Adhesins of Yeasts: Protein Structure and Interactions
The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces...
Saved in:
Published in | Journal of fungi (Basel) Vol. 4; no. 4; p. 119 |
---|---|
Main Author | |
Format | Journal Article |
Language | English |
Published |
Switzerland
MDPI AG
27.10.2018
MDPI |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast
can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of
; the epithelial adhesion family of
; and the agglutinin-like sequence protein family of
are reviewed and discussed. |
---|---|
AbstractList | The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of S. cerevisiae; the epithelial adhesion family of C. glabrata; and the agglutinin-like sequence protein family of C. albicans are reviewed and discussed. The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of ; the epithelial adhesion family of ; and the agglutinin-like sequence protein family of are reviewed and discussed. The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of S. cerevisiae ; the epithelial adhesion family of C. glabrata ; and the agglutinin-like sequence protein family of C. albicans are reviewed and discussed. |
Author | Willaert, Ronnie G |
AuthorAffiliation | 2 Department Bioscience Engineering, University Antwerp, 2020 Antwerp, Belgium 1 Alliance Research Group VUB-UGent NanoMicrobiology (NAMI), IJRG VUB-EPFL NanoBiotechnology & NanoMedicine (NANO), Research Group Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; Ronnie.Willaert@vub.be or Ronnie.Willaert@uantwerpen.be ; Tel.: +32-26291846 |
AuthorAffiliation_xml | – name: 1 Alliance Research Group VUB-UGent NanoMicrobiology (NAMI), IJRG VUB-EPFL NanoBiotechnology & NanoMedicine (NANO), Research Group Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; Ronnie.Willaert@vub.be or Ronnie.Willaert@uantwerpen.be ; Tel.: +32-26291846 – name: 2 Department Bioscience Engineering, University Antwerp, 2020 Antwerp, Belgium |
Author_xml | – sequence: 1 givenname: Ronnie G surname: Willaert fullname: Willaert, Ronnie G email: Ronnie.Willaert@vub.be, Ronnie.Willaert@vub.be organization: Department Bioscience Engineering, University Antwerp, 2020 Antwerp, Belgium. Ronnie.Willaert@vub.be |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30373267$$D View this record in MEDLINE/PubMed |
BookMark | eNpdkV1rFTEQhoNUbK298QfIgjciHJ1k8umFUErVAwUFFfQqZJNsu4c9SZtkBf99t55aW69mmHl4GOZ9SvZSTpGQ5xTeIBp4u8kDBw6UmkfkgCGYlQT9Y-9ev0-Oat0AABVaGoNPyD4CKmRSHRB5HC5iHVPt8tD9jK62-q77UnKLY-q-tjL7NpfYuRS6dWqxON_GnOoz8nhwU41Ht_WQfP9w-u3k0-rs88f1yfHZynPF2soL6TUOmkIvxGACF2pgAZVE7xwdlkZxTg2E4NA4Ay5QCD0gR9n3FAMekvXOG7Lb2Msybl35bbMb7Z9BLufWlTb6KVqqJae9QAo8cBaNkUp4xaVxLKoIbnG937ku534bg4-pFTc9kD7cpPHCnudfViJoI2ARvLoVlHw1x9rsdqw-TpNLMc_VMsoUNdoosaAv_0M3eS5peZVlQjMNFPGGer2jfMm1ljjcHUPB3qRr_6W7wC_un3-H_s0SrwHBKJ9k |
CitedBy_id | crossref_primary_10_3389_ffunb_2021_718557 crossref_primary_10_1016_j_jtemb_2024_127402 crossref_primary_10_1038_s41579_022_00796_9 crossref_primary_10_4239_wjd_v13_i10_809 crossref_primary_10_3390_ijms25052496 crossref_primary_10_3390_pathogens10081013 crossref_primary_10_4155_fmc_2020_0052 crossref_primary_10_1093_genetics_iyad024 crossref_primary_10_3390_microorganisms9030654 crossref_primary_10_1128_mSphere_00191_19 crossref_primary_10_1134_S0006297923010133 crossref_primary_10_1186_s12866_021_02235_w crossref_primary_10_3390_pathogens8020053 crossref_primary_10_1007_s00253_021_11187_0 crossref_primary_10_3390_jof9070737 crossref_primary_10_1007_s42770_023_00943_1 crossref_primary_10_1017_exp_2020_49 crossref_primary_10_1371_journal_ppat_1012076 crossref_primary_10_1134_S0026893319060062 crossref_primary_10_3389_fmicb_2020_544480 crossref_primary_10_3390_fermentation6010020 crossref_primary_10_1007_s12223_020_00840_2 crossref_primary_10_1007_s40588_023_00191_9 crossref_primary_10_1093_femsyr_foab059 crossref_primary_10_1139_cjm_2022_0195 crossref_primary_10_2217_fmb_2020_0059 crossref_primary_10_1021_acsinfecdis_9b00450 crossref_primary_10_1039_D0MD00224K crossref_primary_10_3390_fermentation7030127 crossref_primary_10_3390_jof8040365 crossref_primary_10_3390_jof8121293 crossref_primary_10_3389_fmolb_2022_926959 crossref_primary_10_3390_pr9091628 crossref_primary_10_1016_j_micpath_2020_103969 crossref_primary_10_1080_21505594_2020_1836902 crossref_primary_10_1007_s42770_022_00739_9 crossref_primary_10_3390_jof7090739 crossref_primary_10_1016_j_heliyon_2022_e10850 crossref_primary_10_1016_j_jare_2022_12_013 crossref_primary_10_3390_microorganisms11061395 crossref_primary_10_1038_s41467_022_30087_z crossref_primary_10_1002_prot_26689 crossref_primary_10_1111_apm_13412 crossref_primary_10_1080_26415275_2020_1829489 crossref_primary_10_3390_jof7060453 crossref_primary_10_3390_pathogens10111509 crossref_primary_10_3390_ijms241411359 crossref_primary_10_3389_fcimb_2021_660048 crossref_primary_10_2147_IDR_S383785 crossref_primary_10_3390_foods10071652 crossref_primary_10_1128_MCB_00044_21 crossref_primary_10_3390_pathogens10111397 crossref_primary_10_31857_S0320972523010098 |
Cites_doi | 10.1093/glycob/cwq066 10.1128/CMR.00029-06 10.1093/mmy/myy054 10.1128/MMBR.00035-17 10.1016/j.ejim.2016.06.029 10.1074/jbc.M114.547877 10.1111/j.1574-695X.2012.00943.x 10.1083/jcb.140.3.461 10.1002/yea.320111102 10.1038/nature08064 10.1371/journal.pone.0064636 10.1016/j.bbagen.2017.07.020 10.1159/000060354 10.1093/nar/gkv1344 10.1093/glycob/cwu075 10.1099/00221287-133-3-637 10.1083/jcb.201103129 10.1093/cid/ciw691 10.1111/j.1600-0714.2007.00565.x 10.1016/j.fgb.2007.08.002 10.1099/00221287-35-1-61 10.1128/CMR.00029-17 10.1128/EC.00103-10 10.1073/pnas.1013893107 10.1074/jbc.M115.655654 10.1128/MMBR.00037-06 10.1371/journal.ppat.1000713 10.1371/journal.ppat.0020063 10.1016/j.micpath.2014.03.003 10.1128/EC.00245-09 10.1074/jbc.M406005200 10.1126/science.1222236 10.1371/journal.pone.0192260 10.1016/j.ijid.2017.08.017 10.1016/j.tim.2004.11.007 10.1007/s11046-013-9684-6 10.1073/pnas.240345197 10.1097/PAP.0000000000000016 10.1126/science.283.5407.1535 10.1074/jbc.M401929200 10.1016/0962-8924(94)90003-5 10.1128/mBio.00584-16 10.1007/s10529-010-0352-3 10.1016/j.mycmed.2018.06.007 10.1099/mic.0.033530-0 10.1093/molbev/msp170 10.1080/13693780701218689 10.1021/nn506370f 10.1128/IAI.72.4.2029-2034.2004 10.1074/jbc.M706252200 10.1111/j.1365-2958.2011.07676.x 10.1111/j.1574-6976.2011.00275.x 10.1099/mic.0.26943-0 10.1099/mic.0.2007/013789-0 10.1111/j.1365-2672.2007.03325.x 10.1128/IAI.02284-14 10.1016/j.it.2016.04.003 10.1371/journal.pone.0017632 10.1128/IAI.68.4.1997-2002.2000 10.1128/EC.00185-10 10.1128/MCB.9.8.3155 10.1107/S0907444911054898 10.1007/s00424-007-0212-8 10.1002/yea.1111 10.1016/j.micinf.2011.06.009 10.1371/journal.pone.0016218 10.1111/febs.12102 10.1111/j.1462-5822.2009.01394.x 10.1039/c3ay40473k 10.1038/nrmicro.2017.107 10.1111/j.1742-4658.2006.05238.x 10.1534/genetics.108.100073 10.1371/journal.pone.0144639 10.1002/1097-0061(200101)18:1<49::AID-YEA646>3.0.CO;2-M 10.1111/j.1365-2958.2008.06184.x 10.1016/j.idc.2015.10.013 10.1007/s12104-010-9243-8 10.1002/j.1460-2075.1991.tb04984.x 10.1128/EC.00364-12 10.1128/EC.00284-06 10.1128/CMR.00119-16 10.1016/j.str.2017.10.004 10.1073/pnas.1207653109 10.1016/j.micpath.2018.09.014 10.1016/S0140-6736(12)61729-2 10.1128/jb.178.24.7144-7151.1996 10.1099/mic.0.26431-0 10.1128/AEM.58.11.3709-3714.1992 10.1128/MCB.11.8.4196 10.1038/ijo.2012.62 10.1073/pnas.1103496108 10.1016/j.sbi.2004.08.006 10.1111/j.1567-1364.2008.00462.x 10.1016/j.micres.2009.03.006 10.1128/jb.179.15.4929-4936.1997 10.1099/00221287-96-1-165 10.1128/IAI.68.6.3172-3179.2000 10.1091/mbc.5.9.1003 10.1086/587658 10.1073/pnas.151111298 10.1128/microbiolspec.MB-0005-2014 10.1016/S1473-3099(10)70218-8 10.1016/j.ijmm.2014.07.004 10.1080/13693780701435317 10.3389/fmicb.2016.00280 10.1371/journal.ppat.1000226 10.1111/j.1574-6968.1995.tb07953.x 10.1006/jmbi.1998.2238 10.1111/mmi.13002 10.1186/1471-2180-11-106 10.1101/gad.8.24.2974 10.1371/journal.pone.0105017 10.1093/emboj/18.5.1257 10.1271/bbb.70.660 10.1128/mSphere.00129-16 10.1002/(SICI)1097-4644(19960616)61:4<562::AID-JCB9>3.0.CO;2-M 10.1038/sj.embor.7400145 10.1111/j.1574-695X.1998.tb01111.x 10.1128/EC.00279-10 10.1016/j.str.2015.03.021 10.1016/S0140-6736(13)60937-X 10.1128/JB.150.2.878-889.1982 10.1002/j.1460-2075.1994.tb06799.x 10.1126/science.291.5505.878 10.1111/j.1574-6968.2004.tb09726.x 10.1073/pnas.1013210108 10.1111/j.1567-1364.2006.00189.x 10.1086/506452 10.1128/EC.00309-07 10.1053/jhin.2001.1151 10.1073/pnas.93.16.8419 10.1016/j.cub.2008.06.034 10.1107/S1744309111003460 10.1111/cmi.12091 10.1016/j.tim.2011.10.002 10.1016/j.femsyr.2005.05.004 10.1002/yea.320090509 10.1073/pnas.220420397 10.1111/j.1567-1364.2011.00766.x 10.1093/jac/dkp242 10.1128/EC.00340-06 10.1111/j.1348-0421.2008.00083.x 10.1128/IAI.72.10.6023-6031.2004 10.1128/mBio.00427-15 10.1091/mbc.9.1.161 10.1016/0092-8674(92)90079-R 10.1128/AEM.71.6.2934-2939.2005 10.1128/EC.00310-06 10.1111/j.1439-0507.2010.01862.x 10.1128/IAI.61.5.1940-1949.1993 10.1016/S0092-8674(03)00809-2 10.3390/fermentation2040018 |
ContentType | Journal Article |
Copyright | 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2018 by the authors. 2018 |
Copyright_xml | – notice: 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2018 by the authors. 2018 |
DBID | NPM AAYXX CITATION 8FE 8FH ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO GNUQQ HCIFZ LK8 M7P PIMPY PQEST PQQKQ PQUKI PRINS 7X8 5PM DOA |
DOI | 10.3390/jof4040119 |
DatabaseName | PubMed CrossRef ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Central (Alumni) ProQuest Central ProQuest Central Essentials Biological Science Collection AUTh Library subscriptions: ProQuest Central Natural Science Collection ProQuest One Community College ProQuest Central Korea ProQuest Central Student SciTech Premium Collection (Proquest) (PQ_SDU_P3) Biological Sciences Biological Science Database Publicly Available Content Database ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic PubMed Central (Full Participant titles) Directory of Open Access Journals |
DatabaseTitle | PubMed CrossRef Publicly Available Content Database ProQuest Central Student ProQuest Biological Science Collection ProQuest Central Essentials ProQuest One Academic Eastern Edition ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection Biological Science Database ProQuest SciTech Collection ProQuest Central China ProQuest Central ProQuest One Academic UKI Edition Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest One Academic MEDLINE - Academic |
