Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant.
<p>Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant.</p>
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2025
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| _version_ | 1849927642349830144 |
|---|---|
| author | Takuya Yamaguchi (4543105) |
| author2 | Yasuhisa Asano (727606) |
| author2_role | author |
| author_facet | Takuya Yamaguchi (4543105) Yasuhisa Asano (727606) |
| author_role | author |
| dc.creator.none.fl_str_mv | Takuya Yamaguchi (4543105) Yasuhisa Asano (727606) |
| dc.date.none.fl_str_mv | 2025-11-24T18:30:17Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pgen.1011955.s030 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/dataset/Purification_of_N-terminal_His-tagged_CHUA_005137_from_1_5_L_of_i_Pichia_pastoris_i_culture_supernatant_/30697239 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |
| dc.title.none.fl_str_mv | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| dc.type.none.fl_str_mv | Dataset info:eu-repo/semantics/publishedVersion dataset |
| description | <p>Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_4efd32613208e983dc6a64ceebc151f0 |
| identifier_str_mv | 10.1371/journal.pgen.1011955.s030 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30697239 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant.Takuya Yamaguchi (4543105)Yasuhisa Asano (727606)BiochemistryEvolutionary BiologyEcologyPlant BiologyVirologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedsubsequently converting aldoximenatural defensive chemicalsindicating sequential duplicationcatalyse aldoxime dehydrationdiv >< pcyanogenic millipedes evolvedchamberlinius hualienensis </hualienensis </r </typically lineagerelated enzymesplant lineagesplant kingdomsparalogous genesmillipedes demonstratesmechanisms underlyinghydroxynitrile lyasehydrogen cyanidegiving riseenzymes independentlydependent monooxygenasedeeper understandingcytochrome p450complete setcoding genesbiological characterisation>)- mandelonitrile<p>Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant.</p>2025-11-24T18:30:17ZDatasetinfo:eu-repo/semantics/publishedVersiondataset10.1371/journal.pgen.1011955.s030https://figshare.com/articles/dataset/Purification_of_N-terminal_His-tagged_CHUA_005137_from_1_5_L_of_i_Pichia_pastoris_i_culture_supernatant_/30697239CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/306972392025-11-24T18:30:17Z |
| spellingShingle | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. Takuya Yamaguchi (4543105) Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |
| status_str | publishedVersion |
| title | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| title_full | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| title_fullStr | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| title_full_unstemmed | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| title_short | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| title_sort | Purification of N-terminal His-tagged CHUA_005137 from 1.5 L of <i>Pichia pastoris</i> culture supernatant. |
| topic | Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |