Fluorophore Targeting to Cellular Proteins via Enzyme-Mediated Azide Ligation and Strain-Promoted Cycloaddition
Methods for targeting of small molecules to cellular proteins can allow imaging with fluorophores that are smaller, brighter, and more photostable than fluorescent proteins. Previously, we reported targeting of the blue fluorophore coumarin to cellular proteins fused to a 13-amino acid recognition s...
Saved in:
Published in | Journal of the American Chemical Society Vol. 134; no. 8; pp. 3720 - 3728 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
29.02.2012
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Methods for targeting of small molecules to cellular proteins can allow imaging with fluorophores that are smaller, brighter, and more photostable than fluorescent proteins. Previously, we reported targeting of the blue fluorophore coumarin to cellular proteins fused to a 13-amino acid recognition sequence (LAP), catalyzed by a mutant of the Escherichia coli enzyme lipoic acid ligase (LplA). Here, we extend LplA-based labeling to green- and red-emitting fluorophores by employing a two-step targeting scheme. First, we found that the W37I mutant of LplA catalyzes site-specific ligation of 10-azidodecanoic acid to LAP in cells, in nearly quantitative yield after 30 min. Second, we evaluated a panel of five different cyclooctyne structures and found that fluorophore conjugates to aza-dibenzocyclooctyne (ADIBO) gave the highest and most specific derivatization of azide-conjugated LAP in cells. However, for targeting of hydrophobic fluorophores such as ATTO 647N, the hydrophobicity of ADIBO was detrimental, and superior targeting was achieved by conjugation to the less hydrophobic monofluorinated cyclooctyne (MOFO). Our optimized two-step enzymatic/chemical labeling scheme was used to tag and image a variety of LAP fusion proteins in multiple mammalian cell lines with diverse fluorophores including fluorescein, rhodamine, Alexa Fluor 568, ATTO 647N, and ATTO 655. |
---|---|
AbstractList | Methods for fluorophore targeting to cellular proteins can allow imaging with dyes that are smaller, brighter, and more photostable than fluorescent proteins. Previously, we reported targeting of the blue fluorophore coumarin to cellular proteins fused to a 13-amino acid recognition sequence (LAP), catalyzed by a mutant of the
E. coli
enzyme lipoic acid ligase (LplA). Here, we extend LplA-based labeling to green- and red-emitting fluorophores by employing a two-step targeting scheme. First, we found that the W37I mutant of LplA catalyzes site-specific ligation of 10-azidodecanoic acid to LAP in cells, in nearly quantitative yield after 30 minutes. Second, we evaluated a panel of five different cyclooctyne structures, and found that fluorophore conjugates to aza-dibenzocyclooctyne (ADIBO) gave the highest and most specific derivatization of azide-conjugated LAP in cells. However, for targeting of hydrophobic fluorophores such as ATTO 647N, the hydrophobicity of ADIBO was detrimental, and superior targeting was achieved by conjugation to the less hydrophobic monofluorinated cyclooctyne (MOFO). Our optimized two-step enzymatic/chemical labeling scheme was used to tag and image a variety of LAP fusion proteins in multiple mammalian cell lines with diverse fluorophores including fluorescein, rhodamine, Alexa Fluor 568, ATTO 647N, and ATTO 655. Methods for targeting of small molecules to cellular proteins can allow imaging with fluorophores that are smaller, brighter, and more