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PWWP2A/B: Prominent players in the proteomic landscape (vol 942, 149245, 2025)
Vinayaka Missions Res Fdn Deemed Univ, Aarupadai Veedu Med Coll & Hosp, Dept Med Biotechnol, Pondicherry, India.
Sri Balaji Vidyapeeth Deemed Univ, Mahatma Gandhi Med Adv Res Inst, Pondicherry 607402, India.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.ORCID iD: 0000-0002-3322-8621
Sri Balaji Vidyapeeth Deemed Univ, Mahatma Gandhi Med Adv Res Inst, Pondicherry 607402, India.
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2025 (English)In: Gene, ISSN 0378-1119, E-ISSN 1879-0038, Vol. 948, article id 149344Article in journal (Refereed) Published
Abstract [en]

The authors regret an unintentional mistake in the single-letter code for Tryptophan in the legend of Fig. 5 and in Page 5 where the figure is cited. The authors would like to apologise for any inconvenience caused. The single-letter code for Tryptophan is mistakenly published as “Y”, instead of “W”. The corrected legend for Fig. 5 is provided below: Fig. 5. A) Different homologs of the PWWP domain superimposed on each other, showing histone methyl-lysine-binding aromatic cage. Dark blue and red represents the BRPF1:H3K36me3 peptide complex (PDB Id: 2X4W), light pink corresponds to the modelled PWWP domain structure of PWWP2A, and cyan denotes the PWWP domain structure of PWWP2B (PDB Id: 4LD6). In the BRPF1:H3K36me3 peptide complex, the aromatic cage residues Y1096, Y1099, and F1147, corresponds to F666, W669, and W695 in PWWP2A, and F501, W504, and W530 in PWWP2B. B) Images visualizing the distribution of electrostatic charges on the surface of PWWP2A and PWWP2B proteins. In these visualizations, red indicates negatively charged regions and blue represents positively charged areas. These surface maps confirm the presence of positively charged surfaces in both proteins, supporting their potential interaction with DNA. The corrected text in page 5 is provided below: Similarly, studies on the PWWP domain of the BRPF1 protein identified aromatic residues Y1096, Y1099, and F1147 as key contributors to H3K36me3 binding. Structural superimposition revealed that these residues correspond to F666, W669, and W695 in PWWP2A, and F501, W504, and W530 in PWWP2B

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Elsevier BV , 2025. Vol. 948, article id 149344
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Medical and Health Sciences
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URN: urn:nbn:se:kth:diva-361898DOI: 10.1016/j.gene.2025.149344ISI: 001443903900001PubMedID: 40023690Scopus ID: 2-s2.0-85219081092OAI: oai:DiVA.org:kth-361898DiVA, id: diva2:1949374
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QC 20250409

Available from: 2025-04-02 Created: 2025-04-02 Last updated: 2025-04-09Bibliographically approved

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Kumar, Rajender

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