Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation

Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive al...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Fang, Ming [verfasserIn] Jacob, Reed McDougal, Owen Oxford, Julia Thom

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2012

Schlagwörter:	minor fibrillar collagens variable regions alternative splicing fibrillogenesis heparan sulfate binding sites intrinsic disorder tyrosine sulfation

Anmerkung:	© Higher Education Press and Springer-Verlag Berlin Heidelberg 2012

Übergeordnetes Werk:	Enthalten in: Protein & cell - Beijing : Higher Education Press, 2010, 3(2012), 6 vom: 03. März, Seite 419-433
Übergeordnetes Werk:	volume:3 ; year:2012 ; number:6 ; day:03 ; month:03 ; pages:419-433

Links:	Volltext

DOI / URN:	10.1007/s13238-012-2917-5

Katalog-ID:	SPR030984769

Internformat


LEADER	01000caa a22002652 4500
001	SPR030984769
003	DE-627
005	20230519183600.0
007	cr uuu---uuuuu
008	201007s2012 xx \|\|\|\|\|o 00\| \|\|eng c
024	7		\|a 10.1007/s13238-012-2917-5 \|2 doi
035			\|a (DE-627)SPR030984769
035			\|a (SPR)s13238-012-2917-5-e
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
100	1		\|a Fang, Ming \|e verfasserin \|4 aut
245	1	0	\|a Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
264		1	\|c 2012
336			\|a Text \|b txt \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
500			\|a © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012
520			\|a Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.
650		4	\|a minor fibrillar collagens \|7 (dpeaa)DE-He213
650		4	\|a variable regions \|7 (dpeaa)DE-He213
650		4	\|a alternative splicing \|7 (dpeaa)DE-He213
650		4	\|a fibrillogenesis \|7 (dpeaa)DE-He213
650		4	\|a heparan sulfate binding sites \|7 (dpeaa)DE-He213
650		4	\|a intrinsic disorder \|7 (dpeaa)DE-He213
650		4	\|a tyrosine sulfation \|7 (dpeaa)DE-He213
700	1		\|a Jacob, Reed \|4 aut
700	1		\|a McDougal, Owen \|4 aut
700	1		\|a Oxford, Julia Thom \|4 aut
773	0	8	\|i Enthalten in \|t Protein & cell \|d Beijing : Higher Education Press, 2010 \|g 3(2012), 6 vom: 03. März, Seite 419-433 \|w (DE-627)621548308 \|w (DE-600)2543451-2 \|x 1674-8018 \|7 nnns
773	1	8	\|g volume:3 \|g year:2012 \|g number:6 \|g day:03 \|g month:03 \|g pages:419-433
856	4	0	\|u https://dx.doi.org/10.1007/s13238-012-2917-5 \|z lizenzpflichtig \|3 Volltext
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_SPRINGER
912			\|a SSG-OLC-PHA
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 3 \|j 2012 \|e 6 \|b 03 \|c 03 \|h 419-433

