The proteomics of wool fibre morphogenesis

Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions of follicles that correlated with morphological changes in the developing fibre as determined by transmission electron microscopy. Individual...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of structural biology Vol. 191; no. 3; pp. 341 - 351
Main Authors:	Plowman, Jeffrey E., Harland, Duane P., Ganeshan, Sivasangary, Woods, Joy L., van Shaijik, Bede, Deb-Choudhury, Santanu, Thomas, Ancy, Clerens, Stefan, Scobie, David R.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01.09.2015
Subjects:	Animals Collagen - metabolism Desmoplakins - metabolism Epithelial Cells - metabolism Gene Expression - physiology Hair follicle Hair Follicle - metabolism Histones - metabolism Intermediate Filament Proteins - metabolism KAP Keratin Keratins - metabolism Morphogenesis - physiology Proteomics - methods Ribosomal Proteins - metabolism Sheep - metabolism Vimentin - metabolism Wool Wool - metabolism ORS Keratin Hair follicle KAP IRS Wool IF
ISSN:	1047-8477, 1095-8657, 1095-8657
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Abstract	Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions of follicles that correlated with morphological changes in the developing fibre as determined by transmission electron microscopy. Individual wool follicles were dissected into four portions designated as the bulb, elongation, keratogenous and keratinisation portions. Gel-free proteomic analysis of dissected portions from 30 follicles showed that the first keratins to appear were K31, K35 and K85, in the bulb portion. The first epithelial KAP, trichohyalin, was detected in the bulb portion and the first cortical KAP, KAP11.1 was found in the elongation portion. Other major trichocyte keratins and cortical KAPs began to appear further up the follicle in the keratogenous and keratinisation zones. These results were consistent with what has been observed from gene expression studies and correlated well with the morphological changes observed in the follicle. Other proteins detected by this approach included the keratin anchor protein desmoplakin, as well as vimentin and epithelial keratins, histones, ribosomal proteins and collagens. Two-dimensional electrophoretic (2DE) analysis of dissected portions of 50 follicles revealed substantial changes in the position, number and intensity of the spots of the trichocyte keratins as they progressed through the follicle zones, suggesting that they are subject to modification as a result of the keratinisation process. Also present in the 2DE maps were a number of epithelial keratins, presumably from the inner and outer root sheaths, and the dermal components.
AbstractList	Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions of follicles that correlated with morphological changes in the developing fibre as determined by transmission electron microscopy. Individual wool follicles were dissected into four portions designated as the bulb, elongation, keratogenous and keratinisation portions. Gel-free proteomic analysis of dissected portions from 30 follicles showed that the first keratins to appear were K31, K35 and K85, in the bulb portion. The first epithelial KAP, trichohyalin, was detected in the bulb portion and the first cortical KAP, KAP11.1 was found in the elongation portion. Other major trichocyte keratins and cortical KAPs began to appear further up the follicle in the keratogenous and keratinisation zones. These results were consistent with what has been observed from gene expression studies and correlated well with the morphological changes observed in the follicle. Other proteins detected by this approach included the keratin anchor protein desmoplakin, as well as vimentin and epithelial keratins, histones, ribosomal proteins and collagens. Two-dimensional electrophoretic (2DE) analysis of dissected portions of 50 follicles revealed substantial changes in the position, number and intensity of the spots of the trichocyte keratins as they progressed through the follicle zones, suggesting that they are subject to modification as a result of the keratinisation process. Also present in the 2DE maps were a number of epithelial keratins, presumably from the inner and outer root sheaths, and the dermal components.Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions of follicles that correlated with morphological changes in the developing fibre as determined by transmission electron microscopy. Individual wool follicles were dissected into four portions designated as the bulb, elongation, keratogenous and keratinisation portions. Gel-free proteomic analysis of dissected portions from 30 follicles showed that the first keratins to appear were K31, K35 and K85, in the bulb portion. The first epithelial KAP, trichohyalin, was detected in the bulb portion and the first cortical KAP, KAP11.1 was found in the elongation portion. Other major trichocyte keratins and cortical KAPs began to appear further up the follicle in the keratogenous and keratinisation zones. These results were consistent with what has been observed from gene expression studies and correlated well with the morphological changes observed in the follicle. Other proteins detected by this approach included the keratin anchor protein desmoplakin, as well as vimentin and epithelial keratins, histones, ribosomal proteins and collagens. Two-dimensional electrophoretic (2DE) analysis of dissected portions of 50 follicles revealed substantial changes in the position, number and intensity of the spots of the trichocyte keratins as they progressed through the follicle zones, suggesting that they are subject to modification as a result of the keratinisation process. Also present in the 2DE maps were a number of epithelial keratins, presumably from the inner and outer root sheaths, and the dermal components. Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions of follicles that correlated with morphological changes in the developing fibre as determined by transmission electron microscopy. Individual wool follicles were dissected into four portions designated as the bulb, elongation, keratogenous and keratinisation portions. Gel-free proteomic analysis of dissected portions from 30 follicles showed that the first keratins to appear were K31, K35 and K85, in the bulb portion. The first epithelial KAP, trichohyalin, was detected in the bulb portion and the first cortical KAP, KAP11.1 was found in the elongation portion. Other major trichocyte keratins and cortical KAPs began to appear further up the follicle in the keratogenous and keratinisation zones. These results were consistent with what has been observed from gene expression studies and correlated well with the morphological changes observed in the follicle. Other proteins detected by this approach included the keratin anchor protein desmoplakin, as well as vimentin and epithelial keratins, histones, ribosomal proteins and collagens. Two-dimensional electrophoretic (2DE) analysis of dissected portions of 50 follicles revealed substantial changes in the position, number and intensity of the spots of the trichocyte keratins as they progressed through the follicle zones, suggesting that they are subject to modification as a result of the keratinisation process. Also present in the 2DE maps were a number of epithelial keratins, presumably from the inner and outer root sheaths, and the dermal components.