photostable than fluorescent proteins. Previously, we reported targeting of the blue fluorophore coumarin to cellular proteins fused to a 13-amino acid recognition sequence (LAP), catalyzed by a mutant of the Escherichia coli enzyme lipoic acid ligase (LplA). Here, we extend LplA-based labeling to green- and red-emitting fluorophores by employing a two-step targeting scheme. First, we found that the W37I mutant of LplA catalyzes site-specific ligation of 10-azidodecanoic acid to LAP in cells, in nearly quantitative yield after 30 min. Second, we evaluated a panel of five different cyclooctyne structures and found that fluorophore conjugates to aza-dibenzocyclooctyne (ADIBO) gave the highest and most specific derivatization of azide-conjugated LAP in cells. However, for targeting of hydrophobic fluorophores such as ATTO 647N, the hydrophobicity of ADIBO was detrimental, and superior targeting was achieved by conjugation to the less hydrophobic monofluorinated cyclooctyne (MOFO). Our optimized two-step enzymatic/chemical labeling scheme was used to tag and image a variety of LAP fusion proteins in multiple mammalian cell lines with diverse fluorophores including fluorescein, rhodamine, Alexa Fluor 568, ATTO 647N, and ATTO 655. |
Author | Uttamapinant, Chayasith Poloukhtine, Andrei Sletten, Ellen M Popik, Vladimir V Yao, Jennifer Z Codelli, Julian A Bertozzi, Carolyn R Ting, Alice Y Baskin, Jeremy M |
AuthorAffiliation | Massachusetts Institute of Technology Molecular and Cell Biology and Howard Hughes Medical Institute Lawrence Berkeley National Laboratory Departments of Chemistry University of California University of Georgia |
AuthorAffiliation_xml | – name: Departments of Chemistry – name: – name: University of California – name: Molecular and Cell Biology and Howard Hughes Medical Institute – name: Lawrence Berkeley National Laboratory – name: University of Georgia – name: Massachusetts Institute of Technology – name: Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue. Cambridge, Massachusetts 02139 – name: Department of Chemistry, Complex Carbohydrate Research Center, University of Georgia, Athens, 30602 – name: Department of Chemistry, University of California, Berkeley, California 94720, and The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720 – name: γ Bioconjugate Technologies, LLC, 7850 E. Evans Road, Ste 107, Scottsdale, Arizona, 85260 – name: Department of Chemistry, California Institute of Technology, 1200 East California Boulevard. Pasadena, California 91125 – name: Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, and The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720 |
Author_xml | – sequence: 1 givenname: Jennifer Z surname: Yao fullname: Yao, Jennifer Z – sequence: 2 givenname: Chayasith surname: Uttamapinant fullname: Uttamapinant, Chayasith – sequence: 3 givenname: Andrei surname: Poloukhtine fullname: Poloukhtine, Andrei – sequence: 4 givenname: Jeremy M surname: Baskin fullname: Baskin, Jeremy M – sequence: 5 givenname: Julian A surname: Codelli fullname: Codelli, Julian A – sequence: 6 givenname: Ellen M surname: Sletten fullname: Sletten, Ellen M – sequence: 7 givenname: Carolyn R surname: Bertozzi fullname: Bertozzi, Carolyn R – sequence: 8 givenname: Vladimir V surname: Popik fullname: Popik, Vladimir V – sequence: 9 givenname: Alice Y surname: Ting fullname: Ting, Alice Y email: ating@mit.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22239252$$D View this record in MEDLINE/PubMed |
BookMark | eNptkVtrGzEQhUVISZzLQ_9A0EsJfdhWl72-FIxJ2oJDCkmexViadWR2JUfaDdi_vjJ2TQt9Gob55sxwzgU5dd4hIR85-8KZ4F9XIFjNGrY-IRNeCJYVXJSnZMIYE1lVl_KcXMS4Sm0uan5GzoUQshGFmBB_340--PWrD0ifISxxsG5JB09n2HVjB4H-Cn5A6yJ9t0Dv3HbTY_aAxsKAhk631iCd2yUM1jsKztCnIYB1WVrr_Q6ZbXTnwRi7I67Ihxa6iNeHekle7u-eZz-y-eP3n7PpPIO8YkNWV6Yq5EI3vG0bWZUCZQ5NjahFaySYPDdVDQ3PAXPQpWj4giG0Gk2CC1nLS_Jtr7seFz0ajS591al1sD2EjfJg1b8TZ1_V0r8rKVlZ8yoJ3B4Egn8bMQ6qt1EnT8ChH6NK9lW85Iwl8vOe1MHHGLA9XuFM7fJRx3wSe_P3W0fyTyAJ-LQHQEe18mNwyaX_CP0GaVqb5A |
CitedBy_id | crossref_primary_10_1016_j_tetlet_2013_11_003 crossref_primary_10_1021_cb500957k crossref_primary_10_5059_yukigoseikyokaishi_74_453 crossref_primary_10_1246_bcsj_20180104 crossref_primary_10_1039_D1CS01004B crossref_primary_10_1038_s41467_024_45124_2 crossref_primary_10_1093_jmicro_dfaa011 crossref_primary_10_1021_jacs_5b06847 crossref_primary_10_1039_D3SC01754K crossref_primary_10_1002_anie_201706076 crossref_primary_10_1002_slct_202302947 crossref_primary_10_1021_jacs_7b03121 crossref_primary_10_1038_nprot_2013_096 crossref_primary_10_1039_C2OB26561C crossref_primary_10_1098_rstb_2015_0492 crossref_primary_10_1038_s41598_023_36163_8 crossref_primary_10_1002_ejoc_201201627 crossref_primary_10_1021_nn304793z crossref_primary_10_1091_mbc_E24_04_0174 crossref_primary_10_1021_acsapm_9b00334 crossref_primary_10_1021_acs_chemrev_2c00213 crossref_primary_10_1002_asia_202101317 crossref_primary_10_1002_chem_201403128 crossref_primary_10_1038_nchem_2253 crossref_primary_10_1242_jcs_202952 crossref_primary_10_1371_journal_pone_0226579 crossref_primary_10_1021_cb400828a crossref_primary_10_1002_cptc_202000059 crossref_primary_10_1002_cptc_202000215 crossref_primary_10_1021_jacs_6b08733 crossref_primary_10_1039_C4CS00139G crossref_primary_10_1021_acs_orglett_9b03981 crossref_primary_10_1021_acs_bioconjchem_9b00051 crossref_primary_10_1021_acs_bioconjchem_5b00161 crossref_primary_10_1002_cbic_201200407 crossref_primary_10_1021_ja307647x crossref_primary_10_1002_cbic_201300453 crossref_primary_10_1016_j_neuron_2012_04_026 crossref_primary_10_1039_C3OB42267D crossref_primary_10_1002_ange_201108181 crossref_primary_10_1021_ja405745v crossref_primary_10_1002_anie_201108181 crossref_primary_10_1021_bc400102w crossref_primary_10_1194_jlr_D074070 crossref_primary_10_1016_j_eurpolymj_2014_07_004 crossref_primary_10_1002_aoc_4798 crossref_primary_10_1021_acs_biochem_0c00533 crossref_primary_10_1021_acs_orglett_1c03201 crossref_primary_10_1021_bi501342w crossref_primary_10_1016_j_cbpa_2013_05_015 crossref_primary_10_1021_bi400268m crossref_primary_10_1021_ol500260d crossref_primary_10_1002_ange_201301100 crossref_primary_10_1016_j_chembiol_2014_08_009 crossref_primary_10_1021_ol500389t crossref_primary_10_1016_j_bmc_2018_02_040 crossref_primary_10_1039_c2ob26409a crossref_primary_10_1021_acs_analchem_5b02612 crossref_primary_10_1002_cbic_201500042 crossref_primary_10_1021_cb5002119 crossref_primary_10_1155_2019_3620546 crossref_primary_10_1021_bc500349h crossref_primary_10_1021_acs_bioconjchem_6b00718 crossref_primary_10_1002_chem_201302502 crossref_primary_10_5936_csbj_201402001 crossref_primary_10_3390_molecules21091163 crossref_primary_10_1021_acs_bioconjchem_9b00157 crossref_primary_10_1002_anie_201301100 crossref_primary_10_1021_acs_bioconjchem_9b00710 crossref_primary_10_1021_ja309000s crossref_primary_10_1039_C6PY00856A crossref_primary_10_1002_cbic_201100764 crossref_primary_10_1021_acs_macromol_9b01609 crossref_primary_10_1002_ange_201706076 crossref_primary_10_1039_c3ob41507d crossref_primary_10_1016_j_molcel_2015_03_002 crossref_primary_10_1021_acschembio_6b00346 crossref_primary_10_1021_acs_bioconjchem_9b00203 crossref_primary_10_1002_hlca_201200260 crossref_primary_10_1039_C6MB00023A crossref_primary_10_1021_ja402424j crossref_primary_10_1242_jcs_123612 crossref_primary_10_1039_C3RA46991C crossref_primary_10_1021_bc300364z crossref_primary_10_1128_ecosalplus_esp_0001_2012 crossref_primary_10_1021_ja3070073 crossref_primary_10_1021_acs_analchem_0c03964 crossref_primary_10_1038_s41557_021_00641_1 crossref_primary_10_1002_bip_22407 crossref_primary_10_1371_journal_pone_0052823 crossref_primary_10_1021_jacs_6b04049 crossref_primary_10_1186_s12870_016_0907_0 crossref_primary_10_1021_ja500451w crossref_primary_10_1039_c2ob25752a crossref_primary_10_1007_s00441_015_2145_4 crossref_primary_10_1007_s11033_021_06853_5 crossref_primary_10_1039_C9MD00218A crossref_primary_10_1039_c2sc20652h crossref_primary_10_1371_journal_pone_0074200 |
Cites_doi | 10.1021/ol102205j 10.1002/cbic.201000414 10.1038/nrm2531 10.1021/bi201037r 10.1021/ol202619f 10.1002/anie.201003761 10.1073/pnas.0807820106 10.1016/j.yexcr.2010.04.011 10.1021/bc100272z 10.1126/science.281.5374.269 10.1002/anie.201008267 10.1002/anie.200802088 10.1021/ol2025026 10.1039/c0sc00631a 10.1039/C1CC14415D 10.1021/ar200148z 10.1038/nbt1355 10.1021/cb800025k 10.1021/cb6003228 10.1073/pnas.0707090104 10.1021/cb700054k 10.1002/anie.201008178 10.1021/ja209325n 10.1074/jbc.M109.078717 10.1016/j.chembiol.2008.01.007 10.1021/ja803086r 10.1126/science.1154228 10.1021/bc100306u 10.1002/cbic.201100277 10.1073/pnas.0914067107 10.1039/B917797C 10.1016/j.bpj.2011.09.006 10.1021/ja106553e 10.1007/s004240100619 10.1021/ja904596f 10.1038/nmeth.1768 10.1002/jbio.201100018 10.1002/cbic.201000419 10.1073/pnas.0911116107 10.1016/j.cell.2010.12.002 10.1126/science.1155106 10.1021/ja100014q 10.1016/S0065-2911(05)50003-1 10.1021/ol801141k 10.1039/c0cs00123f 10.1021/ja1081519 |
ContentType | Journal Article |
Copyright | Copyright © 2012 American Chemical
Society 2012 American Chemical Society |
Copyright_xml | – notice: Copyright © 2012 American Chemical Society – notice: 2012 American Chemical Society |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
DOI | 10.1021/ja208090p |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE |
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 | Chemistry |
EISSN | 1520-5126 |
EndPage | 3728 |
ExternalDocumentID | 10_1021_ja208090p 22239252 c153195383 |
Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R37 GM058867 – fundername: NIGMS NIH HHS grantid: R01 GM086214-01 – fundername: NIGMS NIH HHS grantid: R01 GM086214 – fundername: National Institute of General Medical Sciences : NIGMS grantid: R01 GM086214-01 || GM |
GroupedDBID | - .K2 02 4.4 53G 55A 5GY 5RE 5VS 7~N 85S AABXI ABFLS ABMVS ABPPZ ABPTK ABUCX ABUFD ACGFS ACJ ACNCT ACS AEESW AENEX AETEA AFEFF ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH BKOMP CS3 DU5 DZ EBS ED ED~ EJD ET F5P GNL IH9 JG JG~ K2 LG6 P2P ROL RXW TAE TAF TN5 UHB UI2 UKR UPT VF5 VG9 VQA W1F WH7 X XFK YZZ ZHY --- -DZ -ET -~X .DC AAHBH ABJNI ABQRX ACBEA ACGFO ADHLV ADOJD AGXLV AHGAQ CGR CUPRZ CUY CVF ECM EIF GGK IH2 NPM XSW YQT ZCA ~02 AAYXX CITATION 7X8 5PM |
ID | FETCH-LOGICAL-a470t-87d753bc91ff93762e34a98eec2fd3ad44d78a914ae4ac6291b0eafced3765383 |
IEDL.DBID | ACS |
ISSN | 0002-7863 |
IngestDate | Tue Sep 17 21:25:57 EDT 2024 Wed Dec 04 14:30:58 EST 2024 Fri Dec 06 03:10:02 EST 2024 Sat Nov 02 12:13:38 EDT 2024 Thu Aug 27 13:42:38 EDT 2020 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 8 |
Language | English |
License | 2012 American Chemical Society |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a470t-87d753bc91ff93762e34a98eec2fd3ad44d78a914ae4ac6291b0eafced3765383 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://europepmc.org/articles/pmc3306817?pdf=render |
PMID | 22239252 |
PQID | 925716100 |
PQPubID | 23479 |
PageCount | 9 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3306817 proquest_miscellaneous_925716100 crossref_primary_10_1021_ja208090p pubmed_primary_22239252 acs_journals_10_1021_ja208090p |
ProviderPackageCode | JG~ 55A AABXI GNL VF5 7~N ACJ VG9 W1F ACS AEESW AFEFF .K2 ABMVS ABUCX IH9 BAANH AQSVZ ED~ UI2 |
PublicationCentury | 2000 |
PublicationDate | 2012-02-29 |
PublicationDateYYYYMMDD | 2012-02-29 |
PublicationDate_xml | – month: 02 year: 2012 text: 2012-02-29 day: 29 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Journal of the American Chemical Society |
PublicationTitleAlternate | J. Am. Chem. Soc |
PublicationYear | 2012 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | Jin X. (ref14/cit14) 2011; 12 Fernández-Suárez M. (ref1/cit1) 2008; 9 Kuzmin A. (ref21/cit21) 2010; 21 Pauff S. M. (ref48/cit48) 2011; 13 Fujiwara K. (ref18/cit18) 2010; 285 Dommerholt J. (ref33/cit50) 2010; 49 Los G. V. (ref4/cit4) 2008; 3 Griffin B. A. (ref6/cit6) 1998; 281 Fernández-Suárez M. (ref19/cit19) 2007; 25 Zhou Z. (ref10/cit10) 2007; 2 Cohen J. D. (ref15/cit15) 2011; 50 Jewett J. C. (ref41/cit41) 2011; 13 Chang P. V. (ref31/cit31) 2010; 107 Baruah H. (ref16/cit16) 2008; 47 Liu D. S. (ref49/cit49) 2012; 134 Debets M. F. (ref37/cit37) 2010; 46 Westphal V. (ref44/cit44) 2008; 320 Gautier A. (ref5/cit5) 2008; 15 Stockmann H. (ref38/cit38) 2011; 2 Cronan J. E. (ref12/cit12) 2005; 50 Popp M. W. L. (ref9/cit9) 2011; 50 Sletten E. M. (ref32/cit32) 2008; 10 Jayaprakash K. N. (ref39/cit39) 2010; 12 Wombacher R. (ref3/cit3) 2011; 4 Puthenveetil S. (ref13/cit13) 2009; 131 Dempsey G. T. (ref17/cit17) 2011; 8 Agard N. J. (ref20/cit20) 2006; 1 Bostic H. E. (ref40/cit40) 2012; 48 Stroffekova K. (ref8/cit8) 2001; 442 Beatty K. E. (ref26/cit26) 2010; 11 Laughlin S. T. (ref30/cit30) 2008; 320 Sanders B. C. (ref36/cit36) 2011; 133 Hong V. (ref25/cit25) 2010; 21 Beatty K. E. (ref27/cit27) 2011; 12 Codelli J. A. (ref34/cit34) 2008; 130 Plass T. (ref28/cit28) 2011; 50 Lim J. I. (ref42/cit42) 2010; 316 Sletten E. M. (ref24/cit24) 2011; 44 Baskin J. M. (ref29/cit29) 2007; 104 Jewett J. C. (ref35/cit35) 2010; 132 Uttamapinant C. (ref7/cit7) 2010; 107 Wu P. (ref11/cit11) 2009; 106 del Amo D. S. (ref23/cit23) 2010; 132 Mueller V. (ref43/cit43) 2011; 101 Schilling C. I. (ref22/cit22) 2011; 40 Huang B. (ref2/cit2) 2010; 143 |
References_xml | – volume: 12 start-page: 5410 year: 2010 ident: ref39/cit39 publication-title: Org. Lett. doi: 10.1021/ol102205j contributor: fullname: Jayaprakash K. N. – volume: 12 start-page: 65 year: 2011 ident: ref14/cit14 publication-title: ChemBioChem doi: 10.1002/cbic.201000414 contributor: fullname: Jin X. – volume: 9 start-page: 929 year: 2008 ident: ref1/cit1 publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2531 contributor: fullname: Fernández-Suárez M. – volume: 50 start-page: 8221 year: 2011 ident: ref15/cit15 publication-title: Biochemistry doi: 10.1021/bi201037r contributor: fullname: Cohen J. D. – volume: 13 start-page: 6196 year: 2011 ident: ref48/cit48 publication-title: Org. Lett. doi: 10.1021/ol202619f contributor: fullname: Pauff S. M. – volume: 49 start-page: 9422 year: 2010 