (10.1016/j.bbagen.2017.08.008_bb0475) 2006; 103
Fukuda (10.1016/j.bbagen.2017.08.008_bb0135) 2013; 84
Sako (10.1016/j.bbagen.2017.08.008_bb0415) 2006; 2
Hibino (10.1016/j.bbagen.2017.08.008_bb0410) 2009; 544
Paschal (10.1016/j.bbagen.2017.08.008_bb0060) 1987; 330
You (10.1016/j.bbagen.2017.08.008_bb0390) 2017; 45
Watanabe (10.1016/j.bbagen.2017.08.008_bb0305) 2010; 6
You (10.1016/j.bbagen.2017.08.008_bb0395) 2014; 42
Abbondanzieri (10.1016/j.bbagen.2017.08.008_bb0025) 2005; 438
Rodriguez (10.1016/j.bbagen.2017.08.008_bb0165) 2017; 42
Teng (10.1016/j.bbagen.2017.08.008_bb0440) 2016; 5
Larson (10.1016/j.bbagen.2017.08.008_bb0010) 2011; 41
Yanagida (10.1016/j.bbagen.2017.08.008_bb0015) 2017; 93
Iino (10.1016/j.bbagen.2017.08.008_bb0495) 2001; 80
Gosse (10.1016/j.bbagen.2017.08.008_bb0325) 2002; 82
Lin (10.1016/j.bbagen.2017.08.008_bb0515) 2014; 22
Cotter (10.1016/j.bbagen.2017.08.008_bb0105) 2015; 40
Joo (10.1016/j.bbagen.2017.08.008_bb0150) 2008; 77
Svoboda (10.1016/j.bbagen.2017.08.008_bb0055) 1993; 365
Nakamura (10.1016/j.bbagen.2017.08.008_bb0130) 2016; 291
Bustamante (10.1016/j.bbagen.2017.08.008_bb0145) 2004; 73
Ueno (10.1016/j.bbagen.2017.08.008_bb0205) 2010; 98
Enoki (10.1016/j.bbagen.2017.08.008_bb0210) 2015; 87
Johnson (10.1016/j.bbagen.2017.08.008_bb0365) 2007; 129
Ritter (10.1016/j.bbagen.2017.08.008_bb0540) 2010; 5
Efros (10.1016/j.bbagen.2017.08.008_bb0200) 2016; 11
Alivisatos (10.1016/j.bbagen.2017.08.008_bb0195) 2004; 22
Nakada (10.1016/j.bbagen.2017.08.008_bb0455) 2003; 5
Itoh (10.1016/j.bbagen.2017.08.008_bb0275) 2004; 427
Boehr (10.1016/j.bbagen.2017.08.008_bb0270) 2009; 5
Houdusse (10.1016/j.bbagen.2017.08.008_bb0230) 2016; 41
Astumian (10.1016/j.bbagen.2017.08.008_bb0265) 1997; 276
Roy (10.1016/j.bbagen.2017.08.008_bb0190) 2008; 5
Neuman (10.1016/j.bbagen.2017.08.008_bb0345) 2008; 5
Noji (10.1016/j.bbagen.2017.08.008_bb0090) 1997; 386
Ueno (10.1016/j.bbagen.2017.08.008_bb0120) 2014; 289
Balzarotti (10.1016/j.bbagen.2017.08.008_bb0535) 2017; 355
Boyer (10.1016/j.bbagen.2017.08.008_bb0085) 1997; 66
Kodera (10.1016/j.bbagen.2017.08.008_bb0250) 2010; 468
Harada (10.1016/j.bbagen.2017.08.008_bb0070) 2001; 409
Shiroguchi (10.1016/j.bbagen.2017.08.008_bb0245) 2007; 316
Yasuda (10.1016/j.bbagen.2017.08.008_bb0310) 2001; 410
Watanabe (10.1016/j.bbagen.2017.08.008_bb0465) 2002; 295
Toprak (10.1016/j.bbagen.2017.08.008_bb0180) 2007; 36
Pyle (10.1016/j.bbagen.2017.08.008_bb0355) 2008; 37
Kollmannsperger (10.1016/j.bbagen.2017.08.008_bb0435) 2016; 7
Bustamante (10.1016/j.bbagen.2017.08.008_bb0035) 2011; 144
Dessinges (10.1016/j.bbagen.2017.08.008_bb0360) 2004; 101
Ueda (10.1016/j.bbagen.2017.08.008_bb0020) 2001; 294
Yildiz (10.1016/j.bbagen.2017.08.008_bb0175) 2003; 300
Howard (10.1016/j.bbagen.2017.08.008_bb0050) 1989; 342
Axelrod (10.1016/j.bbagen.2017.08.008_bb0170) 2013; 104
Ortega Arroyo (10.1016/j.bbagen.2017.08.008_bb0505) 2014; 14
Kubitscheck (10.1016/j.bbagen.2017.08.008_bb0470) 2005; 168
Hodeib (10.1016/j.bbagen.2017.08.008_bb0370) 2016; 105
Abrahams (10.1016/j.bbagen.2017.08.008_bb0235) 1994; 370
Shibata (10.1016/j.bbagen.2017.08.008_bb0450) 2006; 342
Rief (10.1016/j.bbagen.2017.08.008_bb0340) 1997; 276
Hinner (10.1016/j.bbagen.2017.08.008_bb0430) 2010; 21
Gebhardt (10.1016/j.bbagen.2017.08.008_bb0290) 2006; 103
Karagiannis (10.1016/j.bbagen.2017.08.008_bb0045) 2014; 114
Rondelez (10.1016/j.bbagen.2017.08.008_bb0280) 2005; 433
Marsden (10.1016/j.bbagen.2017.08.008_bb0385) 2006; 361
References_xml – volume: 289
  start-page: 31212
  year: 2014
  end-page: 31223
  ident: bb0120
  article-title: Torque generation of
  publication-title: J. Biol. Chem.
– volume: 286
  start-page: 36460
  year: 2011
  end-page: 36468
  ident: bb0485
  article-title: Activation kinetics of RAF protein in the ternary complex of RAF, RAS-GTP, and kinase on the plasma membrane of living cells: single-molecule imaging analysis
  publication-title: J. Biol. Chem.
– volume: 65
  start-page: 238
  year: 2013
  end-page: 246
  ident: bb0095
  article-title: Operation mechanism of F(o) F(1)-adenosine triphosphate synthase revealed by its structure and dynamics
  publication-title: IUBMB Life
– volume: 144
  start-page: 480
  year: 2011
  end-page: 497
  ident: bb0035
  article-title: Revisiting the central dogma one molecule at a time
  publication-title: Cell
– volume: 368
  start-page: 113
  year: 1994
  end-page: 119
  ident: bb0040
  article-title: Single myosin molecule mechanics: piconewton forces and nanometre steps
  publication-title: Nature
– volume: 22
  start-page: 47
  year: 2004
  end-page: 52
  ident: bb0195
  article-title: The use of nanocrystals in biological detection
  publication-title: Nat. Biotechnol.
– volume: 37
  start-page: 317
  year: 2008
  end-page: 336
  ident: bb0355
  article-title: Translocation and unwinding mechanisms of RNA and DNA helicases
  publication-title: Annu. Rev. Biophys.
– volume: 5
  year: 2010
  ident: bb0540
  article-title: Light sheet microscopy for single molecule tracking in living tissue
  publication-title: PLoS One
– volume: 100
  start-page: 517
  year: 2011
  end-page: 523
  ident: bb0330
  article-title: Improved high-force magnetic tweezers for stretching and refolding of proteins and short DNA
  publication-title: Biophys. J.
– volume: 316
  start-page: 1208
  year: 2007
  end-page: 1212
  ident: bb0245
  article-title: Myosin V walks by lever action and Brownian motion
  publication-title: Science
– volume: 41
  start-page: 249
  year: 2011
  end-page: 262
  ident: bb0010
  article-title: Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes
  publication-title: Mol. Cell
– volume: 104
  start-page: 1401
  year: 2013
  end-page: 1409
  ident: bb0170
  article-title: Evanescent excitation and emission in fluorescence microscopy
  publication-title: Biophys. J.
– volume: 114
  start-page: 3318
  year: 2014
  end-page: 3334
  ident: bb0045
  article-title: Molecular machines like myosin use randomness to behave predictably
  publication-title: Chem. Rev.
– volume: 58
  start-page: 644
  year: 2015
  end-page: 659
  ident: bb0420
  article-title: Imaging live-cell dynamics and structure at the single-molecule level
  publication-title: Mol. Cell
– volume: 14
  start-page: 2065
  year: 2014
  end-page: 2070
  ident: bb0505
  article-title: Label-free, all-optical detection, imaging, and tracking of a single protein
  publication-title: Nano Lett.
– volume: 544
  start-page: 451
  year: 2009
  end-page: 460
  ident: bb0410
  article-title: Single-molecule imaging of fluorescent proteins expressed in living cells
  publication-title: Methods Mol. Biol.
– volume: 21
  start-page: 766
  year: 2010
  end-page: 776
  ident: bb0430
  article-title: How to obtain labeled proteins and what to do with them
  publication-title: Curr. Opin. Biotechnol.
– volume: 19
  start-page: 780
  year: 1994
  end-page: 782
  ident: bb0520
  article-title: Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
  publication-title: Opt. Lett.
– volume: 433
  start-page: 773
  year: 2005
  end-page: 777
  ident: bb0280
  article-title: Highly coupled ATP synthesis by F1-ATPase single molecules
  publication-title: Nature
– volume: 3
  start-page: 1022
  year: 2012
  ident: bb0300
  article-title: Controlled rotation of the F(1)-ATPase reveals differential and continuous binding changes for ATP synthesis
  publication-title: Nat. Commun.
– volume: 409
  start-page: 113
  year: 2001
  end-page: 115
  ident: bb0070
  article-title: Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase
  publication-title: Nature
– volume: 288
  start-page: 32700
  year: 2013
  end-page: 32707
  ident: bb0110
  article-title: Basic properties of rotary dynamics of the molecular motor
  publication-title: J. Biol. Chem.
– volume: 45
  start-page: 206
  year: 2017
  end-page: 214
  ident: bb0390
  article-title: RHAU helicase stabilizes G4 in its nucleotide-free state and destabilizes G4 upon ATP hydrolysis
  publication-title: Nucleic Acids Res.
– volume: 77
  start-page: 51
  year: 2008
  end-page: 76
  ident: bb0150
  article-title: Advances in single-molecule fluorescence methods for molecular biology
  publication-title: Annu. Rev. Biochem.
– volume: 365
  start-page: 721
  year: 1993
  end-page: 727
  ident: bb0055
  article-title: Direct observation of kinesin stepping by optical trapping interferometry
  publication-title: Nature
– volume: 276
  start-page: 1109
  year: 1997
  end-page: 1112
  ident: bb0340
  article-title: Reversible unfolding of individual titin immunoglobulin domains by AFM
  publication-title: Science
– volume: 43
  start-page: 185
  year: 2010
  end-page: 217
  ident: bb0375
  article-title: Insight into helicase mechanism and function revealed through single-molecule approaches
  publication-title: Q. Rev. Biophys.
– volume: 103
  start-page: 8680
  year: 2006
  end-page: 8685
  ident: bb0290
  article-title: Myosin-V is a mechanical ratchet
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 333
  start-page: 1279
  year: 2011
  end-page: 1282
  ident: bb0125
  article-title: Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface
  publication-title: Science
– volume: 72
  start-page: 19
  year: 2003
  end-page: 54
  ident: bb0075
  article-title: The rotary motor of bacterial flagella
  publication-title: Annu. Rev. Biochem.
– start-page: SS1
  year: 2003
  end-page: 5
  ident: bb0405
  article-title: Single-molecule visualization in cell biology
  publication-title: Nat. Rev. Mol. Cell Biol.
– volume: 427
  start-page: 465
  year: 2004
  end-page: 468
  ident: bb0275
  article-title: Mechanically driven ATP synthesis by F1-ATPase
  publication-title: Nature
– volume: 4
  year: 2015
  ident: bb0510
  article-title: Structural dynamics of myosin 5 during processive motion revealed by interferometric scattering microscopy
  publication-title: elife
– volume: 5
  start-page: 491
  year: 2008
  end-page: 505
  ident: bb0345
  article-title: Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
  publication-title: Nat. Methods
– volume: 291
  start-page: 22404
  year: 2016
  end-page: 22413
  ident: bb0130
  article-title: Single-molecule imaging analysis of binding, processive movement, and dissociation of cellobiohydrolase
  publication-title: J. Biol. Chem.