Author	Scobie, David R. Woods, Joy L. Harland, Duane P. Plowman, Jeffrey E. Clerens, Stefan Ganeshan, Sivasangary van Shaijik, Bede Deb-Choudhury, Santanu Thomas, Ancy
Author_xml	– sequence: 1 givenname: Jeffrey E. surname: Plowman fullname: Plowman, Jeffrey E. email: jeff.plowman@agresearch.co.nz – sequence: 2 givenname: Duane P. surname: Harland fullname: Harland, Duane P. – sequence: 3 givenname: Sivasangary surname: Ganeshan fullname: Ganeshan, Sivasangary – sequence: 4 givenname: Joy L. surname: Woods fullname: Woods, Joy L. – sequence: 5 givenname: Bede surname: van Shaijik fullname: van Shaijik, Bede – sequence: 6 givenname: Santanu surname: Deb-Choudhury fullname: Deb-Choudhury, Santanu – sequence: 7 givenname: Ancy surname: Thomas fullname: Thomas, Ancy – sequence: 8 givenname: Stefan surname: Clerens fullname: Clerens, Stefan – sequence: 9 givenname: David R. surname: Scobie fullname: Scobie, David R.
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/26208467$$D View this record in MEDLINE/PubMed
BookMark	eNp9kD1PwzAQhi0EouXjB7CgjAip4WzHdiomhPiSkFhgthz7TF0lcbFTEP-eVC0LA8vdDe9zunuOyH4feyTkjEJJgcqrZbnMTcmAihJUCSD2yJTCXMxqKdT-Zq7UrK6UmpCjnJcAUFFGD8mESQZ1JdWUXL4usFilOGDsgs1F9MVXjG3hQ5Ow6GJaLeI79phDPiEH3rQZT3f9mLzd373ePs6eXx6ebm-eZ7ZifBjrHOa0kl6ymnNnpBK1VY3lgjaSIQXvZMNVzdGYyklvWcOpc14wUzvJPT8mF9u941kfa8yD7kK22Lamx7jOmiqoqVBCwBg930XXTYdOr1LoTPrWv_-NAbUN2BRzTui1DYMZQuyHZEKrKeiNSb3Uo0m9MalB6dHkSNI_5O_y_5jrLYOjns-ASWcbsLfoQkI7aBfDP_QPS4CJ2Q
CitedBy_id	crossref_primary_10_1002_elps_201600433 crossref_primary_10_1002_prca_201700048 crossref_primary_10_3390_ijms25063260 crossref_primary_10_1016_j_jid_2017_02_983 crossref_primary_10_1111_jmi_12875 crossref_primary_10_1002_2211_5463_13126 crossref_primary_10_1111_exd_14439 crossref_primary_10_1111_bjd_16148 crossref_primary_10_1007_s10735_020_09855_y crossref_primary_10_1016_j_jprot_2017_10_008 crossref_primary_10_1017_S1751731118001647 crossref_primary_10_1016_j_ab_2017_08_020 crossref_primary_10_3389_fgene_2022_993192 crossref_primary_10_1016_j_jprot_2020_103853 crossref_primary_10_1111_age_12694 crossref_primary_10_1002_pmic_201800047 crossref_primary_10_1111_ics_13081 crossref_primary_10_1186_s12864_022_08501_z crossref_primary_10_1007_s11250_021_02899_6 crossref_primary_10_1007_s11250_022_03216_5 crossref_primary_10_1016_j_zool_2019_01_002 crossref_primary_10_1007_s10142_022_00856_6 crossref_primary_10_3390_ijms242015227 crossref_primary_10_1016_j_smallrumres_2021_106408 crossref_primary_10_1016_j_bpj_2022_04_029 crossref_primary_10_1016_j_jmps_2021_104290
Cites_doi	10.1016/S0074-7696(05)43001-6 10.1016/0892-0354(91)90016-6 10.1016/j.jsb.2013.06.005 10.1016/j.cap.2005.11.022 10.1016/S0074-7696(06)51006-X 10.1111/j.1600-0625.2006.00512.x 10.4103/0974-7753.77516 10.1038/sj.jid.5700734 10.1016/S0022-5320(82)90021-1 10.1074/jbc.M103305200 10.1083/jcb.3.2.203 10.1074/jbc.M206422200 10.1016/S0074-7696(08)61266-8 10.1016/j.cub.2008.12.005 10.1016/S0022-5320(73)90029-4 10.1016/j.jsb.2005.11.013 10.1083/jcb.102.4.1419 10.1006/abio.2001.5459 10.1016/j.jprot.2009.09.017 10.1038/sj.jid.5700702 10.1242/jcs.11.1.205 10.1002/elps.201000134 10.1074/jbc.M100657200 10.1111/j.1600-0625.2011.01274.x 10.1074/jbc.274.28.19874 10.1016/j.jsb.2010.11.019 10.1016/S0022-5320(82)80044-0 10.1016/S0022-5320(64)80092-7 10.1016/j.diff.2008.10.009
ContentType	Journal Article
Copyright	2015 Elsevier Inc. Copyright © 2015 Elsevier Inc. All rights reserved.
Copyright_xml	– notice: 2015 Elsevier Inc. – notice: Copyright © 2015 Elsevier Inc. All rights reserved.
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8
DOI	10.1016/j.jsb.2015.07.005
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic
DatabaseTitleList	MEDLINE - Academic MEDLINE
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Biology
EISSN	1095-8657
EndPage	351
ExternalDocumentID	26208467 10_1016_j_jsb_2015_07_005 S1047847715300307
Genre	Research Support, Non-U.S. Gov't Journal Article
GroupedDBID	--- --K --M -DZ -~X .55 .GJ .~1 0R~ 1B1 1RT 1~. 1~5 29L 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 85S 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABFNM ABFRF ABGSF ABJNI ABMAC ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACRLP ADBBV ADEZE ADFGL ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AETEA AFFNX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AHPSJ AI. AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CAG COF CS3 DM4 DOVZS DU5 EBS EFBJH EFLBG EJD EO8 EO9 EP2 EP3 F5P FA8 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ H~9 IH2 IHE J1W K-O KOM L7B LG5 LX2 M41 MO0 MVM N9A O-L O9- OAUVE OZT P-8 P-9 PC. Q38 R2- RIG RNS ROL RPZ SBG SDF SDG SDP SES SEW SPCBC SSU SSZ T5K TWZ UKR UNMZH VH1 WH7 WUQ X7M XJT XOL XPP Y6R ZA5 ZGI ZKB ZMT ZU3 ZXP ~02 ~G- ~KM 9DU AATTM AAXKI AAYWO AAYXX ABUFD ABWVN ACLOT ACRPL ACVFH ADCNI ADNMO AEIPS AEUPX AFJKZ AFPUW AGQPQ AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP CITATION EFKBS ~HD AGCQF AGRNS BNPGV CGR CUY CVF ECM EIF NPM SSH 7X8
ID	FETCH-LOGICAL-c423t-c4909146f62833da6758c7bc351b62e10fd6b3783eaa4d6fc2b31ddf52a8d63f3
ISICitedReferencesCount	31
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000360599200009&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	1047-8477 1095-8657
IngestDate	Mon Sep 29 02:41:04 EDT 2025 Mon Jul 21 05:59:42 EDT 2025 Sat Nov 29 04:43:34 EST 2025 Tue Nov 18 21:49:48 EST 2025 Fri Feb 23 02:28:15 EST 2024
IsPeerReviewed	true
IsScholarly	true
Issue	3
Keywords	ORS Keratin Hair follicle KAP IRS Wool IF
Language	English
License	Copyright © 2015 Elsevier Inc. All rights reserved.