ident: ref33/cit50 publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201003761 contributor: fullname: Dommerholt J. – volume: 106 start-page: 3000 year: 2009 ident: ref11/cit11 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0807820106 contributor: fullname: Wu P. – volume: 316 start-page: 2027 year: 2010 ident: ref42/cit42 publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2010.04.011 contributor: fullname: Lim J. I. – volume: 21 start-page: 1912 year: 2010 ident: ref25/cit25 publication-title: Bioconjugate Chem. doi: 10.1021/bc100272z contributor: fullname: Hong V. – volume: 281 start-page: 269 year: 1998 ident: ref6/cit6 publication-title: Science doi: 10.1126/science.281.5374.269 contributor: fullname: Griffin B. A. – volume: 50 start-page: 5024 year: 2011 ident: ref9/cit9 publication-title: Angew. Chem., Int. Ed. doi: 10.1002/anie.201008267 contributor: fullname: Popp M. W. L. – volume: 47 start-page: 7018 year: 2008 ident: ref16/cit16 publication-title: Angew. Chem., Int. Ed. doi: 10.1002/anie.200802088 contributor: fullname: Baruah H. – volume: 13 start-page: 5937 year: 2011 ident: ref41/cit41 publication-title: Org. Lett. doi: 10.1021/ol2025026 contributor: fullname: Jewett J. C. – volume: 2 start-page: 932 year: 2011 ident: ref38/cit38 publication-title: Chem. Sci. doi: 10.1039/c0sc00631a contributor: fullname: Stockmann H. – volume: 48 start-page: 1431 year: 2012 ident: ref40/cit40 publication-title: Chem. Commun. doi: 10.1039/C1CC14415D contributor: fullname: Bostic H. E. – volume: 44 start-page: 666 year: 2011 ident: ref24/cit24 publication-title: Acc. Chem. Res. doi: 10.1021/ar200148z contributor: fullname: Sletten E. M. – volume: 25 start-page: 1483 year: 2007 ident: ref19/cit19 publication-title: Nat. Biotechnol. doi: 10.1038/nbt1355 contributor: fullname: Fernández-Suárez M. – volume: 3 start-page: 373 year: 2008 ident: ref4/cit4 publication-title: ACS Chem. Biol. doi: 10.1021/cb800025k contributor: fullname: Los G. V. – volume: 1 start-page: 644 year: 2006 ident: ref20/cit20 publication-title: ACS Chem. Biol. doi: 10.1021/cb6003228 contributor: fullname: Agard N. J. – volume: 104 start-page: 16793 year: 2007 ident: ref29/cit29 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0707090104 contributor: fullname: Baskin J. M. – volume: 2 start-page: 337 year: 2007 ident: ref10/cit10 publication-title: ACS Chem. Biol. doi: 10.1021/cb700054k contributor: fullname: Zhou Z. – volume: 50 start-page: 3878 year: 2011 ident: ref28/cit28 publication-title: Angew. Chem., Int. Ed. doi: 10.1002/anie.201008178 contributor: fullname: Plass T. – volume: 134 start-page: 792 year: 2012 ident: ref49/cit49 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja209325n contributor: fullname: Liu D. S. – volume: 285 start-page: 9971 year: 2010 ident: ref18/cit18 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.078717 contributor: fullname: Fujiwara K. – volume: 15 start-page: 128 year: 2008 ident: ref5/cit5 publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2008.01.007 contributor: fullname: Gautier A. – volume: 130 start-page: 11486 year: 2008 ident: ref34/cit34 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja803086r contributor: fullname: Codelli J. A. – volume: 320 start-page: 246 year: 2008 ident: ref44/cit44 publication-title: Science doi: 10.1126/science.1154228 contributor: fullname: Westphal V. – volume: 21 start-page: 2076 year: 2010 ident: ref21/cit21 publication-title: Bioconjugate Chem. doi: 10.1021/bc100306u contributor: fullname: Kuzmin A. – volume: 12 start-page: 2137 year: 2011 ident: ref27/cit27 publication-title: ChemBioChem doi: 10.1002/cbic.201100277 contributor: fullname: Beatty K. E. – volume: 107 start-page: 10914 year: 2010 ident: ref7/cit7 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0914067107 contributor: fullname: Uttamapinant C. – volume: 46 start-page: 97 year: 2010 ident: ref37/cit37 publication-title: Chem. Commun. doi: 10.1039/B917797C contributor: fullname: Debets M. F. – volume: 101 start-page: 1651 year: 2011 ident: ref43/cit43 publication-title: Biophys. J. doi: 10.1016/j.bpj.2011.09.006 contributor: fullname: Mueller V. – volume: 132 start-page: 16893 year: 2010 ident: ref23/cit23 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja106553e contributor: fullname: del Amo D. S. – volume: 442 start-page: 859 year: 2001 ident: ref8/cit8 publication-title: Pflugers Arch. Ges. Phys. doi: 10.1007/s004240100619 contributor: fullname: Stroffekova K. – volume: 131 start-page: 16430 year: 2009 ident: ref13/cit13 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja904596f contributor: fullname: Puthenveetil S. – volume: 8 start-page: 1027 year: 2011 ident: ref17/cit17 publication-title: Nat. Methods doi: 10.1038/nmeth.1768 contributor: fullname: Dempsey G. T. – volume: 4 start-page: 391 year: 2011 ident: ref3/cit3 publication-title: J. Biophoton. doi: 10.1002/jbio.201100018 contributor: fullname: Wombacher R. – volume: 11 start-page: 2092 year: 2010 ident: ref26/cit26 publication-title: ChemBioChem doi: 10.1002/cbic.201000419 contributor: fullname: Beatty K. E. – volume: 107 start-page: 1821 year: 2010 ident: ref31/cit31 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0911116107 contributor: fullname: Chang P. V. – volume: 143 start-page: 1047 year: 2010 ident: ref2/cit2 publication-title: Cell doi: 10.1016/j.cell.2010.12.002 contributor: fullname: Huang B. – volume: 320 start-page: 664 year: 2008 ident: ref30/cit30 publication-title: Science doi: 10.1126/science.1155106 contributor: fullname: Laughlin S. T. – volume: 132 start-page: 3688 year: 2010 ident: ref35/cit35 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja100014q contributor: fullname: Jewett J. C. – volume: 50 start-page: 103 year: 2005 ident: ref12/cit12 publication-title: Adv. Microb. Physiol. doi: 10.1016/S0065-2911(05)50003-1 contributor: fullname: Cronan J. E. – volume: 10 start-page: 3097 year: 2008 ident: ref32/cit32 publication-title: Org. Lett. doi: 10.1021/ol801141k contributor: fullname: Sletten E. M. – volume: 40 start-page: 4840 year: 2011 ident: ref22/cit22 publication-title: Chem. Soc. Rev. doi: 10.1039/c0cs00123f contributor: fullname: Schilling C. I. – volume: 133 start-page: 949 year: 2011 ident: ref36/cit36 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja1081519 contributor: fullname: Sanders B. C. |
SSID | ssj0004281 |
Score | 2.4528897 |
Snippet | Methods for targeting of small molecules to cellular proteins can allow imaging with fluorophores that are smaller, brighter, and more photostable than... Methods for fluorophore targeting to cellular proteins can allow imaging with dyes that are smaller, brighter, and more photostable than fluorescent proteins.... |
SourceID | pubmedcentral proquest crossref pubmed acs |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 3720 |