DatabaseTitleList | Publicly Available Content Database PubMed CrossRef |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 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: 3 dbid: BENPR name: AUTh Library subscriptions: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Botany |
EISSN | 2309-608X |
ExternalDocumentID | oai_doaj_org_article_18641b53104d42e99675c7469a2e7e0a 10_3390_jof4040119 30373267 |
Genre | Journal Article Review |
GrantInformation_xml | – fundername: Federaal Wetenschapsbeleid grantid: ESA grant |
GroupedDBID | 53G 5VS 8FE 8FH AADQD AAFWJ AAHBH ADBBV AFKRA AFPKN AFZYC ALMA_UNASSIGNED_HOLDINGS AOIJS BBNVY BCNDV BENPR BHPHI CCPQU GROUPED_DOAJ HCIFZ HYE IAO KQ8 LK8 M7P MODMG M~E NPM OK1 OZF PGMZT PIMPY PROAC RPM AAYXX CITATION ABUWG AZQEC DWQXO GNUQQ PQEST PQQKQ PQUKI PRINS 7X8 5PM |
ID | FETCH-LOGICAL-c472t-c56c83f810b55f9d457f2d3763caa1f376744190dda39a90ad10db03436bb13d3 |
IEDL.DBID | RPM |
ISSN | 2309-608X |
IngestDate | Fri Oct 04 13:11:13 EDT 2024 Tue Sep 17 21:16:21 EDT 2024 Fri Aug 16 01:00:51 EDT 2024 Fri Sep 13 08:00:36 EDT 2024 Fri Aug 23 02:57:10 EDT 2024 Sat Sep 28 08:33:25 EDT 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 4 |
Keywords | Als proteins Candida albicans the epithelial adhesion family the agglutinin-like sequence protein family yeast adhesions the flocculation protein family Candida glabrata Epa proteins Flo proteins Saccharomyces cerevisiae |
Language | English |
License | Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c472t-c56c83f810b55f9d457f2d3763caa1f376744190dda39a90ad10db03436bb13d3 |
Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ORCID | 0000-0002-5400-7019 |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6308950/ |
PMID | 30373267 |
PQID | 2582801335 |
PQPubID | 2059559 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_18641b53104d42e99675c7469a2e7e0a pubmedcentral_primary_oai_pubmedcentral_nih_gov_6308950 proquest_miscellaneous_2127198975 proquest_journals_2582801335 crossref_primary_10_3390_jof4040119 pubmed_primary_30373267 |
PublicationCentury | 2000 |
PublicationDate | 20181027 |
PublicationDateYYYYMMDD | 2018-10-27 |
PublicationDate_xml | – month: 10 year: 2018 text: 20181027 day: 27 |
PublicationDecade | 2010 |
PublicationPlace | Switzerland |
PublicationPlace_xml | – name: Switzerland – name: Basel |
PublicationTitle | Journal of fungi (Basel) |
PublicationTitleAlternate | J Fungi (Basel) |
PublicationYear | 2018 |
Publisher | MDPI AG MDPI |
Publisher_xml | – name: MDPI AG – name: MDPI |
References | ref57 ref56 ref59 ref58 ref53 ref52 ref55 ref54 ref51 ref50 ref46 ref45 ref48 ref47 ref42 ref41 ref44 ref43 ref49 ref8 ref7 ref9 ref4 ref3 ref6 ref5 ref100 ref101 ref40 ref35 ref34 ref37 ref36 ref31 ref148 ref30 ref149 ref33 ref146 ref32 ref147 ref39 ref38 Miki (ref120) 1982; 150 ref151 ref152 ref150 ref24 ref23 ref26 ref25 ref20 ref22 ref21 ref28 ref27 ref29 ref13 ref12 ref15 ref128 ref14 ref129 ref97 ref126 ref96 ref127 ref11 ref99 ref124 ref10 ref98 ref125 ref17 ref16 ref19 ref18 ref93 Hoffman (ref130) 1993; 61 ref133 ref92 ref134 ref95 ref131 ref94 ref132 ref91 ref90 ref89 ref139 ref86 ref137 ref85 ref138 ref88 ref135 ref87 ref136 ref82 ref144 ref81 ref145 ref84 ref142 ref83 ref143 ref140 ref141 ref80 ref79 ref108 ref78 ref109 ref106 ref107 ref75 ref104 ref74 ref105 ref102 Mösch (ref67) 2000; 5 ref76 ref103 ref2 ref1 ref71 ref111 ref70 ref112 ref73 ref72 ref110 ref68 ref119 ref117 ref69 ref118 ref64 ref115 ref63 ref116 ref66 ref113 ref65 ref114 Smit (ref77) 1992; 58 ref60 ref122 ref123 ref62 ref61 ref121 |
References_xml | – ident: ref129 doi: 10.1093/glycob/cwq066 – ident: ref23 doi: 10.1128/CMR.00029-06 – ident: ref49 doi: 10.1093/mmy/myy054 – ident: ref134 doi: 10.1128/MMBR.00035-17 – ident: ref22 doi: 10.1016/j.ejim.2016.06.029 – ident: ref62 doi: 10.1074/jbc.M114.547877 – ident: ref30 doi: 10.1111/j.1574-695X.2012.00943.x – ident: ref36 doi: 10.1083/jcb.140.3.461 – ident: ref1 doi: 10.1002/yea.320111102 – ident: ref102 doi: 10.1038/nature08064 – ident: ref17 doi: 10.1371/journal.pone.0064636 – ident: ref151 doi: 10.1016/j.bbagen.2017.07.020 – volume: 5 start-page: 185 year: 2000 ident: ref67 article-title: Pseudohyphal Development of Saccharomyces cerevisiae publication-title: Contrib. Microbiol. doi: 10.1159/000060354 contributor: fullname: Mösch – ident: ref37 doi: 10.1093/nar/gkv1344 – ident: ref55 doi: 10.1093/glycob/cwu075 – ident: ref4 doi: 10.1099/00221287-133-3-637 – ident: ref125 doi: 10.1083/jcb.201103129 – ident: ref46 doi: 10.1093/cid/ciw691 – ident: ref109 doi: 10.1111/j.1600-0714.2007.00565.x – ident: ref42 doi: 10.1016/j.fgb.2007.08.002 – ident: ref118 doi: 10.1099/00221287-35-1-61 – ident: ref61 doi: 10.1128/CMR.00029-17 – ident: ref106 doi: 10.1128/EC.00103-10 – ident: ref92 doi: 10.1073/pnas.1013893107 – ident: ref52 doi: 10.1074/jbc.M115.655654 – ident: ref144 doi: 10.1128/MMBR.00037-06 – ident: ref12 doi: 10.1371/journal.ppat.1000713 – ident: ref104 doi: 10.1371/journal.ppat.0020063 – ident: ref108 doi: 10.1016/j.micpath.2014.03.003 – ident: ref105 doi: 10.1128/EC.00245-09 – ident: ref96 doi: 10.1074/jbc.M406005200 – ident: ref11 doi: 10.1126/science.1222236 – ident: ref100 doi: 10.1371/journal.pone.0192260 – ident: ref47 doi: 10.1016/j.ijid.2017.08.017 – ident: ref143 doi: 10.1016/j.tim.2004.11.007 – ident: ref99 doi: 10.1007/s11046-013-9684-6 – ident: ref8 doi: 10.1073/pnas.240345197 – ident: ref21 doi: 10.1097/PAP.0000000000000016 – ident: ref94 doi: 10.1126/science.283.5407.1535 – ident: ref88 doi: 10.1074/jbc.M401929200 – ident: ref133 doi: 10.1016/0962-8924(94)90003-5 – ident: ref112 doi: 10.1128/mBio.00584-16 – ident: ref38 doi: 10.1007/s10529-010-0352-3 – ident: ref45 doi: 10.1016/j.mycmed.2018.06.007 – ident: ref139 doi: 10.1099/mic.0.033530-0 – ident: ref117 doi: 10.1093/molbev/msp170 – ident: ref27 doi: 10.1080/13693780701218689 – ident: ref123 doi: 10.1021/nn506370f – ident: ref126 doi: 10.1128/IAI.72.4.2029-2034.2004 – ident: ref85 doi: 10.1074/jbc.M706252200 – ident: ref111 doi: 10.1111/j.1365-2958.2011.07676.x – ident: ref6 doi: 10.1111/j.1574-6976.2011.00275.x – ident: ref90 doi: 10.1099/mic.0.26943-0 – ident: ref145 doi: 10.1099/mic.0.2007/013789-0 – ident: ref72 doi: 10.1111/j.1365-2672.2007.03325.x – ident: ref140 doi: 10.1128/IAI.02284-14 – ident: ref15 doi: 10.1016/j.it.2016.04.003 – ident: ref132 doi: 10.1371/journal.pone.0017632 – ident: ref95 doi: 10.1128/IAI.68.4.1997-2002.2000 – ident: ref110 doi: 10.1128/EC.00185-10 – ident: ref32 doi: 10.1128/MCB.9.8.3155 – ident: ref43 doi: 10.1107/S0907444911054898 – ident: ref3 doi: 10.1007/s00424-007-0212-8 – ident: ref89 doi: 10.1002/yea.1111 – ident: ref98 doi: 10.1016/j.micinf.2011.06.009 – ident: ref107 doi: 10.1371/journal.pone.0016218 – ident: ref54 doi: 10.1111/febs.12102 – ident: ref97 doi: 10.1111/j.1462-5822.2009.01394.x – ident: ref122 doi: 10.1039/c3ay40473k – ident: ref142 doi: 10.1038/nrmicro.2017.107 – ident: ref41 doi: 10.1111/j.1742-4658.2006.05238.x – ident: ref31 doi: 10.1534/genetics.108.100073 – ident: ref14 doi: 10.1371/journal.pone.0144639 – ident: ref51 doi: 10.1002/1097-0061(200101)18:1<49::AID-YEA646>3.0.CO;2-M – ident: ref150 doi: 10.1111/j.1365-2958.2008.06184.x – ident: ref24 doi: 10.1016/j.idc.2015.10.013 – ident: ref82 doi: 10.1007/s12104-010-9243-8 – ident: ref33 doi: 10.1002/j.1460-2075.1991.tb04984.x – ident: ref2 doi: 10.1128/EC.00364-12 – ident: ref75 doi: 10.1128/EC.00284-06 – ident: ref19 doi: 10.1128/CMR.00119-16 – ident: ref152 doi: 10.1016/j.str.2017.10.004 – ident: ref44 doi: 10.1073/pnas.1207653109 – ident: ref48 doi: 10.1016/j.micpath.2018.09.014 – ident: ref10 doi: 10.1016/S0140-6736(12)61729-2 – ident: ref40 doi: 10.1128/jb.178.24.7144-7151.1996 – ident: ref124 doi: 10.1099/mic.0.26431-0 – volume: 58 start-page: 3709 year: 1992 ident: ref77 article-title: Flocculence of Saccharomyces cerevisiae cells is induced by nutrient limitation, with cell surface hydrophobicity as a major determinant publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.58.11.3709-3714.1992 contributor: fullname: Smit – ident: ref35 doi: 10.1128/MCB.11.8.4196 – ident: ref20 doi: 10.1038/ijo.2012.62 – ident: ref63 doi: 10.1073/pnas.1103496108 – ident: ref116 doi: 10.1016/j.sbi.2004.08.006 – ident: ref60 doi: 10.1111/j.1567-1364.2008.00462.x – ident: ref101 doi: 10.1016/j.micres.2009.03.006 – ident: ref113 doi: 10.1128/jb.179.15.4929-4936.1997 – ident: ref119 doi: 10.1099/00221287-96-1-165 – ident: ref131 doi: 10.1128/IAI.68.6.3172-3179.2000 – ident: ref66 doi: 10.1091/mbc.5.9.1003 – ident: ref16 doi: 10.1086/587658 – ident: ref115 doi: 10.1073/pnas.151111298 – ident: ref149 doi: 10.1128/microbiolspec.MB-0005-2014 – ident: ref26 doi: 10.1016/S1473-3099(10)70218-8 – ident: ref148 doi: 10.1016/j.ijmm.2014.07.004 – ident: ref87 doi: 10.1080/13693780701435317 – ident: ref135 doi: 10.3389/fmicb.2016.00280 – ident: ref86 doi: 10.1371/journal.ppat.1000226 – ident: ref79 doi: 10.1111/j.1574-6968.1995.tb07953.x – ident: ref81 doi: 10.1006/jmbi.1998.2238 – ident: ref141 doi: 10.1111/mmi.13002 – ident: ref147 doi: 10.1186/1471-2180-11-106 – ident: ref59 doi: 10.1101/gad.8.24.2974 – ident: ref18 doi: 10.1371/journal.pone.0105017 – ident: ref58 doi: 10.1093/emboj/18.5.1257 – ident: ref71 doi: 10.1271/bbb.70.660 – ident: ref80 doi: 10.1128/mSphere.00129-16 – ident: ref114 doi: 10.1002/(SICI)1097-4644(19960616)61:4<562::AID-JCB9>3.0.CO;2-M – ident: ref9 doi: 10.1038/sj.embor.7400145 – ident: ref5 doi: 10.1111/j.1574-695X.1998.tb01111.x – ident: ref128 doi: 10.1128/EC.00279-10 – ident: ref64 doi: 10.1016/j.str.2015.03.021 – ident: ref13 doi: 10.1016/S0140-6736(13)60937-X – volume: 150 start-page: 878 year: 1982 ident: ref120 article-title: Possible Mechanism for Flocculation Interactions Governed by Gene FLO1 in Saccharomyces cerevisiae publication-title: J. Bacteriol. doi: 10.1128/JB.150.2.878-889.1982 contributor: fullname: Miki – ident: ref34 doi: 10.1002/j.1460-2075.1994.tb06799.x – ident: ref68 doi: 10.1126/science.291.5505.878 – ident: ref65 doi: 10.1111/j.1574-6968.2004.tb09726.x – ident: ref53 doi: 10.1073/pnas.1013210108 – ident: ref74 doi: 