– volume: 36
  start-page: 171
  year: 2007
  end-page: 190
  ident: bb0155
  article-title: High-resolution, single-molecule measurements of biomolecular motion
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
– volume: 330
  start-page: 672
  year: 1987
  end-page: 674
  ident: bb0060
  article-title: Isolated flagellar outer arm dynein translocates brain microtubules in vitro
  publication-title: Nature
– volume: 42
  start-page: 8789
  year: 2014
  end-page: 8795
  ident: bb0395
  article-title: Dynamics and stability of polymorphic human telomeric G-quadruplex under tension
  publication-title: Nucleic Acids Res.
– volume: 5
  start-page: 3975
  year: 2014
  ident: bb0140
  article-title: Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin
  publication-title: Nat. Commun.
– volume: 101
  start-page: 6439
  year: 2004
  end-page: 6444
  ident: bb0360
  article-title: Single-molecule assay reveals strand switching and enhanced processivity of UvrD
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 103
  start-page: 3633
  year: 2006
  end-page: 3638
  ident: bb0475
  article-title: Tumor suppressor PTEN acts through dynamic interaction with the plasma membrane
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 31
  start-page: 49
  year: 2015
  end-page: 56
  ident: bb0115
  article-title: Rotational mechanism of
  publication-title: Curr. Opin. Struct. Biol.
– volume: 93
  start-page: 51
  year: 2017
  end-page: 63
  ident: bb0015
  article-title: Single molecule detection, thermal fluctuation and life
  publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
– volume: 22
  start-page: 9159
  year: 2014
  end-page: 9170
  ident: bb0515
  article-title: Shot-noise limited localization of single 20
  publication-title: Opt. Express
– volume: 87
  start-page: 2079
  year: 2015
  end-page: 2086
  ident: bb0210
  article-title: High-speed angle-resolved imaging of a single gold nanorod with microsecond temporal resolution and one-degree angle precision
  publication-title: Anal. Chem.
– volume: 3
  start-page: 793
  year: 2006
  end-page: 795
  ident: bb0530
  article-title: Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
  publication-title: Nat. Methods
– volume: 468
  start-page: 72
  year: 2010
  end-page: 76
  ident: bb0250
  article-title: Video imaging of walking myosin V by high-speed atomic force microscopy
  publication-title: Nature
– volume: 36
  start-page: 349
  year: 2007
  end-page: 369
  ident: bb0180
  article-title: New fluorescent tools for watching nanometer-scale conformational changes of single molecules
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
– volume: 43
  start-page: 19
  year: 2014
  end-page: 39
  ident: bb0380
  article-title: Reconstructing folding energy landscapes by single-molecule force spectroscopy
  publication-title: Annu. Rev. Biophys.
– volume: 98
  start-page: 2014
  year: 2010
  end-page: 2023
  ident: bb0205
  article-title: Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution
  publication-title: Biophys. J.
– volume: 2
  start-page: 56
  year: 2006
  ident: bb0415
  article-title: Imaging single molecules in living cells for systems biology
  publication-title: Mol. Syst. Biol.
– volume: 5
  start-page: 507
  year: 2008
  end-page: 516
  ident: bb0190
  article-title: A practical guide to single-molecule FRET
  publication-title: Nat. Methods
– volume: 438
  start-page: 460
  year: 2005
  end-page: 465
  ident: bb0025
  article-title: Direct observation of base-pair stepping by RNA polymerase
  publication-title: Nature
– volume: 342
  start-page: 154
  year: 1989
  end-page: 158
  ident: bb0050
  article-title: Movement of microtubules by single kinesin molecules
  publication-title: Nature
– volume: 83
  start-page: 697
  year: 2014
  end-page: 725
  ident: bb0350
  article-title: RNA helicase proteins as chaperones and remodelers
  publication-title: Annu. Rev. Biochem.
– volume: 5
  start-page: 626
  year: 2003
  end-page: 632
  ident: bb0455
  article-title: Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization
  publication-title: Nat. Cell Biol.
– year: 2016
  ident: bb0005
  article-title: Molecular Biology of Assemblies and Machines
– volume: 42
  start-page: 111
  year: 2017
  end-page: 129
  ident: bb0165
  article-title: The growing and glowing toolbox of fluorescent and photoactive proteins
  publication-title: Trends Biochem. Sci.
– volume: 5
  year: 2016
  ident: bb0440
  article-title: Labeling proteins inside living cells using external fluorophores for microscopy
  publication-title: elife
– volume: 13
  start-page: 101
  year: 2004
  end-page: 111
  ident: bb0400
  article-title: Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU
  publication-title: Mol. Cell
– volume: 8
  start-page: 86
  year: 2011
  end-page: 92
  ident: bb0295
  article-title: Mechanical modulation of catalytic power on F1-ATPase
  publication-title: Nat. Chem. Biol.
– volume: 105
  start-page: 3
  year: 2016
  end-page: 15
  ident: bb0370
  article-title: Single molecule studies of helicases with magnetic tweezers
  publication-title: Methods
– volume: 39
  start-page: 539
  year: 2010
  end-page: 557
  ident: bb0225
  article-title: Structural and functional insights into the myosin motor mechanism
  publication-title: Annu. Rev. Biophys.
– volume: 41
  start-page: 103
  year: 2008
  end-page: 132
  ident: bb0080
  article-title: Bacterial flagellar motor
  publication-title: Q. Rev. Biophys.
– volume: 2
  start-page: 168
  year: 2000
  end-page: 172
  ident: bb0490
  article-title: Single-molecule imaging of EGFR signalling on the surface of living cells
  publication-title: Nat. Cell Biol.
– volume: 130
  start-page: 309
  year: 2007
  end-page: 321
  ident: bb0315
  article-title: Coupling of rotation and catalysis in F-1-ATPase revealed by single-molecule imaging and manipulation
  publication-title: Cell
– volume: 5
  start-page: 789
  year: 2009
  end-page: 796
  ident: bb0270
  article-title: The role of dynamic conformational ensembles in biomolecular recognition
  publication-title: Nat. Chem. Biol.
– volume: 48
  start-page: 1
  year: 2007
  end-page: 15
  ident: bb0445
  article-title: Exploring dynamics in living cells by tracking single particles
  publication-title: Cell Biochem. Biophys.
– volume: 271
  start-page: 795
  year: 1996
  end-page: 799
  ident: bb0335
  article-title: Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules
  publication-title: Science
– volume: 129
  start-page: 1299
  year: 2007
  end-page: 1309
  ident: bb0365
  article-title: Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase
  publication-title: Cell
– volume: 16
  start-page: 2156
  year: 2016
  end-page: 2168
  ident: bb0460
  article-title: Cortical polarity of the RING protein PAR-2 is maintained by exchange rate kinetics at the cortical-cytoplasmic boundary
  publication-title: Cell Rep.