SubjectTerms | Animals Azides - chemistry Azides - metabolism Biocatalysis Cells, Cultured Chlorocebus aethiops COS Cells Cyclization Cyclooctanes - chemistry Cyclooctanes - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fluorescent Dyes - chemistry Fluorescent Dyes - metabolism HEK293 Cells HeLa Cells Humans Ligases - chemistry Ligases - genetics Ligases - metabolism Luminescent Proteins - chemistry Luminescent Proteins - metabolism Molecular Structure Mutation |
Title | Fluorophore Targeting to Cellular Proteins via Enzyme-Mediated Azide Ligation and Strain-Promoted Cycloaddition |
URI | http://dx.doi.org/10.1021/ja208090p https://www.ncbi.nlm.nih.gov/pubmed/22239252 https://search.proquest.com/docview/925716100 https://pubmed.ncbi.nlm.nih.gov/PMC3306817 |
Volume | 134 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwhV1LT9wwEB5Remgvbelz24KsttegxDZxfEQpK1RBhQRI3CK_IlZs7dVuFon99Yy9G8qWtlxy8SRKPM7MN5qZbwC-VbJimpUq27OCZrzFixSFzkxZWKcQQ2sVA8Xjn-XhOf9xsXexAV__kcGnkR-IIqqR-eQJPKUCw-6If-rT382PtCp6jCuqkvX0Qfdvja7HzNZdzwM8-WdZ5D0_M3wJ3_tunWV5ydXuvNO7ZvGQvPF_n_AKXqxwJtlfHowt2HD-NTyr-_FubyAMx_MwDZPLMHXkLNWDoxcjXSC1G49jcSo5iRwOIz8j1yNFDvzi5pfLjtNoD2fJ_mJkHTlKDB3BE-UtOU3zJrKTVOGHIvWNGYdYsBQl3sL58OCsPsxW0xcyxUXeoZm0GMpoI4u2RQxTUse4kpVzhraWKcu5FZWSBVeOK1NSWejcqdY4i8JoRtk72PTBuw9ASsl43iIwy5XkrdGKFi0qzlomVSWFHsAOqqdZ_T2zJiXGKQYm_b4N4EuvuWayZOH4mxDpddrgXsbEh_IuzGeNRLuEyDbPB_B-qeK7p0R4hMt0AGJN-XcCkX57fcWPLhMNN8NoqyrEx8de_hM8R5RFUx-8_Ayb3XTuthHJdHonneRbiLnvtg |
link.rule.ids | 230,314,780,784,885,2765,27076,27924,27925,56738,56788 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3fT9swELYYPLCXDcaAMgbWxGtQYrtJ_Igiqm5rERJF4i3yr4hqnV016ST613N2G6AMaXvJiy_Wxef4vtOdv0PoLOc5lTQVUVdnJGIVPHiWyEiliTYCMLQUPlAcXqX9W_bjrnu3osnxd2FAiRpmqkMS_5ldwNMEEQA3PJ6-Q1td36rSw6Di5vkOJMmTFupmeUpbFqGXr3oPpOp1D_QXrHxdHfnC3fQ-LvsWBUVDlcmv83kjz9XiFYfj_33JDvqwQp34YrlNdtGGsZ_QdtE2e9tDrjeZu5mb3ruZwaNQHQ4-DTcOF2Yy8aWq-NozOoxtjf-MBb60i4ffJhqGRh9G44vFWBs8CHwdzmJhNb4J3Sei61DvByLFg5o4X77kJT6j297lqOhHq14MkWBZ3MChqSGwkYonVQWIJiWGMsFzYxSpNBWaMZ3lgidMGCZUSngiYyMqZTQIw6FK99GmddYcIpxyyuIKYFosOKuUFCSpwH5aUy5ynskOOoFlK1f_Ul2GNDmBMKVdtw761hqwnC45Od4Swq1pS1hLnwYR1rh5XXI4pQDnxnEHHSwt_TSLB0swTDooW9sDTwKejHt9xI7vAyk3hdgrT7Kjfyl_irb7o-GgHHy_-vkFvQf8RcINeX6MNpvZ3HwFjNPIk7C5HwG4Jvgj |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwELdgSLAXvjfKx7AQr5kS203ixyqsGrCNStukvUX-1CqKXTUp0vrXc3aTsg4keMmLz5bjs-9-J59_h9DHkpdU0lwkQ12QhFn48CKTicozbQRgaClCoHh6lh9fsi9Xw6suUAxvYWASDYzUxEv8cKrn2nYMA4EqiADA4en8PnowBCsbUrhG1fnvd5CkzHq4W5Q57ZmEbncNXkg1217oD2h5N0PylssZP0HfNpONmSbfD5etPFSrOzyO__83T9HjDn3i0Xq7PEP3jHuOHlV90bcXyI9nS7_w82u_MPgiZomDb8Otx5WZzULKKp4EZoepa_DPqcBHbnXzwySnseCH0Xi0mmqDTyJvh3dYOI3PYxWKZBLz_kCkulEzH9KYgsRLdDk-uqiOk64mQyJYkbZgPDUEOFLxzFpANjkxlAleGqOI1VRoxnRRCp4xYZhQOeGZTI2wymgQBuNK99CO8868QjjnlKUW4FoqOLNKCpJZ0KHWlIuSF3KADmDp6u5MNXW8LicQrvTrNkAfeiXW8zU3x9-EcK_eGtYyXIcIZ_yyqTlYK8C7aTpA-2ttb0YJoAmayQAVW_tgIxBIubdb3PQ6knNTiMHKrHj9r8m_Rw8nn8b1yeezr2_QLsAwEh_K87dop10szTuAOq08iPv7F7jn-qY |
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=Fluorophore+targeting+to+cellular+proteins+via+enzyme-mediated+azide+ligation+and+strain-promoted+cycloaddition&rft.jtitle=Journal+of+the+American+Chemical+Society&rft.au=Yao%2C+Jennifer+Z.&rft.au=Uttamapinant%2C+Chayasith&rft.au=Poloukhtine%2C+Andrei&rft.au=Baskin%2C+Jeremy+M.&rft.date=2012-02-29&rft.issn=0002-7863&rft.eissn=1520-5126&rft.volume=134&rft.issue=8&rft.spage=3720&rft.epage=3728&rft_id=info:doi/10.1021%2Fja208090p&rft_id=info%3Apmid%2F22239252&rft.externalDBID=PMC3306817 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0002-7863&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0002-7863&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0002-7863&client=summon |