10.1111/j.1567-1364.2006.00189.x – ident: ref137 doi: 10.1086/506452 – ident: ref91 doi: 10.1128/EC.00309-07 – ident: ref25 doi: 10.1053/jhin.2001.1151 – ident: ref56 doi: 10.1073/pnas.93.16.8419 – ident: ref103 doi: 10.1016/j.cub.2008.06.034 – ident: ref83 doi: 10.1107/S1744309111003460 – ident: ref28 doi: 10.1111/cmi.12091 – ident: ref93 doi: 10.1016/j.tim.2011.10.002 – ident: ref73 doi: 10.1016/j.femsyr.2005.05.004 – ident: ref78 doi: 10.1002/yea.320090509 – ident: ref29 doi: 10.1073/pnas.220420397 – ident: ref76 doi: 10.1111/j.1567-1364.2011.00766.x – ident: ref138 doi: 10.1093/jac/dkp242 – ident: ref127 doi: 10.1128/EC.00340-06 – ident: ref50 doi: 10.1111/j.1348-0421.2008.00083.x – ident: ref136 doi: 10.1128/IAI.72.10.6023-6031.2004 – ident: ref39 doi: 10.1128/mBio.00427-15 – ident: ref57 doi: 10.1091/mbc.9.1.161 – ident: ref7 doi: 10.1016/0092-8674(92)90079-R – ident: ref70 doi: 10.1128/AEM.71.6.2934-2939.2005 – ident: ref69 doi: 10.1128/EC.00310-06 – ident: ref146 doi: 10.1111/j.1439-0507.2010.01862.x – volume: 61 start-page: 1940 year: 1993 ident: ref130 article-title: Analysis of Candida albicans Adhesion to Salivary Mucin publication-title: Infect. Immun. doi: 10.1128/IAI.61.5.1940-1949.1993 contributor: fullname: Hoffman – ident: ref84 doi: 10.1016/S0092-8674(03)00809-2 – ident: ref121 doi: 10.3390/fermentation2040018 |
SSID | ssj0001586993 |
Score | 2.3541222 |
SecondaryResourceType | review_article |
Snippet | The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast
can switch from a unicellular lifestyle to a... The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a... The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a... |
SourceID | doaj pubmedcentral proquest crossref pubmed |
SourceType | Open Website Open Access Repository Aggregation Database Index Database |
StartPage | 119 |
SubjectTerms | Adhesins Als proteins Amino acid sequence Candida albicans Candida glabrata Candidiasis Carbohydrates Cell adhesion & migration Cell walls Epa proteins Flo proteins Flocculation Fungal infections Glycoproteins Lectins Nutrients Protein families Protein structure Proteins Review Saccharomyces cerevisiae Self-recognition the agglutinin-like sequence protein family the epithelial adhesion family the flocculation protein family Yeast yeast adhesions |
SummonAdditionalLinks | – databaseName: Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1LS8QwEA4iHryIb-uLil6LeT-8qSgiKIIKeipJk6AeWnHXg__eSbOuuyJ48dhmDtOZaeebZuYLQgeN4c44HirKHK54tLbSOoRKR4yjxI0wIg0KX13Li3t--SAeJo76Sj1hmR44G-6QaMmJg0jB3HMaAJ4r0Sgo6iwNKuAMjYiYKKbyfLCWkHkzHymDuv7wpYscApYkSp2JDNQT9f-GLn82SU5knfNFtDCCi-VxVnMJzYR2Gc2ddADpPlaQPPZPAYr9QdnF8jGdwjM4Km8S88JzW972zLDvb6G0rS_7P395iGGwiu7Pz-5OL6rRQQhVwxUdVo2QjWZRE-yEiMZzoSL16dPQWEtiImQBVGOw95YZa7D1BHuHGWfSOcI8W0OzbdeGDVQaK7VPrOssBu69gQsNlSkABxUNla5A-1_GqV8z30UNdUIyYf1twgKdJLuNJRJHdX8DPFePPFf_5bkCbX9ZvR69OIOapm08gKVMFGhvvAwhn_YxbBu6d5AhVKVWLwUy69lJY00gIytApKpAasp9U6pOr7TPTz2ttmRYG4E3_-PZttA8IKueOJeqbTQLHg87gF6GbrcP1E-93esP priority: 102 providerName: Directory of Open Access Journals – databaseName: AUTh Library subscriptions: ProQuest Central dbid: BENPR link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELZKy4FLVd4pLQqCa7SO3-ZSdatWKySqCqhUTpGftByS0t0e-PfMJNndLkIcE_tgzXg838zY3xDyIVjhrRepYtzTSmTnKmNSqkymNCsapJX4UPjzuZpdik9X8mqLzJZvYfBa5fJM7A_q2AXMkU8Y1ncAr3A5cR6zAGExObr9VWH_KKyzjs00HpEdVgss2O5MT88vvqzzLdIo8MUDQymHSH_ys8sCtnCNJDsPfFJP3f8vvPn3tckHfuhsj-yOALI8HjT-lGyl9hl5PO0A5P1-TtRxvE4Q_s_LLpffsS_P_GN5gVwMN235teeKvb9LpWtj2ecCh2cN8xfk8uz028msGlsjVEFotqiCVMHwbGrqpcw2Cqkzi3hYBOfqjBQtgHMsjdFx6yx1sabRUy648r7mkb8k223XptektE6ZiDzsPCcRo4UPA7EqQAmdLVO-IO-XwmluBwaMBiIHFGGzFmFBpii31Qxkre5_dHc_mtEImtooUXuweiqiYAlCLS2DhgDdsaQTdQU5WEq9GU1p3qwVX5B3q2EwAqxsuDZ19zCnZhovf2mY82pQ0mol4KM1YFRdEL2hvo2lbo60N9c90bbi1FhJ9_-_rDfkCaConiSX6QOyDbpMh4BUFv7tuAn_AEL06P8 priority: 102 providerName: ProQuest |
Title | Adhesins of Yeasts: Protein Structure and Interactions |
URI | https://www.ncbi.nlm.nih.gov/pubmed/30373267 https://www.proquest.com/docview/2582801335/abstract/ https://search.proquest.com/docview/2127198975 https://pubmed.ncbi.nlm.nih.gov/PMC6308950 https://doaj.org/article/18641b53104d42e99675c7469a2e7e0a |
Volume | 4 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT9wwEB0B7aGXqvQzLaxStdewTvzdG4tAqBJo1RaJniI7tmGrkiAWDv33HTvJwqKeekzsSNbM2H4vnnkG-NxoZrVlvqioJQULxhRKeV-oQEgQpOGax0Lhk1NxfMa-nvPzDeBjLUxK2m_sYq_9fbXXLi5TbuX1VTMd88Sm85MDQYnSnEw3YVNS-oCi96XBSuCm20uRUqT0019dYBirZRklQnHJlghZ5No-lOT6_4UxH6dKPth7jl7A8wE05vv94LZhw7cv4emsQ2D35xWIfXfpkfIv8y7kP-NdPMsv-TzqLyza_HvSh7278blpXZ7-__WlDMvXcHZ0-OPguBiuQygaJqvbouGiUTSokljOg3aMy1C5uEA0xpQhyrIgttHEOUO10cS4kjhLKKPC2pI6-ga22q717yDXRigXtddp8Mw5jQ8K-SnCBxl0JWwGn0bj1Ne96kWNbCFas763ZgazaLdVj6hUnV50Nxf14K-6VIKVFmc6YY5VHumV5I1EUm4qLz0xGeyMVq-H6bOsq3iYh-CU8gw-rpox8ONphml9d4d9ykrGhC-Jfd72TlqNZHRyBnLNfWtDXW_BWEvi2kNsvf_vLz_AMwRVSTO3kjuwhW72uwhcbu0EnswOT-ffJon4T1LY_gWMqu9u |
link.rule.ids | 230,315,733,786,790,870,891,2115,21416,27957,27958,33779,33780,43840,53827,53829,74659 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB7BFoleEM8SKBAE16iO3-aCuqjVAu2qglYqp8iObdoektK0B_494yS720WIY2IfrJmx55vx-BuA97XhzjgeCsocKXi0ttA6hEJHQqIktTAiPRQ-nMvZCf9yKk7HhFs3llUuzsT-oPZtnXLkOzTd7yBeYeLj5a8idY1Kt6tjC427sMEZhioT2JjuzY--rbIsQkv0wAMvKcP4fueijRwNt0zUOrc8UU_Y_y-U-Xex5C3vs_8QHoywMd8d9PwI7oTmMdybtgjtfj8BuevPAgb9Xd7G_EfqxtN9yI8SA8N5k3_vGWJvrkJuG5_3GcDhMUP3FE72944_zYqxIUJRc0Wvi1rIWrOoS-KEiMZzoSL16YiorS1jImZBdGOI95YZa4j1JfGOMM6kcyXz7BlMmrYJzyE3Vmqf2NdZDNx7gx8aI1QEECoaKl0G7xbCqS4H3osK44UkwmolwgymSW7LGYmruv_RXv2sRtOvSi156XCvE-45DRhgKVErDMstDSoQm8H2QurVuIG6aqXuDN4uh9H0032GbUJ7g3NKqlLJl8I5W4OSlitBz6wQmaoM1Jr61pa6PtKcn_X02pIRbQR58f9lvYH7s-PDg-rg8_zrS9hEHNXT5FK1DRPUa3iFWOXavR4N8g8XJegy |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB5BixAXxLMECgTBNVrHb3NBXeiqvFYroFI5RXZs0-WQlKY98O8ZJ9ndLkIcE_tgzcPzjT3-BuBVbbgzjoeCMkcKHq0ttA6h0JGQKEktjEgPhT_P5dEx_3AiTsb6p24sq1ztif1G7ds6nZFPaLrfQbzCxCSOZRGLd7M3Z7-K1EEq3bSO7TSuw67iUqCF704P54svmxMXoSVG44GjlGGuP_nZRo5GXCaanStRqSfv_xfi_Ltw8kokmt2B2yOEzA8Gnd-Fa6G5BzemLcK83_dBHvjT0C2bLm9j_j115ule54vExrBs8q89W-zlecht4_P-NHB42NA9gOPZ4be3R8XYHKGouaIXRS1krVnUJXFCROO5UJH6tF3U1pYxkbQg0jHEe8uMNcT6knhHGGfSuZJ59hB2mrYJjyA3VmqfmNhZDNx7gx8as1UEEyoaKl0GL1fCqc4GDowKc4ckwmojwgymSW7rGYm3uv_Rnv-oRjeoSi156dDvCfecBky2lKhRXcbSoAKxGeyvpF6NztRVG9Vn8GI9jG6Q7jZsE9pLnFNSlcq_FM7ZG5S0XglGaYUoVWWgttS3tdTtkWZ52lNtS0a0EeTx_5f1HG6iLVaf3s8_PoFbCKl6xlyq9mEH1RqeImy5cM9Ge_wD_z3sbw |
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=Adhesins+of+Yeasts%3A+Protein+Structure+and+Interactions&rft.jtitle=Journal+of+fungi+%28Basel%29&rft.au=Willaert%2C+Ronnie+G&rft.date=2018-10-27&rft.eissn=2309-608X&rft.volume=4&rft.issue=4&rft_id=info:doi/10.3390%2Fjof4040119&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2309-608X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2309-608X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2309-608X&client=summon |