– volume: 104
  start-page: 218103
  year: 2010
  ident: bb0220
  article-title: Fluctuation theorem applied to F1-ATPase
  publication-title: Phys. Rev. Lett.
– volume: 452
  start-page: 598
  year: 2008
  end-page: 603
  ident: bb0030
  article-title: Following translation by single ribosomes one codon at a time
  publication-title: Nature
– volume: 437
  start-page: 916
  year: 2005
  end-page: 919
  ident: bb0255
  article-title: Direct observation of steps in rotation of the bacterial flagellar motor
  publication-title: Nature
– volume: 407
  start-page: 235
  year: 1997
  end-page: 238
  ident: bb0160
  article-title: Single molecular assay of individual ATP turnover by a myosin-GFP fusion protein expressed in vitro
  publication-title: FEBS Lett.
– volume: 295
  start-page: 1083
  year: 2002
  end-page: 1086
  ident: bb0465
  article-title: Single-molecule speckle analysis of actin filament turnover in lamellipodia
  publication-title: Science
– volume: 40
  start-page: 611
  year: 2015
  end-page: 622
  ident: bb0105
  article-title: Recent insights into the structure, regulation, and function of the V-ATPases
  publication-title: Trends Biochem. Sci.
– volume: 41
  start-page: 94
  year: 2016
  end-page: 105
  ident: bb0065
  article-title: How dynein moves along microtubules
  publication-title: Trends Biochem. Sci.
– volume: 294
  start-page: 864
  year: 2001
  end-page: 867
  ident: bb0020
  article-title: Single-molecule analysis of chemotactic signaling in
  publication-title: Science
– volume: 7
  start-page: 10372
  year: 2016
  ident: bb0435
  article-title: Live-cell protein labelling with nanometre precision by cell squeezing
  publication-title: Nat. Commun.
– volume: 80
  start-page: 2667
  year: 2001
  end-page: 2677
  ident: bb0495
  article-title: Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
  publication-title: Biophys. J.
– volume: 333
  start-page: 755
  year: 2011
  end-page: 758
  ident: bb0240
  article-title: High-speed atomic force microscopy reveals rotary catalysis of rotorless F(1)-ATPase
  publication-title: Science
– volume: 276
  start-page: 917
  year: 1997
  end-page: 922
  ident: bb0265
  article-title: Thermodynamics and kinetics of a Brownian motor
  publication-title: Science
– volume: 11
  start-page: 661
  year: 2016
  end-page: 671
  ident: bb0200
  article-title: Origin and control of blinking in quantum dots
  publication-title: Nat. Nanotechnol.
– volume: 13
  start-page: 1
  year: 2016
  end-page: 11
  ident: bb0480
  article-title: Switching of the positive feedback for RAS activation by a concerted function of SOS membrane association domains
  publication-title: Biophys Physicobiol.
– volume: 73
  start-page: 705
  year: 2004
  end-page: 748
  ident: bb0145
  article-title: Mechanical processes in biochemistry
  publication-title: Annu. Rev. Biochem.
– volume: 300
  start-page: 2061
  year: 2003
  end-page: 2065
  ident: bb0175
  article-title: Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization
  publication-title: Science
– volume: 41
  start-page: 989
  year: 2016
  end-page: 997
  ident: bb0230
  article-title: How myosin generates force on actin filaments
  publication-title: Trends Biochem. Sci.
– volume: 313
  start-page: 1642
  year: 2006
  end-page: 1645
  ident: bb0525
  article-title: Imaging intracellular fluorescent proteins at nanometer resolution
  publication-title: Science
– volume: 84
  year: 2013
  ident: bb0135
  article-title: High-speed atomic force microscope combined with single-molecule fluorescence microscope
  publication-title: Rev. Sci. Instrum.
– volume: 112
  start-page: 9626
  year: 2015
  end-page: 9631
  ident: bb0320
  article-title: Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 4
  start-page: 319
  year: 2007
  end-page: 321
  ident: bb0500
  article-title: Subunit counting in membrane-bound proteins
  publication-title: Nat. Methods
– volume: 342
  start-page: 316
  year: 2006
  end-page: 322
  ident: bb0450
  article-title: Formation of signal transduction complexes during immobile phase of NGFR movements
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 370
  start-page: 621
  year: 1994
  end-page: 628
  ident: bb0235
  article-title: Structure at 2.8
  publication-title: Nature
– volume: 168
  start-page: 233
  year: 2005
  end-page: 243
  ident: bb0470
  article-title: Nuclear transport of single molecules: dwell times at the nuclear pore complex
  publication-title: J. Cell Biol.
– volume: 12
  start-page: 290
  year: 2016
  end-page: 297
  ident: bb0215
  article-title: Direct observation of intermediate states during the stepping motion of kinesin-1
  publication-title: Nat. Chem. Biol.
– volume: 6
  start-page: 814
  year: 2010
  end-page: 820
  ident: bb0305
  article-title: Phosphate release in F1-ATPase catalytic cycle follows ADP release
  publication-title: Nat. Chem. Biol.
– volume: 386
  start-page: 299
  year: 1997
  end-page: 302
  ident: bb0090
  article-title: Direct observation of the rotation of F1-ATPase
  publication-title: Nature
– volume: 82
  start-page: 3314
  year: 2002
  end-page: 3329
  ident: bb0325
  article-title: Magnetic tweezers: micromanipulation and force measurement at the molecular level
  publication-title: Biophys. J.
– volume: 355
  start-page: 606
  year: 2017
  end-page: 612
  ident: bb0535
  article-title: Nanometer resolution imaging and tracking of fluorescent molecules with minimal photon fluxes
  publication-title: Science
– volume: 66
  start-page: 717
  year: 1997
  end-page: 749
  ident: bb0085
  article-title: The ATP synthase—a splendid molecular machine
  publication-title: Annu. Rev. Biochem.
– volume: 26
  start-page: 373
  year: 1997
  end-page: 399
  ident: bb0185
  article-title: Single-particle tracking: applications to membrane dynamics
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
– volume: 100
  start-page: 2312
  year: 2003
  end-page: 2315
  ident: bb0100
  article-title: Evidence for rotation of V1-ATPase
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 410
  start-page: 898
  year: 2001
  end-page: 904
  ident: bb0310
  article-title: Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
  publication-title: Nature
– volume: 361
  start-page: 327
  year: 2006
  end-page: 335
  ident: bb0385
  article-title: Unwinding single RNA molecules using helicases involved in eukaryotic translation initiation
  publication-title: J. Mol. Biol.
– volume: 42
  start-page: 831
  year: 2017
  end-page: 834
  ident: bb0425
  article-title: Precise background subtraction in stimulated emission double depletion nanoscopy
  publication-title: Opt. Lett.
– volume: 435
  start-page: 308
  year: 2005
  end-page: 312
  ident: bb0285
  article-title: Mechanics of the kinesin step
  publication-title: Nature
– volume: 4
  start-page: 1631
  year: 2013
  ident: bb0260
  article-title: Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force
  publication-title: Nat. Commun.
– volume: 16
  start-page: 2156
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0460
  article-title: Cortical polarity of the RING protein PAR-2 is maintained by exchange rate kinetics at the cortical-cytoplasmic boundary
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2016.07.047
– volume: 342
  start-page: 316
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0450
  article-title: Formation of signal transduction complexes during immobile phase of NGFR movements
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2006.01.126
– volume: 437
  start-page: 916
  year: 2005
  ident: 10.1016/j.bbagen.2017.08.008_bb0255
  article-title: Direct observation of steps in rotation of the bacterial flagellar motor
  publication-title: Nature
  doi: 10.1038/nature04003
– volume: 104
  start-page: 1401
  year: 2013
  ident: 10.1016/j.bbagen.2017.08.008_bb0170
  article-title: Evanescent excitation and emission in fluorescence microscopy
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2013.02.044
– volume: 41
  start-page: 989
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0230
  article-title: How myosin generates force on actin filaments
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2016.09.006
– volume: 370
  start-page: 621
  year: 1994
  ident: 10.1016/j.bbagen.2017.08.008_bb0235
  article-title: Structure at 2.8A resolution of F1-ATPase from bovine heart mitochondria
  publication-title: Nature
  doi: 10.1038/370621a0
– volume: 435
  start-page: 308
  year: 2005
  ident: 10.1016/j.bbagen.2017.08.008_bb0285
  article-title: Mechanics of the kinesin step
  publication-title: Nature
  doi: 10.1038/nature03528
– volume: 333
  start-page: 755
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0240
  article-title: High-speed atomic force microscopy reveals rotary catalysis of rotorless F(1)-ATPase
  publication-title: Science
  doi: 10.1126/science.1205510
– volume: 66
  start-page: 717
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0085
  article-title: The ATP synthase—a splendid molecular machine
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.66.1.717
– volume: 98
  start-page: 2014
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0205
  article-title: Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2010.01.011
– volume: 365
  start-page: 721
  year: 1993
  ident: 10.1016/j.bbagen.2017.08.008_bb0055
  article-title: Direct observation of kinesin stepping by optical trapping interferometry
  publication-title: Nature
  doi: 10.1038/365721a0
– volume: 433
  start-page: 773
  year: 2005
  ident: 10.1016/j.bbagen.2017.08.008_bb0280
  article-title: Highly coupled ATP synthesis by F1-ATPase single molecules
  publication-title: Nature
  doi: 10.1038/nature03277
– volume: 291
  start-page: 22404
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0130
  article-title: Single-molecule imaging analysis of binding, processive movement, and dissociation of cellobiohydrolase Trichoderma reesei Cel6A and its domains on crystalline cellulose
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M116.752048
– volume: 13
  start-page: 1
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0480
  article-title: Switching of the positive feedback for RAS activation by a concerted function of SOS membrane association domains
  publication-title: Biophys Physicobiol.
  doi: 10.2142/biophysico.13.0_1
– volume: 65
  start-page: 238
  year: 2013
  ident: 10.1016/j.bbagen.2017.08.008_bb0095
  article-title: Operation mechanism of F(o) F(1)-adenosine triphosphate synthase revealed by its structure and dynamics
  publication-title: IUBMB Life
  doi: 10.1002/iub.1120
– volume: 410
  start-page: 898
  year: 2001
  ident: 10.1016/j.bbagen.2017.08.008_bb0310
  article-title: Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
  publication-title: Nature
  doi: 10.1038/35073513
– volume: 84
  year: 2013
  ident: 10.1016/j.bbagen.2017.08.008_bb0135
  article-title: High-speed atomic force microscope combined with single-molecule fluorescence microscope
  publication-title: Rev. Sci. Instrum.
  doi: 10.1063/1.4813280
– volume: 288
  start-page: 32700
  year: 2013
  ident: 10.1016/j.bbagen.2017.08.008_bb0110
  article-title: Basic properties of rotary dynamics of the molecular motor Enterococcus hirae V1-ATPase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.506329
– volume: 2
  start-page: 56
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0415
  article-title: Imaging single molecules in living cells for systems biology
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb4100100
– volume: 342
  start-page: 154
  year: 1989
  ident: 10.1016/j.bbagen.2017.08.008_bb0050
  article-title: Movement of microtubules by single kinesin molecules
  publication-title: Nature
  doi: 10.1038/342154a0
– volume: 112
  start-page: 9626
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0320
  article-title: Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1422885112
– volume: 271
  start-page: 795
  year: 1996
  ident: 10.1016/j.bbagen.2017.08.008_bb0335
  article-title: Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules
  publication-title: Science
  doi: 10.1126/science.271.5250.795
– volume: 4
  start-page: 319
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0500
  article-title: Subunit counting in membrane-bound proteins
  publication-title: Nat. Methods
  doi: 10.1038/nmeth1024
– volume: 19
  start-page: 780
  year: 1994
  ident: 10.1016/j.bbagen.2017.08.008_bb0520
  article-title: Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
  publication-title: Opt. Lett.
  doi: 10.1364/OL.19.000780
– volume: 104
  start-page: 218103
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0220
  article-title: Fluctuation theorem applied to F1-ATPase
  publication-title: Phys. Rev. Lett.
  doi: 10.1103/PhysRevLett.104.218103
– volume: 100
  start-page: 517
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0330
  article-title: Improved high-force magnetic tweezers for stretching and refolding of proteins and short DNA
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2010.12.3700
– volume: 14
  start-page: 2065
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0505
  article-title: Label-free, all-optical detection, imaging, and tracking of a single protein
  publication-title: Nano Lett.