Indexfelder

author_variant	m f mf r j rj o m om j t o jt jto
matchkey_str	article:16748018:2012----::iofbilrolgnvralrgoslentvslcnitisci
hierarchy_sort_str	2012
publishDate	2012
allfields	10.1007/s13238-012-2917-5 doi (DE-627)SPR030984769 (SPR)s13238-012-2917-5-e DE-627 ger DE-627 rakwb eng Fang, Ming verfasserin aut Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012 Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213 Jacob, Reed aut McDougal, Owen aut Oxford, Julia Thom aut Enthalten in Protein & cell Beijing : Higher Education Press, 2010 3(2012), 6 vom: 03. März, Seite 419-433 (DE-627)621548308 (DE-600)2543451-2 1674-8018 nnns volume:3 year:2012 number:6 day:03 month:03 pages:419-433 https://dx.doi.org/10.1007/s13238-012-2917-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 3 2012 6 03 03 419-433
spelling	10.1007/s13238-012-2917-5 doi (DE-627)SPR030984769 (SPR)s13238-012-2917-5-e DE-627 ger DE-627 rakwb eng Fang, Ming verfasserin aut Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012 Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213 Jacob, Reed aut McDougal, Owen aut Oxford, Julia Thom aut Enthalten in Protein & cell Beijing : Higher Education Press, 2010 3(2012), 6 vom: 03. März, Seite 419-433 (DE-627)621548308 (DE-600)2543451-2 1674-8018 nnns volume:3 year:2012 number:6 day:03 month:03 pages:419-433 https://dx.doi.org/10.1007/s13238-012-2917-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 3 2012 6 03 03 419-433
allfields_unstemmed	10.1007/s13238-012-2917-5 doi (DE-627)SPR030984769 (SPR)s13238-012-2917-5-e DE-627 ger DE-627 rakwb eng Fang, Ming verfasserin aut Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012 Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213 Jacob, Reed aut McDougal, Owen aut Oxford, Julia Thom aut Enthalten in Protein & cell Beijing : Higher Education Press, 2010 3(2012), 6 vom: 03. März, Seite 419-433 (DE-627)621548308 (DE-600)2543451-2 1674-8018 nnns volume:3 year:2012 number:6 day:03 month:03 pages:419-433 https://dx.doi.org/10.1007/s13238-012-2917-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 3 2012 6 03 03 419-433
allfieldsGer	10.1007/s13238-012-2917-5 doi (DE-627)SPR030984769 (SPR)s13238-012-2917-5-e DE-627 ger DE-627 rakwb eng Fang, Ming verfasserin aut Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012 Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213 Jacob, Reed aut McDougal, Owen aut Oxford, Julia Thom aut Enthalten in Protein & cell Beijing : Higher Education Press, 2010 3(2012), 6 vom: 03. März, Seite 419-433 (DE-627)621548308 (DE-600)2543451-2 1674-8018 nnns volume:3 year:2012 number:6 day:03 month:03 pages:419-433 https://dx.doi.org/10.1007/s13238-012-2917-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 3 2012 6 03 03 419-433
allfieldsSound	10.1007/s13238-012-2917-5 doi (DE-627)SPR030984769 (SPR)s13238-012-2917-5-e DE-627 ger DE-627 rakwb eng Fang, Ming verfasserin aut Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012 Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213 Jacob, Reed aut McDougal, Owen aut Oxford, Julia Thom aut Enthalten in Protein & cell Beijing : Higher Education Press, 2010 3(2012), 6 vom: 03. März, Seite 419-433 (DE-627)621548308 (DE-600)2543451-2 1674-8018 nnns volume:3 year:2012 number:6 day:03 month:03 pages:419-433 https://dx.doi.org/10.1007/s13238-012-2917-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 3 2012 6 03 03 419-433
language	English
source	Enthalten in Protein & cell 3(2012), 6 vom: 03. März, Seite 419-433 volume:3 year:2012 number:6 day:03 month:03 pages:419-433
sourceStr	Enthalten in Protein & cell 3(2012), 6 vom: 03. März, Seite 419-433 volume:3 year:2012 number:6 day:03 month:03 pages:419-433
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	minor fibrillar collagens variable regions alternative splicing fibrillogenesis heparan sulfate binding sites intrinsic disorder tyrosine sulfation
isfreeaccess_bool	false
container_title	Protein & cell
authorswithroles_txt_mv	Fang, Ming @@aut@@ Jacob, Reed @@aut@@ McDougal, Owen @@aut@@ Oxford, Julia Thom @@aut@@
publishDateDaySort_date	2012-03-03T00:00:00Z
hierarchy_top_id	621548308
id	SPR030984769
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR030984769</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519183600.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2012 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s13238-012-2917-5</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR030984769</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s13238-012-2917-5-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Fang, Ming</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2012</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Higher Education Press and Springer-Verlag Berlin Heidelberg 2012</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">minor fibrillar collagens</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">variable regions</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">alternative splicing</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">fibrillogenesis</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">heparan sulfate binding sites</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">intrinsic disorder</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">tyrosine sulfation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jacob, Reed</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">McDougal, Owen</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Oxford, Julia Thom</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Protein & cell</subfield><subfield code="d">Beijing : Higher Education Press, 2010</subfield><subfield code="g">3(2012), 6 vom: 03. März, Seite 419-433</subfield><subfield code="w">(DE-627)621548308</subfield><subfield code="w">(DE-600)2543451-2</subfield><subfield code="x">1674-8018</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:3</subfield><subfield code="g">year:2012</subfield><subfield code="g">number:6</subfield><subfield code="g">day:03</subfield><subfield code="g">month:03</subfield><subfield code="g">pages:419-433</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s13238-012-2917-5</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_702</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4246</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">3</subfield><subfield code="j">2012</subfield><subfield code="e">6</subfield><subfield code="b">03</subfield><subfield code="c">03</subfield><subfield code="h">419-433</subfield></datafield></record></collection>
