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- Publisher Website: 10.1002/cplu.201900130
- Scopus: eid_2-s2.0-85065195494
- PMID: 31943990
- WOS: WOS:000477962500002
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Article: Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations
Title | Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations |
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Authors | |
Keywords | Acetylation HMG proteins Kinase assays Post-translational modifications Ser/Thr ligation |
Issue Date | 2019 |
Publisher | Wiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%292192-6506 |
Citation | ChemPlusChem, 2019, v. 84 n. 7, p. 779-785 How to Cite? |
Abstract | High‐mobility‐group (HMG) proteins are a class of abundant non‐histone nuclear proteins, among which HMGA1a is well‐known for its association with transcription regulation as well as tumor formation and disease development. To study the functions of post‐translational modifications, homogeneous HMGA1a protein with site‐specific lysine acetylations (64/66/70/73) has been chemically synthesized. The full‐length HMGA1a protein was assembled through two Ser/Thr ligations of three peptide fragments at Gly37‐Thr37 and Thr75‐Thr76 sites, respectively. Further in vitro studies with chemically synthesized proteins suggested that these acetylations did not significantly affect the CK2‐catalyzed phosphorylation on the HMGA1a acidic tail. |
Persistent Identifier | http://hdl.handle.net/10722/272141 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 0.778 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Liu, H | - |
dc.contributor.author | Liu, H | - |
dc.contributor.author | Li, X | - |
dc.date.accessioned | 2019-07-20T10:36:27Z | - |
dc.date.available | 2019-07-20T10:36:27Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | ChemPlusChem, 2019, v. 84 n. 7, p. 779-785 | - |
dc.identifier.issn | 2192-6506 | - |
dc.identifier.uri | http://hdl.handle.net/10722/272141 | - |
dc.description.abstract | High‐mobility‐group (HMG) proteins are a class of abundant non‐histone nuclear proteins, among which HMGA1a is well‐known for its association with transcription regulation as well as tumor formation and disease development. To study the functions of post‐translational modifications, homogeneous HMGA1a protein with site‐specific lysine acetylations (64/66/70/73) has been chemically synthesized. The full‐length HMGA1a protein was assembled through two Ser/Thr ligations of three peptide fragments at Gly37‐Thr37 and Thr75‐Thr76 sites, respectively. Further in vitro studies with chemically synthesized proteins suggested that these acetylations did not significantly affect the CK2‐catalyzed phosphorylation on the HMGA1a acidic tail. | - |
dc.language | eng | - |
dc.publisher | Wiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%292192-6506 | - |
dc.relation.ispartof | ChemPlusChem | - |
dc.subject | Acetylation | - |
dc.subject | HMG proteins | - |
dc.subject | Kinase assays | - |
dc.subject | Post-translational modifications | - |
dc.subject | Ser/Thr ligation | - |
dc.title | Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations | - |
dc.type | Article | - |
dc.identifier.email | Li, X: xuechenl@hku.hk | - |
dc.identifier.authority | Li, X=rp00742 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1002/cplu.201900130 | - |
dc.identifier.pmid | 31943990 | - |
dc.identifier.scopus | eid_2-s2.0-85065195494 | - |
dc.identifier.hkuros | 299165 | - |
dc.identifier.volume | 84 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 779 | - |
dc.identifier.epage | 785 | - |
dc.identifier.isi | WOS:000477962500002 | - |
dc.publisher.place | Germany | - |
dc.identifier.issnl | 2192-6506 | - |