  doi: 10.1021/nl500234t
– volume: 45
  start-page: 206
  year: 2017
  ident: 10.1016/j.bbagen.2017.08.008_bb0390
  article-title: RHAU helicase stabilizes G4 in its nucleotide-free state and destabilizes G4 upon ATP hydrolysis
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw881
– volume: 103
  start-page: 3633
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0475
  article-title: Tumor suppressor PTEN acts through dynamic interaction with the plasma membrane
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0510570103
– volume: 80
  start-page: 2667
  year: 2001
  ident: 10.1016/j.bbagen.2017.08.008_bb0495
  article-title: Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(01)76236-4
– volume: 452
  start-page: 598
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0030
  article-title: Following translation by single ribosomes one codon at a time
  publication-title: Nature
  doi: 10.1038/nature06716
– volume: 77
  start-page: 51
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0150
  article-title: Advances in single-molecule fluorescence methods for molecular biology
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.77.070606.101543
– volume: 333
  start-page: 1279
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0125
  article-title: Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface
  publication-title: Science
  doi: 10.1126/science.1208386
– volume: 286
  start-page: 36460
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0485
  article-title: Activation kinetics of RAF protein in the ternary complex of RAF, RAS-GTP, and kinase on the plasma membrane of living cells: single-molecule imaging analysis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.262675
– volume: 407
  start-page: 235
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0160
  article-title: Single molecular assay of individual ATP turnover by a myosin-GFP fusion protein expressed in vitro
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(97)00359-1
– volume: 83
  start-page: 697
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0350
  article-title: RNA helicase proteins as chaperones and remodelers
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-060713-035546
– volume: 300
  start-page: 2061
  year: 2003
  ident: 10.1016/j.bbagen.2017.08.008_bb0175
  article-title: Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization
  publication-title: Science
  doi: 10.1126/science.1084398
– volume: 7
  start-page: 10372
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0435
  article-title: Live-cell protein labelling with nanometre precision by cell squeezing
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms10372
– volume: 39
  start-page: 539
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0225
  article-title: Structural and functional insights into the myosin motor mechanism
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev.biophys.050708.133751
– volume: 4
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0510
  article-title: Structural dynamics of myosin 5 during processive motion revealed by interferometric scattering microscopy
  publication-title: elife
  doi: 10.7554/eLife.05413
– volume: 72
  start-page: 19
  year: 2003
  ident: 10.1016/j.bbagen.2017.08.008_bb0075
  article-title: The rotary motor of bacterial flagella
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.72.121801.161737
– volume: 93
  start-page: 51
  year: 2017
  ident: 10.1016/j.bbagen.2017.08.008_bb0015
  article-title: Single molecule detection, thermal fluctuation and life
  publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
  doi: 10.2183/pjab.93.004
– volume: 31
  start-page: 49
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0115
  article-title: Rotational mechanism of Enterococcus hirae V1-ATPase by crystal-structure and single-molecule analyses
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2015.02.013
– volume: 40
  start-page: 611
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0105
  article-title: Recent insights into the structure, regulation, and function of the V-ATPases
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2015.08.005
– volume: 468
  start-page: 72
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0250
  article-title: Video imaging of walking myosin V by high-speed atomic force microscopy
  publication-title: Nature
  doi: 10.1038/nature09450
– volume: 114
  start-page: 3318
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0045
  article-title: Molecular machines like myosin use randomness to behave predictably
  publication-title: Chem. Rev.
  doi: 10.1021/cr400344n
– volume: 2
  start-page: 168
  year: 2000
  ident: 10.1016/j.bbagen.2017.08.008_bb0490
  article-title: Single-molecule imaging of EGFR signalling on the surface of living cells
  publication-title: Nat. Cell Biol.
  doi: 10.1038/35004044
– volume: 22
  start-page: 9159
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0515
  article-title: Shot-noise limited localization of single 20nm gold particles with nanometer spatial precision within microseconds
  publication-title: Opt. Express
  doi: 10.1364/OE.22.009159
– volume: 276
  start-page: 917
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0265
  article-title: Thermodynamics and kinetics of a Brownian motor
  publication-title: Science
  doi: 10.1126/science.276.5314.917
– volume: 386
  start-page: 299
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0090
  article-title: Direct observation of the rotation of F1-ATPase
  publication-title: Nature
  doi: 10.1038/386299a0
– volume: 3
  start-page: 793
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0530
  article-title: Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
  publication-title: Nat. Methods
  doi: 10.1038/nmeth929
– volume: 103
  start-page: 8680
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0290
  article-title: Myosin-V is a mechanical ratchet
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0510191103
– volume: 36
  start-page: 349
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0180
  article-title: New fluorescent tools for watching nanometer-scale conformational changes of single molecules
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
  doi: 10.1146/annurev.biophys.36.040306.132700
– volume: 42
  start-page: 8789
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0395
  article-title: Dynamics and stability of polymorphic human telomeric G-quadruplex under tension
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku581
– volume: 6
  start-page: 814
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0305
  article-title: Phosphate release in F1-ATPase catalytic cycle follows ADP release
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.443
– volume: 316
  start-page: 1208
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0245
  article-title: Myosin V walks by lever action and Brownian motion
  publication-title: Science
  doi: 10.1126/science.1140468
– volume: 438
  start-page: 460
  year: 2005
  ident: 10.1016/j.bbagen.2017.08.008_bb0025
  article-title: Direct observation of base-pair stepping by RNA polymerase
  publication-title: Nature
  doi: 10.1038/nature04268
– volume: 42
  start-page: 111
  year: 2017
  ident: 10.1016/j.bbagen.2017.08.008_bb0165
  article-title: The growing and glowing toolbox of fluorescent and photoactive proteins
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2016.09.010
– volume: 294
  start-page: 864
  year: 2001
  ident: 10.1016/j.bbagen.2017.08.008_bb0020
  article-title: Single-molecule analysis of chemotactic signaling in Dictyostelium cells
  publication-title: Science
  doi: 10.1126/science.1063951
– volume: 5
  start-page: 3975
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0140
  article-title: Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms4975
– volume: 5
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0440
  article-title: Labeling proteins inside living cells using external fluorophores for microscopy
  publication-title: elife
  doi: 10.7554/eLife.20378
– volume: 130
  start-page: 309
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0315
  article-title: Coupling of rotation and catalysis in F-1-ATPase revealed by single-molecule imaging and manipulation
  publication-title: Cell
  doi: 10.1016/j.cell.2007.05.020
– volume: 43
  start-page: 185
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0375
  article-title: Insight into helicase mechanism and function revealed through single-molecule approaches
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583510000107
– volume: 100
  start-page: 2312
  year: 2003
  ident: 10.1016/j.bbagen.2017.08.008_bb0100
  article-title: Evidence for rotation of V1-ATPase
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0436796100
– volume: 409
  start-page: 113
  year: 2001
  ident: 10.1016/j.bbagen.2017.08.008_bb0070
  article-title: Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase
  publication-title: Nature
  doi: 10.1038/35051126
– volume: 129
  start-page: 1299
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0365
  article-title: Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase
  publication-title: Cell
  doi: 10.1016/j.cell.2007.04.038
– volume: 361
  start-page: 327
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0385
  article-title: Unwinding single RNA molecules using helicases involved in eukaryotic translation initiation
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2006.06.016
– start-page: SS1
  year: 2003
  ident: 10.1016/j.bbagen.2017.08.008_bb0405
  article-title: Single-molecule visualization in cell biology
  publication-title: Nat. Rev. Mol. Cell Biol.
