Expression and purification of recombinant mouse CRISP4 using a baculovirus system
Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Gaikwad, Avinash S. [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
|---|
| Schlagwörter: |
|---|
| Übergeordnetes Werk: |
Enthalten in: Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake - Satriano, Claudio ELSEVIER, 2014, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:167 ; year:2020 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.pep.2019.105543 |
|---|
| Katalog-ID: |
ELV048870846 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | ELV048870846 | ||
| 003 | DE-627 | ||
| 005 | 20230626022954.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 200108s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.pep.2019.105543 |2 doi | |
| 028 | 5 | 2 | |a /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica |
| 035 | |a (DE-627)ELV048870846 | ||
| 035 | |a (ELSEVIER)S1046-5928(19)30501-7 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 550 |q VZ |
| 082 | 0 | 4 | |a 610 |a 333.7 |q VZ |
| 084 | |a BIODIV |q DE-30 |2 fid | ||
| 084 | |a 42.90 |2 bkl | ||
| 084 | |a 42.11 |2 bkl | ||
| 100 | 1 | |a Gaikwad, Avinash S. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| 264 | 1 | |c 2020transfer abstract | |
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. | ||
| 520 | |a Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. | ||
| 650 | 7 | |a Epididymal CRISP |2 Elsevier | |
| 650 | 7 | |a Insect cell expression |2 Elsevier | |
| 650 | 7 | |a Cysteine-rich secretory protein |2 Elsevier | |
| 650 | 7 | |a CRISP4 |2 Elsevier | |
| 650 | 7 | |a CAP proteins |2 Elsevier | |
| 700 | 1 | |a Lee Loh, Khai |4 oth | |
| 700 | 1 | |a O'Connor, Anne E. |4 oth | |
| 700 | 1 | |a Reid, Hugh H. |4 oth | |
| 700 | 1 | |a O'Bryan, Moira K. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Satriano, Claudio ELSEVIER |t Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |d 2014 |g Amsterdam [u.a.] |w (DE-627)ELV023049715 |
| 773 | 1 | 8 | |g volume:167 |g year:2020 |g pages:0 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.pep.2019.105543 |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a SYSFLAG_U | ||
| 912 | |a FID-BIODIV | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_72 | ||
| 912 | |a GBV_ILN_217 | ||
| 912 | |a GBV_ILN_255 | ||
| 912 | |a GBV_ILN_257 | ||
| 912 | |a GBV_ILN_286 | ||
| 912 | |a GBV_ILN_341 | ||
| 936 | b | k | |a 42.90 |j Ökologie: Allgemeines |q VZ |
| 936 | b | k | |a 42.11 |j Biomathematik |j Biokybernetik |q VZ |
| 951 | |a AR | ||
| 952 | |d 167 |j 2020 |h 0 | ||
| author_variant |
a s g as asg |
|---|---|
| matchkey_str |
gaikwadavinashsleelohkhaioconnoranneerei:2020----:xrsinnprfctoorcmiatoscipuig |
| hierarchy_sort_str |
2020transfer abstract |
| bklnumber |
42.90 42.11 |
| publishDate |
2020 |
| allfields |
10.1016/j.pep.2019.105543 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica (DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 DE-627 ger DE-627 rakwb eng 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Gaikwad, Avinash S. verfasserin aut Expression and purification of recombinant mouse CRISP4 using a baculovirus system 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier Lee Loh, Khai oth O'Connor, Anne E. oth Reid, Hugh H. oth O'Bryan, Moira K. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:167 year:2020 pages:0 https://doi.org/10.1016/j.pep.2019.105543 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 167 2020 0 |
| spelling |
10.1016/j.pep.2019.105543 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica (DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 DE-627 ger DE-627 rakwb eng 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Gaikwad, Avinash S. verfasserin aut Expression and purification of recombinant mouse CRISP4 using a baculovirus system 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier Lee Loh, Khai oth O'Connor, Anne E. oth Reid, Hugh H. oth O'Bryan, Moira K. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:167 year:2020 pages:0 https://doi.org/10.1016/j.pep.2019.105543 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 167 2020 0 |
| allfields_unstemmed |
10.1016/j.pep.2019.105543 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica (DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 DE-627 ger DE-627 rakwb eng 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Gaikwad, Avinash S. verfasserin aut Expression and purification of recombinant mouse CRISP4 using a baculovirus system 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier Lee Loh, Khai oth O'Connor, Anne E. oth Reid, Hugh H. oth O'Bryan, Moira K. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:167 year:2020 pages:0 https://doi.org/10.1016/j.pep.2019.105543 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 167 2020 0 |
| allfieldsGer |
10.1016/j.pep.2019.105543 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica (DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 DE-627 ger DE-627 rakwb eng 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Gaikwad, Avinash S. verfasserin aut Expression and purification of recombinant mouse CRISP4 using a baculovirus system 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier Lee Loh, Khai oth O'Connor, Anne E. oth Reid, Hugh H. oth O'Bryan, Moira K. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:167 year:2020 pages:0 https://doi.org/10.1016/j.pep.2019.105543 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 167 2020 0 |
| allfieldsSound |