author	Fang, Ming
spellingShingle	Fang, Ming misc minor fibrillar collagens misc variable regions misc alternative splicing misc fibrillogenesis misc heparan sulfate binding sites misc intrinsic disorder misc tyrosine sulfation Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
authorStr	Fang, Ming
ppnlink_with_tag_str_mv	@@773@@(DE-627)621548308
format	electronic Article
delete_txt_mv	keep
author_role	aut aut aut aut
collection	springer
remote_str	true
illustrated	Not Illustrated
issn	1674-8018
topic_title	Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation minor fibrillar collagens (dpeaa)DE-He213 variable regions (dpeaa)DE-He213 alternative splicing (dpeaa)DE-He213 fibrillogenesis (dpeaa)DE-He213 heparan sulfate binding sites (dpeaa)DE-He213 intrinsic disorder (dpeaa)DE-He213 tyrosine sulfation (dpeaa)DE-He213
topic	misc minor fibrillar collagens misc variable regions misc alternative splicing misc fibrillogenesis misc heparan sulfate binding sites misc intrinsic disorder misc tyrosine sulfation
topic_unstemmed	misc minor fibrillar collagens misc variable regions misc alternative splicing misc fibrillogenesis misc heparan sulfate binding sites misc intrinsic disorder misc tyrosine sulfation
topic_browse	misc minor fibrillar collagens misc variable regions misc alternative splicing misc fibrillogenesis misc heparan sulfate binding sites misc intrinsic disorder misc tyrosine sulfation
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	cr
hierarchy_parent_title	Protein & cell
hierarchy_parent_id	621548308
hierarchy_top_title	Protein & cell
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)621548308 (DE-600)2543451-2
title	Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
ctrlnum	(DE-627)SPR030984769 (SPR)s13238-012-2917-5-e
title_full	Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
author_sort	Fang, Ming
journal	Protein & cell
journalStr	Protein & cell
lang_code	eng
isOA_bool	false
recordtype	marc
publishDateSort	2012
contenttype_str_mv	txt
container_start_page	419
author_browse	Fang, Ming Jacob, Reed McDougal, Owen Oxford, Julia Thom
container_volume	3
format_se	Elektronische Aufsätze
author-letter	Fang, Ming
doi_str_mv	10.1007/s13238-012-2917-5
title_sort	minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
title_auth	Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
abstract	Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012
abstractGer	Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012
abstract_unstemmed	Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function. © Higher Education Press and Springer-Verlag Berlin Heidelberg 2012
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2014 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	6
title_short	Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
url	https://dx.doi.org/10.1007/s13238-012-2917-5
remote_bool	true
author2	Jacob, Reed McDougal, Owen Oxford, Julia Thom
author2Str	Jacob, Reed McDougal, Owen Oxford, Julia Thom
ppnlink	621548308
mediatype_str_mv	c
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1007/s13238-012-2917-5
up_date	2024-07-03T21:18:59.355Z
_version_	1803594277172805632
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR030984769</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519183600.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2012 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s13238-012-2917-5</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR030984769</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s13238-012-2917-5-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Fang, Ming</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2012</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Higher Education Press and Springer-Verlag Berlin Heidelberg 2012</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">minor fibrillar collagens</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">variable regions</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">alternative splicing</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">fibrillogenesis</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">heparan sulfate binding sites</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">intrinsic disorder</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">tyrosine sulfation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jacob, Reed</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">McDougal, Owen</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Oxford, Julia Thom</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Protein & cell</subfield><subfield code="d">Beijing : Higher Education Press, 2010</subfield><subfield code="g">3(2012), 6 vom: 03. März, Seite 419-433</subfield><subfield code="w">(DE-627)621548308</subfield><subfield code="w">(DE-600)2543451-2</subfield><subfield code="x">1674-8018</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:3</subfield><subfield code="g">year:2012</subfield><subfield code="g">number:6</subfield><subfield code="g">day:03</subfield><subfield code="g">month:03</subfield><subfield code="g">pages:419-433</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s13238-012-2917-5</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_702</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4246</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">3</subfield><subfield code="j">2012</subfield><subfield code="e">6</subfield><subfield code="b">03</subfield><subfield code="c">03</subfield><subfield code="h">419-433</subfield></datafield></record></collection>
score	7.399214

Nicht das Richtige dabei?

Schreiben Sie uns!

Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?