– volume: 42
  start-page: 831
  year: 2017
  ident: 10.1016/j.bbagen.2017.08.008_bb0425
  article-title: Precise background subtraction in stimulated emission double depletion nanoscopy
  publication-title: Opt. Lett.
  doi: 10.1364/OL.42.000831
– volume: 21
  start-page: 766
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0430
  article-title: How to obtain labeled proteins and what to do with them
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/j.copbio.2010.09.011
– volume: 144
  start-page: 480
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0035
  article-title: Revisiting the central dogma one molecule at a time
  publication-title: Cell
  doi: 10.1016/j.cell.2011.01.033
– volume: 41
  start-page: 103
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0080
  article-title: Bacterial flagellar motor
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583508004691
– volume: 355
  start-page: 606
  year: 2017
  ident: 10.1016/j.bbagen.2017.08.008_bb0535
  article-title: Nanometer resolution imaging and tracking of fluorescent molecules with minimal photon fluxes
  publication-title: Science
  doi: 10.1126/science.aak9913
– volume: 82
  start-page: 3314
  year: 2002
  ident: 10.1016/j.bbagen.2017.08.008_bb0325
  article-title: Magnetic tweezers: micromanipulation and force measurement at the molecular level
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(02)75672-5
– volume: 12
  start-page: 290
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0215
  article-title: Direct observation of intermediate states during the stepping motion of kinesin-1
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.2028
– year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0005
– volume: 276
  start-page: 1109
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0340
  article-title: Reversible unfolding of individual titin immunoglobulin domains by AFM
  publication-title: Science
  doi: 10.1126/science.276.5315.1109
– volume: 295
  start-page: 1083
  year: 2002
  ident: 10.1016/j.bbagen.2017.08.008_bb0465
  article-title: Single-molecule speckle analysis of actin filament turnover in lamellipodia
  publication-title: Science
  doi: 10.1126/science.1067470
– volume: 289
  start-page: 31212
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0120
  article-title: Torque generation of Enterococcus hirae V-ATPase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M114.598177
– volume: 41
  start-page: 94
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0065
  article-title: How dynein moves along microtubules
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2015.11.004
– volume: 3
  start-page: 1022
  year: 2012
  ident: 10.1016/j.bbagen.2017.08.008_bb0300
  article-title: Controlled rotation of the F(1)-ATPase reveals differential and continuous binding changes for ATP synthesis
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms2026
– volume: 427
  start-page: 465
  year: 2004
  ident: 10.1016/j.bbagen.2017.08.008_bb0275
  article-title: Mechanically driven ATP synthesis by F1-ATPase
  publication-title: Nature
  doi: 10.1038/nature02212
– volume: 13
  start-page: 101
  year: 2004
  ident: 10.1016/j.bbagen.2017.08.008_bb0400
  article-title: Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(03)00481-7
– volume: 105
  start-page: 3
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0370
  article-title: Single molecule studies of helicases with magnetic tweezers
  publication-title: Methods
  doi: 10.1016/j.ymeth.2016.06.019
– volume: 73
  start-page: 705
  year: 2004
  ident: 10.1016/j.bbagen.2017.08.008_bb0145
  article-title: Mechanical processes in biochemistry
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.72.121801.161542
– volume: 5
  start-page: 626
  year: 2003
  ident: 10.1016/j.bbagen.2017.08.008_bb0455
  article-title: Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization
  publication-title: Nat. Cell Biol.
  doi: 10.1038/ncb1009
– volume: 5
  start-page: 507
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0190
  article-title: A practical guide to single-molecule FRET
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.1208
– volume: 544
  start-page: 451
  year: 2009
  ident: 10.1016/j.bbagen.2017.08.008_bb0410
  article-title: Single-molecule imaging of fluorescent proteins expressed in living cells
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-59745-483-4_30
– volume: 48
  start-page: 1
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0445
  article-title: Exploring dynamics in living cells by tracking single particles
  publication-title: Cell Biochem. Biophys.
  doi: 10.1007/s12013-007-0010-0
– volume: 5
  start-page: 789
  year: 2009
  ident: 10.1016/j.bbagen.2017.08.008_bb0270
  article-title: The role of dynamic conformational ensembles in biomolecular recognition
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.232
– volume: 36
  start-page: 171
  year: 2007
  ident: 10.1016/j.bbagen.2017.08.008_bb0155
  article-title: High-resolution, single-molecule measurements of biomolecular motion
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
  doi: 10.1146/annurev.biophys.36.101106.101451
– volume: 58
  start-page: 644
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0420
  article-title: Imaging live-cell dynamics and structure at the single-molecule level
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2015.02.033
– volume: 43
  start-page: 19
  year: 2014
  ident: 10.1016/j.bbagen.2017.08.008_bb0380
  article-title: Reconstructing folding energy landscapes by single-molecule force spectroscopy
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev-biophys-051013-022754
– volume: 5
  start-page: 491
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0345
  article-title: Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.1218
– volume: 101
  start-page: 6439
  year: 2004
  ident: 10.1016/j.bbagen.2017.08.008_bb0360
  article-title: Single-molecule assay reveals strand switching and enhanced processivity of UvrD
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0306713101
– volume: 26
  start-page: 373
  year: 1997
  ident: 10.1016/j.bbagen.2017.08.008_bb0185
  article-title: Single-particle tracking: applications to membrane dynamics
  publication-title: Annu. Rev. Biophys. Biomol. Struct.