10.1016/j.pep.2019.105543 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica (DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 DE-627 ger DE-627 rakwb eng 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Gaikwad, Avinash S. verfasserin aut Expression and purification of recombinant mouse CRISP4 using a baculovirus system 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier Lee Loh, Khai oth O'Connor, Anne E. oth Reid, Hugh H. oth O'Bryan, Moira K. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:167 year:2020 pages:0 https://doi.org/10.1016/j.pep.2019.105543 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 167 2020 0 |
| language |
English |
| source |
Enthalten in Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake Amsterdam [u.a.] volume:167 year:2020 pages:0 |
| sourceStr |
Enthalten in Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake Amsterdam [u.a.] volume:167 year:2020 pages:0 |
| format_phy_str_mv |
Article |
| bklname |
Ökologie: Allgemeines Biomathematik Biokybernetik |
| institution |
findex.gbv.de |
| topic_facet |
Epididymal CRISP Insect cell expression Cysteine-rich secretory protein CRISP4 CAP proteins |
| dewey-raw |
550 |
| isfreeaccess_bool |
false |
| container_title |
Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
| authorswithroles_txt_mv |
Gaikwad, Avinash S. @@aut@@ Lee Loh, Khai @@oth@@ O'Connor, Anne E. @@oth@@ Reid, Hugh H. @@oth@@ O'Bryan, Moira K. @@oth@@ |
| publishDateDaySort_date |
2020-01-01T00:00:00Z |
| hierarchy_top_id |
ELV023049715 |
| dewey-sort |
3550 |
| id |
ELV048870846 |
| 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">ELV048870846</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626022954.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200108s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.pep.2019.105543</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV048870846</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S1046-5928(19)30501-7</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="082" ind1="0" ind2="4"><subfield code="a">550</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="a">333.7</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="q">DE-30</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.90</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.11</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gaikwad, Avinash S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Expression and purification of recombinant mouse CRISP4 using a baculovirus system</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Epididymal CRISP</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Insect cell expression</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Cysteine-rich secretory protein</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">CRISP4</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">CAP proteins</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee Loh, Khai</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">O'Connor, Anne E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Reid, Hugh H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">O'Bryan, Moira K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Satriano, Claudio ELSEVIER</subfield><subfield code="t">Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake</subfield><subfield code="d">2014</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV023049715</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:167</subfield><subfield code="g">year:2020</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.pep.2019.105543</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</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_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_72</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_217</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_255</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_257</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_286</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_341</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.90</subfield><subfield code="j">Ökologie: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.11</subfield><subfield code="j">Biomathematik</subfield><subfield code="j">Biokybernetik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">167</subfield><subfield code="j">2020</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| author |
Gaikwad, Avinash S. |
| spellingShingle |
Gaikwad, Avinash S. ddc 550 ddc 610 fid BIODIV bkl 42.90 bkl 42.11 Elsevier Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| authorStr |
Gaikwad, Avinash S. |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)ELV023049715 |
| format |
electronic Article |
| dewey-ones |
550 - Earth sciences 610 - Medicine & health 333 - Economics of land & energy |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
elsevier |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Expression and purification of recombinant mouse CRISP4 using a baculovirus system Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins Elsevier |
| topic |
ddc 550 ddc 610 fid BIODIV bkl 42.90 bkl 42.11 Elsevier Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins |
| topic_unstemmed |
ddc 550 ddc 610 fid BIODIV bkl 42.90 bkl 42.11 Elsevier Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins |
| topic_browse |
ddc 550 ddc 610 fid BIODIV bkl 42.90 bkl 42.11 Elsevier Epididymal CRISP Elsevier Insect cell expression Elsevier Cysteine-rich secretory protein Elsevier CRISP4 Elsevier CAP proteins |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
l k l lk lkl a e o ae aeo h h r hh hhr m k o mk mko |
| hierarchy_parent_title |
Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
| hierarchy_parent_id |
ELV023049715 |
| dewey-tens |
550 - Earth sciences & geology 610 - Medicine & health 330 - Economics |
| hierarchy_top_title |
Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)ELV023049715 |
| title |
Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| ctrlnum |
(DE-627)ELV048870846 (ELSEVIER)S1046-5928(19)30501-7 |
| title_full |
Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| author_sort |
Gaikwad, Avinash S. |
| journal |
Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
| journalStr |
Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
500 - Science 600 - Technology 300 - Social sciences |
| recordtype |
marc |
| publishDateSort |
2020 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Gaikwad, Avinash S. |
| container_volume |
167 |
| class |
550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl |
| format_se |
Elektronische Aufsätze |
| author-letter |
Gaikwad, Avinash S. |
| doi_str_mv |
10.1016/j.pep.2019.105543 |
| dewey-full |
550 610 333.7 |
| title_sort |
expression and purification of recombinant mouse crisp4 using a baculovirus system |
| title_auth |
Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| abstract |
Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. |
| abstractGer |
Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. |
| abstract_unstemmed |
Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 |
| title_short |
Expression and purification of recombinant mouse CRISP4 using a baculovirus system |
| url |
https://doi.org/10.1016/j.pep.2019.105543 |
| remote_bool |
true |
| author2 |
Lee Loh, Khai O'Connor, Anne E. Reid, Hugh H. O'Bryan, Moira K. |
| author2Str |
Lee Loh, Khai O'Connor, Anne E. Reid, Hugh H. O'Bryan, Moira K. |
| ppnlink |
ELV023049715 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth |
| doi_str |
10.1016/j.pep.2019.105543 |
| up_date |
2024-07-06T20:01:10.080Z |
| _version_ |
1803861171981254656 |
| 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">ELV048870846</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626022954.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200108s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.pep.2019.105543</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000849.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV048870846</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S1046-5928(19)30501-7</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="082" ind1="0" ind2="4"><subfield code="a">550</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="a">333.7</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="q">DE-30</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.90</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.11</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gaikwad, Avinash S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Expression and purification of recombinant mouse CRISP4 using a baculovirus system</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Cysteine-rich secretory protein 4 (CRISP4) is a member of the CAP superfamily protein, is highly expressed in the male reproductive tract and is required for optimal mammalian fertility. CRISPs are characterized by the presence of 16 conserved cysteine residues which forms 8 disulphide bond spread across the N-terminal CAP domain, a hinge region and a C-terminal ion channel regulatory (ICR) domain. Previous attempts to purify recombinant CRISPs as a group have resulted in misfolded and/or insoluble recombinant proteins, protein aggregates or unusable low protein yield. Thus, defining the functions of CRISPs have been impeded. In this study, we report a three-step purification protocol for expression and purification of mouse CRISP4 protein in High Five™ cells using a baculovirus expression system. Recombinant mouse CRISP4 was recognized by western blotting and structurally characterized using Circular Dichroism (CD). Using the protocol described herein, we generated high yields of soluble and correctly folded recombinant mouse CRISP4.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Epididymal CRISP</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Insect cell expression</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Cysteine-rich secretory protein</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">CRISP4</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">CAP proteins</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee Loh, Khai</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">O'Connor, Anne E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Reid, Hugh H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">O'Bryan, Moira K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Satriano, Claudio ELSEVIER</subfield><subfield code="t">Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake</subfield><subfield code="d">2014</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV023049715</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:167</subfield><subfield code="g">year:2020</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.pep.2019.105543</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</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_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_72</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_217</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_255</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_257</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_286</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_341</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.90</subfield><subfield code="j">Ökologie: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.11</subfield><subfield code="j">Biomathematik</subfield><subfield code="j">Biokybernetik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">167</subfield><subfield code="j">2020</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.3979836 |