LinkModel	OpenURL
MergedId	FETCHMERGED-LOGICAL-c423t-c4909146f62833da6758c7bc351b62e10fd6b3783eaa4d6fc2b31ddf52a8d63f3
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
PMID	26208467
PQID	1708157550
PQPubID	23479
PageCount	11
ParticipantIDs	proquest_miscellaneous_1708157550 pubmed_primary_26208467 crossref_citationtrail_10_1016_j_jsb_2015_07_005 crossref_primary_10_1016_j_jsb_2015_07_005 elsevier_sciencedirect_doi_10_1016_j_jsb_2015_07_005
PublicationCentury	2000
PublicationDate	2015-09-01
PublicationDateYYYYMMDD	2015-09-01
PublicationDate_xml	– month: 09 year: 2015 text: 2015-09-01 day: 01
PublicationDecade	2010
PublicationPlace	United States
PublicationPlace_xml	– name: United States
PublicationTitle	Journal of structural biology
PublicationTitleAlternate	J Struct Biol
PublicationYear	2015
Publisher	Elsevier Inc
Publisher_xml	– name: Elsevier Inc
References	Birbeck, Mercer (b0005) 1957; 3 Orwin, Thomson, Flower (b0090) 1973; 45 Langbein, Rogers, Winter, Praetzel, Schweizer (b0035) 2001; 276 Marshall, Orwin, Gillespie (b0045) 1991; 4 McKinnon, Harland (b0065) 2011; 173 Deb-Choudhury, Plowman, Thomas, Krsinic, Dyer, Clerens (b0010) 2010; 31 Rogers, Langbein, Praetzel-Wunder, Winter, Schweizer (b0120) 2006; 251 McKinnon (b0055) 2006; 6 Woods, Orwin (b0145) 1980; vol. 2 Woods, Orwin (b0150) 1982; 80 Koehn, Clerens, Deb-Choudhury, Morton, Dyer, Plowman (b0020) 2009; 73 Orwin (b0075) 1979; 60 Rogers, Langbein, Winter, Ehmann, Praetzel, Schweizer (b0115) 2002; 277 Rogers, Winter, Langbein, Wollschlager, Praetzel-Wunder, Jave-Suarez, Schweizer (b0125) 2007; 127 Rogers (b0105) 2006; 15 Plowman, Bryson, Flanagan, Jordan (b0095) 2002; 300 Rothnagel, Rogers (b0135) 1986; 102 McKinnon, A.J., Harland, D.P., Woods, J.L., 2014. Relating self-assembly to protein expression in wool cortical cells. In: Tandon, S.K., Yamashita, Y. (Eds.), AgReserach Ltd., Christchurch, New Zealand. Roth, Helwig (b0130) 1964; 11 Langbein, Rogers, Winter, Praetzel, Beckhaus, Rackwitz, Schweizer (b0030) 1999; 274 Hearle (b0015) 2003; 51 Rogers, Langbein, Winter, Ehmann, Praetzel, Korn, Schweizer (b0110) 2001; 276 Yu, Gordon, Nixon, Bawden, Rogers, Wildermoth, Maqbool, Pearson (b0155) 2009; 77 Langbein, Rogers, Praetzel-Wunder, Böckler, Schirmacher, Schweizer (b0040) 2007; 127 Matsunaga, Abe, Ishii, Watanabe, Kiyoshi, Nöcker, Tsuchiya, Tsumoto (b0050) 2013; 183 McKinnon, Harland (b0060) 2010; 2 Yu, Wildermoth, Wallace, Gordon, Maqbool, MacLean, Nixon, Pearson (b0160) 2011; 20 Orwin, Thomson (b0080) 1972; 11 Schneider, Schmidt-Ullrich, Paus (b0140) 2009; 19 Langbein, Schweizer (b0025) 2005; 243 Orwin, Woods (b0085) 1982; 80 Rafik, Briki, Burghammer, Doucet (b0100) 2006; 154 Rogers (10.1016/j.jsb.2015.07.005_b0125) 2007; 127 Deb-Choudhury (10.1016/j.jsb.2015.07.005_b0010) 2010; 31 Rogers (10.1016/j.jsb.2015.07.005_b0110) 2001; 276 Woods (10.1016/j.jsb.2015.07.005_b0145) 1980; vol. 2 Koehn (10.1016/j.jsb.2015.07.005_b0020) 2009; 73 Rogers (10.1016/j.jsb.2015.07.005_b0120) 2006; 251 10.1016/j.jsb.2015.07.005_b0070 Orwin (10.1016/j.jsb.2015.07.005_b0080) 1972; 11 Rogers (10.1016/j.jsb.2015.07.005_b0115) 2002; 277 Orwin (10.1016/j.jsb.2015.07.005_b0090) 1973; 45 Langbein (10.1016/j.jsb.2015.07.005_b0030) 1999; 274 Roth (10.1016/j.jsb.2015.07.005_b0130) 1964; 11 Woods (10.1016/j.jsb.2015.07.005_b0150) 1982; 80 McKinnon (10.1016/j.jsb.2015.07.005_b0060) 2010; 2 Rogers (10.1016/j.jsb.2015.07.005_b0105) 2006; 15 Orwin (10.1016/j.jsb.2015.07.005_b0075) 1979; 60 Birbeck (10.1016/j.jsb.2015.07.005_b0005) 1957; 3 McKinnon (10.1016/j.jsb.2015.07.005_b0065) 2011; 173 McKinnon (10.1016/j.jsb.2015.07.005_b0055) 2006; 6 Langbein (10.1016/j.jsb.2015.07.005_b0025) 2005; 243 Langbein (10.1016/j.jsb.2015.07.005_b0035) 2001; 276 Matsunaga (10.1016/j.jsb.2015.07.005_b0050) 2013; 183 Orwin (10.1016/j.jsb.2015.07.005_b0085) 1982; 80 Rafik (10.1016/j.jsb.2015.07.005_b0100) 2006; 154 Rothnagel (10.1016/j.jsb.2015.07.005_b0135) 1986; 102 Plowman (10.1016/j.jsb.2015.07.005_b0095) 2002; 300 Marshall (10.1016/j.jsb.2015.07.005_b0045) 1991; 4 Yu (10.1016/j.jsb.2015.07.005_b0160) 2011; 20 Yu (10.1016/j.jsb.2015.07.005_b0155) 2009; 77 Schneider (10.1016/j.jsb.2015.07.005_b0140) 2009; 19 Langbein (10.1016/j.jsb.2015.07.005_b0040) 2007; 127 Hearle (10.1016/j.jsb.2015.07.005_b0015) 2003; 51
References_xml	– volume: 251 start-page: 209 year: 2006 end-page: 263 ident: b0120 article-title: Human hair keratin-associated proteins (KAPs) publication-title: Int. Rev. Cytol. – volume: 31 start-page: 2894 year: 2010 end-page: 2902 ident: b0010 article-title: Electrophoretic mapping of highly homologous keratins: a novel marker peptide approach publication-title: Electrophoresis – volume: 243 start-page: 1 year: 2005 end-page: 78 ident: b0025 article-title: Keratins of the human hair follicle publication-title: Int. Rev. Cytol. – volume: 127 start-page: 1532 year: 2007 end-page: 1535 ident: b0040 article-title: Novel type I hair keratins K39 and K40 are the last to be expressed in differentiation of the hair: completion of the human hair keratin catalogue publication-title: J. Invest. Dermatol. – reference: McKinnon, A.J., Harland, D.P., Woods, J.L., 2014. Relating self-assembly to protein expression in wool cortical cells. In: Tandon, S.K., Yamashita, Y. (Eds.), AgReserach Ltd., Christchurch, New Zealand. – volume: vol. 2 start-page: 141 year: 1980 end-page: 149 ident: b0145 article-title: Studies on the surface layers of the wool fibre cuticle publication-title: Fibrous Proteins: Scientific, Industrial and Medical Aspects – volume: 154 start-page: 79 year: 2006 end-page: 88 ident: b0100 article-title: In vivo formation steps of the hard α-keratin intermediate filament along a hair follicle: evidence for structural polymorphism publication-title: J. Struct. Biol. – volume: 277 start-page: 48993 year: 2002 end-page: 49002 ident: b0115 article-title: Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1 publication-title: J. Biol. Chem. – volume: 51 start-page: 95 year: 2003 end-page: 117 ident: b0015 article-title: A total model for the structural mechanics of wool publication-title: Wool Technol. Sheep Breed. – volume: 276 start-page: 19440 year: 2001 end-page: 19451 ident: b0110 article-title: Characterization of a cluster of human high/ultrahigh sulfur keratin-associated protein genes embedded in the type I keratin gene domain on chromosome 17q12-21 publication-title: J. Biol. Chem. – volume: 3 start-page: 203 year: 1957 end-page: 213 ident: b0005 article-title: The electron microscopy of the human hair follicle. Part1. Introduction and the hair cortex publication-title: J. Biophys. Biochem. Cytol. – volume: 173 start-page: 229 year: 2011 end-page: 240 ident: b0065 article-title: A concerted polymerization-mesophase separation model for formation of trichocyte intermediate filaments and macrofibril templates. 1: Relating phase separation to structural development publication-title: J. Struct. Biol. – volume: 11 start-page: 205 year: 1972 end-page: 219 ident: b0080 article-title: An ultrastructural study of the membranes of keratinizing wool follicle cells publication-title: J. Cell Sci. – volume: 127 start-page: 1197 year: 2007 end-page: 1204 ident: b0125 article-title: Characterization of human KAP24.1, a cuticular hair keratin-associated protein with unusual amino-acid composition and repeat structure publication-title: J. Invest. Dermatol. – volume: 80 start-page: 312 year: 1982 end-page: 322 ident: b0085 article-title: Number changes and development potential of wool follicle cells in the early stages of fiber differentiation publication-title: J. Ultrastruct. Res. – volume: 15 start-page: 931 year: 2006 end-page: 949 ident: b0105 article-title: Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re-discovered publication-title: Exp. Dermatol. – volume: 80 start-page: 230 year: 1982 end-page: 242 ident: b0150 article-title: The cytology of cuticle scale pattern formation in the wool follicle publication-title: J. Ultrastruct. Res. – volume: 20 start-page: 582 year: 2011 end-page: 588 ident: b0160 article-title: Annotations of sheep keratin intermediate filament genes and their patterns of expression publication-title: Exp. Dermatol. – volume: 60 start-page: 331 year: 1979 end-page: 374 ident: b0075 article-title: The cytology and cytochemistry of the wool follicle publication-title: Int. Rev. Cytol. – volume: 4 start-page: 47 year: 1991 end-page: 83 ident: b0045 article-title: Structure and biochemistry of mammalian hard keratin publication-title: Electron Microsc. Rev. – volume: 45 start-page: 15 year: 1973 end-page: 29 ident: b0090 article-title: Plasma membrane differentiations of keratinizing cells of the wool follicle (2. desmosomes) publication-title: Ultrastruct. Res. – volume: 102 start-page: 1419 year: 1986 end-page: 1429 ident: b0135 article-title: Trichohyalin, and intermediate filament-associated protein of the hair follicle publication-title: J. Cell Biol. – volume: 6 start-page: 375 year: 2006 end-page: 378 ident: b0055 article-title: The self-assembly of keratin intermediate filaments into macrofibrils: is this process mediated by a mesophase? publication-title: Curr. Appl. Phys. – volume: 19 start-page: R132 year: 2009 end-page: R142 ident: b0140 article-title: The hair follicle as a dynamic miniorgan publication-title: Curr. Biol. – volume: 183 start-page: 484 year: 2013 end-page: 494 ident: b0050 article-title: Bidirectional binding property of high glycine–tyrosine keratin-associated protein contributes to the mechanical strength and shape of hair publication-title: J. Struct. Biol. – volume: 2 start-page: 101 year: 2010 end-page: 103 ident: b0060 article-title: The role of liquid-crystalline structures in the morphogenesis of animal fibers publication-title: Int. J. Trichol. – volume: 276 start-page: 35123 year: 2001 end-page: 35132 ident: b0035 article-title: The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins publication-title: J. Biol. Chem. – volume: 77 start-page: 307 year: 2009 end-page: 316 ident: b0155 article-title: Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles publication-title: Differentiation – volume: 11 start-page: 52 year: 1964 end-page: 67 ident: b0130 article-title: The cytology of the cuticle of the cortex, the cortex, and the medulla of the mouse hair publication-title: J. Ultrastruct. Res. – volume: 274 start-page: 19874 year: 1999 end-page: 19884 ident: b0030 article-title: The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle publication-title: J. Biol. Chem. – volume: 300 start-page: 221 year: 2002 end-page: 229 ident: b0095 article-title: Problems associated with the identification of proteins in homologous families: the wool keratin family as a case study publication-title: Anal. Biochem. – volume: 73 start-page: 323 year: 2009 end-page: 330 ident: b0020 article-title: Higher sequence coverage and improved confidence in the identification of cysteine-rich proteins from the wool cuticle using combined chemical and enzymatic digestion publication-title: J. Proteomics – volume: 243 start-page: 1 year: 2005 ident: 10.1016/j.jsb.2015.07.005_b0025 article-title: Keratins of the human hair follicle publication-title: Int. Rev. Cytol. doi: 10.1016/S0074-7696(05)43001-6 – volume: 4 start-page: 47 issue: 1 year: 1991 ident: 10.1016/j.jsb.2015.07.005_b0045 article-title: Structure and biochemistry of mammalian hard keratin publication-title: Electron Microsc. Rev. doi: 10.1016/0892-0354(91)90016-6 – volume: 183 start-page: 484 issue: 3 year: 2013 ident: 10.1016/j.jsb.2015.07.005_b0050 article-title: Bidirectional binding property of high glycine–tyrosine keratin-associated protein contributes to the mechanical strength and shape of hair publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2013.06.005 – volume: 6 start-page: 375 year: 2006 ident: 10.1016/j.jsb.2015.07.005_b0055 article-title: The self-assembly of keratin intermediate filaments into macrofibrils: is this process mediated by a mesophase? publication-title: Curr. Appl. Phys. doi: 10.1016/j.cap.2005.11.022 – volume: 251 start-page: 209 year: 2006 ident: 10.1016/j.jsb.2015.07.005_b0120 article-title: Human hair keratin-associated proteins (KAPs) publication-title: Int. Rev. Cytol. doi: 10.1016/S0074-7696(06)51006-X – volume: 15 start-page: 931 issue: 12 year: 2006 ident: 10.1016/j.jsb.2015.07.005_b0105 article-title: Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re-discovered publication-title: Exp. Dermatol. doi: 10.1111/j.1600-0625.2006.00512.x – volume: 2 start-page: 101 issue: 2 year: 2010 ident: 10.1016/j.jsb.2015.07.005_b0060 article-title: The role of liquid-crystalline structures in the morphogenesis of animal fibers publication-title: Int. J. Trichol. doi: 10.4103/0974-7753.77516 – volume: 127 start-page: 1532 year: 2007 ident: 10.1016/j.jsb.2015.07.005_b0040 article-title: Novel type I hair keratins K39 and K40 are the last to be expressed in differentiation of the hair: completion of the human hair keratin catalogue publication-title: J. Invest. Dermatol. doi: 10.1038/sj.jid.5700734 – volume: 80 start-page: 230 issue: 2 year: 1982 ident: 10.1016/j.jsb.2015.07.005_b0150 article-title: The cytology of cuticle scale pattern formation in the wool follicle publication-title: J. Ultrastruct. Res. doi: 10.1016/S0022-5320(82)90021-1 – volume: 276 start-page: 35123 issue: 37 year: 2001 ident: 10.1016/j.jsb.2015.07.005_b0035 article-title: The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins publication-title: J. Biol. Chem. doi: 10.1074/jbc.M103305200 – volume: 3 start-page: 203 year: 1957 ident: 10.1016/j.jsb.2015.07.005_b0005 article-title: The electron microscopy of the human hair follicle. Part1. Introduction and the hair cortex publication-title: J. Biophys. Biochem. Cytol. doi: 10.1083/jcb.3.2.203 – volume: 277 start-page: 48993 issue: 50 year: 2002 ident: 10.1016/j.jsb.2015.07.005_b0115 article-title: Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M206422200 – volume: 60 start-page: 331 year: 1979 ident: 10.1016/j.jsb.2015.07.005_b0075 article-title: The cytology and cytochemistry of the wool follicle publication-title: Int. Rev. Cytol. doi: 10.1016/S0074-7696(08)61266-8 – volume: 19 start-page: R132 issue: 3 year: 2009 ident: 10.1016/j.jsb.2015.07.005_b0140 article-title: The hair follicle as a dynamic miniorgan publication-title: Curr. Biol. doi: 10.1016/j.cub.2008.12.005 – volume: 45 start-page: 15 year: 1973 ident: 10.1016/j.jsb.2015.07.005_b0090 article-title: Plasma membrane differentiations of keratinizing cells of the wool follicle (2. desmosomes) publication-title: Ultrastruct. Res. doi: 10.1016/S0022-5320(73)90029-4 – volume: 154 start-page: 79 issue: 1 year: 2006 ident: 10.1016/j.jsb.2015.07.005_b0100 article-title: In vivo formation steps of the hard α-keratin intermediate filament along a hair follicle: evidence for structural polymorphism publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.11.013 – volume: 51 start-page: 95 issue: 1 year: 2003 ident: 10.1016/j.jsb.2015.07.005_b0015 article-title: A total model for the structural mechanics of wool publication-title: Wool Technol. Sheep Breed. – volume: 102 start-page: 1419 year: 1986 ident: 10.1016/j.jsb.2015.07.005_b0135 article-title: Trichohyalin, and intermediate filament-associated protein of the hair follicle publication-title: J. Cell Biol. doi: 10.1083/jcb.102.4.1419 – volume: 300 start-page: 221 issue: 2 year: 2002 ident: 10.1016/j.jsb.2015.07.005_b0095 article-title: Problems associated with the identification of proteins in homologous families: the wool keratin family as a case study publication-title: Anal. Biochem. doi: 10.1006/abio.2001.5459 – volume: 73 start-page: 323 issue: 2 year: 2009 ident: 10.1016/j.jsb.2015.07.005_b0020 article-title: Higher sequence coverage and improved confidence in the identification of cysteine-rich proteins from the wool cuticle using combined chemical and enzymatic digestion publication-title: J. Proteomics doi: 10.1016/j.jprot.2009.09.017 – volume: 127 start-page: 1197 issue: 5 year: 2007 ident: 10.1016/j.jsb.2015.07.005_b0125 article-title: Characterization of human KAP24.1, a cuticular hair keratin-associated protein with unusual amino-acid composition and repeat structure publication-title: J. Invest. Dermatol. doi: 10.1038/sj.jid.5700702 – volume: 11 start-page: 205 issue: 1 year: 1972 ident: 10.1016/j.jsb.2015.07.005_b0080 article-title: An ultrastructural study of the membranes of keratinizing wool follicle cells publication-title: J. Cell Sci. doi: 10.1242/jcs.11.1.205 – volume: 31 start-page: 2894 issue: 17 year: 2010 ident: 10.1016/j.jsb.2015.07.005_b0010 article-title: Electrophoretic mapping of highly homologous keratins: a novel marker peptide approach publication-title: Electrophoresis doi: 10.1002/elps.201000134 – ident: 10.1016/j.jsb.2015.07.005_b0070 – volume: 276 start-page: 19440 issue: 22 year: 2001 ident: 10.1016/j.jsb.2015.07.005_b0110 article-title: Characterization of a cluster of human high/ultrahigh sulfur keratin-associated protein genes embedded in the type I keratin gene domain on chromosome 17q12-21 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M100657200 – volume: 20 start-page: 582 issue: 7 year: 2011 ident: 10.1016/j.jsb.2015.07.005_b0160 article-title: Annotations of sheep keratin intermediate filament genes and their patterns of expression publication-title: Exp. Dermatol. doi: 10.1111/j.1600-0625.2011.01274.x – volume: 274 start-page: 19874 issue: 28 year: 1999 ident: 10.1016/j.jsb.2015.07.005_b0030 article-title: The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.28.19874 – volume: vol. 2 start-page: 141 year: 1980 ident: 10.1016/j.jsb.2015.07.005_b0145 article-title: Studies on the surface layers of the wool fibre cuticle – volume: 173 start-page: 229 issue: 2 year: 2011 ident: 10.1016/j.jsb.2015.07.005_b0065 article-title: A concerted polymerization-mesophase separation model for formation of trichocyte intermediate filaments and macrofibril templates. 1: Relating phase separation to structural development publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2010.11.019 – volume: 80 start-page: 312 issue: 3 year: 1982 ident: 10.1016/j.jsb.2015.07.005_b0085 article-title: Number changes and development potential of wool follicle cells in the early stages of fiber differentiation publication-title: J. Ultrastruct. Res. doi: 10.1016/S0022-5320(82)80044-0 – volume: 11 start-page: 52 year: 1964 ident: 10.1016/j.jsb.2015.07.005_b0130 article-title: The cytology of the cuticle of the cortex, the cortex, and the medulla of the mouse hair publication-title: J. Ultrastruct. Res. doi: 10.1016/S0022-5320(64)80092-7 – volume: 77 start-page: 307 issue: 3 year: 2009 ident: 10.1016/j.jsb.2015.07.005_b0155 article-title: Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles publication-title: Differentiation doi: 10.1016/j.diff.2008.10.009
SSID	ssj0004121
Score	2.3023703
Snippet	Gel and gel-free proteomic techniques have been used for the first time to directly study the proteins present in whole wool follicles and dissected portions...
SourceID	proquest pubmed crossref elsevier
SourceType	Aggregation Database Index Database Enrichment Source Publisher
StartPage	341
SubjectTerms	Animals Collagen - metabolism Desmoplakins - metabolism Epithelial Cells - metabolism Gene Expression - physiology Hair follicle Hair Follicle - metabolism Histones - metabolism Intermediate Filament Proteins - metabolism KAP Keratin Keratins - metabolism Morphogenesis - physiology Proteomics - methods Ribosomal Proteins - metabolism Sheep - metabolism Vimentin - metabolism Wool Wool - metabolism
Title	The proteomics of wool fibre morphogenesis
URI	https://dx.doi.org/10.1016/j.jsb.2015.07.005 https://www.ncbi.nlm.nih.gov/pubmed/26208467 https://www.proquest.com/docview/1708157550
Volume	191
WOSCitedRecordID	wos000360599200009&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVESC databaseName: Elsevier SD Freedom Collection Journals 2021 customDbUrl: eissn: 1095-8657 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0004121 issn: 1047-8477 databaseCode: AIEXJ dateStart: 19950101 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3da9swEBdpu8Fexr7XfRQP9tTgYFuWZD-WLftilMI6yJuRLLlLyOxSt2kL--N3-nS7kbIN9iISJY6du9PdT9LdTwi9lo1iRV7WMYTTMs5huMWAm1lMaS4zTIVS7rAJtr9fzGblwWj0w9fCrJasbYuLi_L4v6oa-kDZunT2L9QdfhQ64DUoHVpQO7R_rHjDvqDrjU2ixrnm2WxgXqzG3zuQa3ekHdy8XwNMLaWsoeNwFE3Bfy67c7di6irAxtPJ4MNOfJbk2zMO2PUgfPQe3vbf3FLrfMV73uoCkhAQuk667YjL8efJ1YWIlIRMK7c65itkriVwGiYIiIA2qCrXVxKwCEtMHbywPbTLmRu-4lOxZcZy4RlbftrfPL9dhFhMFr3QCXvEULImZAhzIfnwi2EkgkcCZ2983AbayhgpwSdu7X2czj4NdbWprdvz_8Hvipv8wF9utA7XrJu3GPxyeA_ddfqN9qzB3Ecj1T5At-1RpJcP0S6YTTSYTdQ1kTabyJhNdM1sHqGv76aHbz7E7hyNuAawfAptCagwpw0FLIkl13PEmokaRCloptKkkVRgVmDFeS5pU2cCp1I2JOOFpLjBj9Fm27XqKYo01xHGKsG5lLkoKCdEKVFmgsO8VXGyjRIvhap2JPP6rJNl5bMJFxUIrtKCqxKd-gCX7IZLji3Dyk1fzr1oKwcRLfSrwA5uuuyVV0MF7lPviYHhd2d9lTLAxDBlIck2emL1E55Cn9Wg4fmzf7vpc3RnGCYv0CYMXvUS3apXp_P-ZAdtsFmx4yzuJ9QznBM
linkProvider	Elsevier
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=The+proteomics+of+wool+fibre+morphogenesis&rft.jtitle=Journal+of+structural+biology&rft.au=Plowman%2C+Jeffrey+E.&rft.au=Harland%2C+Duane+P.&rft.au=Ganeshan%2C+Sivasangary&rft.au=Woods%2C+Joy+L.&rft.date=2015-09-01&rft.pub=Elsevier+Inc&rft.issn=1047-8477&rft.eissn=1095-8657&rft.volume=191&rft.issue=3&rft.spage=341&rft.epage=351&rft_id=info:doi/10.1016%2Fj.jsb.2015.07.005&rft.externalDocID=S1047847715300307
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1047-8477&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1047-8477&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1047-8477&client=summon