  doi: 10.1146/annurev.biophys.26.1.373
– volume: 330
  start-page: 672
  year: 1987
  ident: 10.1016/j.bbagen.2017.08.008_bb0060
  article-title: Isolated flagellar outer arm dynein translocates brain microtubules in vitro
  publication-title: Nature
  doi: 10.1038/330672a0
– volume: 313
  start-page: 1642
  year: 2006
  ident: 10.1016/j.bbagen.2017.08.008_bb0525
  article-title: Imaging intracellular fluorescent proteins at nanometer resolution
  publication-title: Science
  doi: 10.1126/science.1127344
– volume: 368
  start-page: 113
  year: 1994
  ident: 10.1016/j.bbagen.2017.08.008_bb0040
  article-title: Single myosin molecule mechanics: piconewton forces and nanometre steps
  publication-title: Nature
  doi: 10.1038/368113a0
– volume: 37
  start-page: 317
  year: 2008
  ident: 10.1016/j.bbagen.2017.08.008_bb0355
  article-title: Translocation and unwinding mechanisms of RNA and DNA helicases
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev.biophys.37.032807.125908
– volume: 11
  start-page: 661
  year: 2016
  ident: 10.1016/j.bbagen.2017.08.008_bb0200
  article-title: Origin and control of blinking in quantum dots
  publication-title: Nat. Nanotechnol.
  doi: 10.1038/nnano.2016.140
– volume: 5
  year: 2010
  ident: 10.1016/j.bbagen.2017.08.008_bb0540
  article-title: Light sheet microscopy for single molecule tracking in living tissue
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0011639
– volume: 4
  start-page: 1631
  year: 2013
  ident: 10.1016/j.bbagen.2017.08.008_bb0260
  article-title: Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms2631
– volume: 168
  start-page: 233
  year: 2005
  ident: 10.1016/j.bbagen.2017.08.008_bb0470
  article-title: Nuclear transport of single molecules: dwell times at the nuclear pore complex
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200411005
– volume: 87
  start-page: 2079
  year: 2015
  ident: 10.1016/j.bbagen.2017.08.008_bb0210
  article-title: High-speed angle-resolved imaging of a single gold nanorod with microsecond temporal resolution and one-degree angle precision
  publication-title: Anal. Chem.
  doi: 10.1021/ac502408c
– volume: 8
  start-page: 86
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0295
  article-title: Mechanical modulation of catalytic power on F1-ATPase
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.715
– volume: 41
  start-page: 249
  year: 2011
  ident: 10.1016/j.bbagen.2017.08.008_bb0010
  article-title: Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2011.01.008
– volume: 22
  start-page: 47
  year: 2004
  ident: 10.1016/j.bbagen.2017.08.008_bb0195
  article-title: The use of nanocrystals in biological detection
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt927
SSID ssj0000595
ssj0025309
Score 2.3101568
SecondaryResourceType review_article
Snippet Biological molecular machines support various activities and behaviors of cells, such as energy production, signal transduction, growth, differentiation, and...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 241
SubjectTerms energy
image analysis
mechanical properties
Molecular machines
molecular motor proteins
Motor proteins
Signal transduction
Single-molecule imaging
Single-molecule manipulation
Title Single-molecule imaging and manipulation of biomolecular machines and systems
URI https://dx.doi.org/10.1016/j.bbagen.2017.08.008
https://www.ncbi.nlm.nih.gov/pubmed/28789884
https://www.proquest.com/docview/1927594420
https://www.proquest.com/docview/2020870092
Volume 1862
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3BTtwwEB0hUFUuFYUWtqUolXo1G8d27BzRCrTtCg6lCG5W4tjSVpBF7HLohW9nJo6pkIqQekmU2I6smfH4OR7PA_iGGL0IuXZMcokXzQNrXFmwvGhVXYtWx_8dp2fl9EL-uFJXazBJZ2EorHLw_dGn9956eDMepDm-nc_H57Sph3BCcfxeoQT5YSk1Wfnhw98wD4QPKu4kSEa10_G5PsaraXDQUhZUrvtEnkQy-e_p6SX42U9DJ1vwbsCP2VHs4ntY8902vImMkn-24e0kEbjtwOk5TkvXnt1EBlyfzW96SqKs7tqM0l4k6q5sETI6hp-YcrGQIiz9sq8Zcz0vP8DFyfGvyZQN7AnMiUqtmFc8iOBLgYhHmTy0bc1D1bac4suc8lrg9CgbVYTGYbEUDtFeYxQOaFwici8-wnq36PweZFUrTCnrELQvpHOiqQx3RR6CqE1Z6zACkYRm3ZBanBgurm2KIftto6gtidoS8WVuRsCeWt3G1Bqv1NdJH_aZiVj0_q-0_JrUZ1EHtCVSd35xv7SIb7Wq0F7zl-sUxGOqKTnVCHaj7p_6i-tNUxkjP_133z7DJj6ZGAi-D-uru3v_BXHOqjnoDfkANo6-z6ZndJ_9vJw9Ag22_fM
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT-MwEB0h0Iq9IBbYpbAfWYmraRzbsXNE1Vbd3bYXWomblTi21BWkiJYDF3474zguQgIh7SWHeBxZM_bMczyeB3CGGD1zqTSEU44PSR2pTJ6RNKtFWbJahv8dk2k-mvM_V-JqCwbxLoxPq-x8f_Dprbfu3vQ7bfZvF4v-pT_UQzghKH4vEwz98A7H5etpDM4fn_M8ED-IcJTAiReP9-faJK-qwlXry6BS2Vby9CyTr8ent_BnG4eG-7DXAcjkIozxE2zZ5gA-BErJhwPYHUQGt0OYXGJcurbkJlDg2mRx03ISJWVTJ77uReTuSpYu8ffwI1UuNvoUS7tqJUOx59URzIe_ZoMR6egTiGGFWBMrqGPO5gwhj1Cpq-uSuqKuqU8wM8JKhvGRVyJzlcFmzgzCvUoJXNG4R6SWfYbtZtnYY0iKmqmcl85Jm3FjWFUoarLUOVaqvJSuBywqTZuutrinuLjWMYnsnw6q1l7V2jNfpqoHZNPrNtTWeEdeRnvoF3NEo_t_p-fPaD6NNvBnImVjl_crjQBXigInbPq2TOaJTKWvTtWDL8H2m_HihlMVSvGT_x7bD9gdzSZjPf49_XsKH7FFhazwr7C9vru33xD0rKvv7aR-At60_d4
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=Single-molecule+imaging+and+manipulation+of+biomolecular+machines+and+systems&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Iino%2C+Ryota&rft.au=Iida%2C+Tatsuya&rft.au=Nakamura%2C+Akihiko&rft.au=Saita%2C+Ei-Ichiro&rft.date=2018-02-01&rft.issn=0304-4165&rft.volume=1862&rft.issue=2&rft.spage=241&rft_id=info:doi/10.1016%2Fj.bbagen.2017.08.008&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon