Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Evelyne Walker-Nasir"'
Autor:
Evelyne Walker-Nasir, Zahra Zamani, Afshan Kaleem, Nasir-ud-Din, Ikram ul Haq, Daniel C. Hoessli, Abdul Rauf Shakoori, Zeeshan Iqbal, Asma Butt
Publikováno v:
Journal of Cellular Biochemistry. 112:138-146
The multifunctionality of proteins is dictated by post-translational modifications (PTMs) which involve the attachment of small functional groups such as phosphate and acetate, as well as carbohydrate moieties. These functional groups make the protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7961ee1d9e062fb9331cf14cf3f91f78
https://doi.org/10.1002/jcb.22909
https://doi.org/10.1002/jcb.22909
Autor:
Daniel C. Hoessli, Afshan Kaleem, Evelyne Walker-Nasir, Ishtiaq Ahmad, Abdul Rauf Shakoori, Nasir-ud-Din
Publikováno v:
Journal of Cellular Biochemistry, Vol. 108, No 4 (2009) pp. 816-824
Mapping and chemical characterization of post-translational modifications (PTMs) in proteins are critical to understand the regulatory mechanisms involving modified proteins and their role in disease. Neurofibromatosis type 1 (NF-1) is an autosomal d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::868e5177a7df44ac403b8818ad22db68
https://doi.org/10.1002/jcb.22301
https://doi.org/10.1002/jcb.22301
Autor:
Daniel C. Hoessli, Ishtiaq Ahmad, Abid Mehmood, Nasir-ud-Din, Abdul Rauf Shakoori, Wajahat M. Qazi, Ahmed Khurshid, Evelyne Walker-Nasir
Publikováno v:
Journal of Cellular Biochemistry, Vol. 108, No 1 (2009) pp. 64-74
Phosphorylation, one of the most common protein post-translational modifications (PTMs) on hydroxyl groups of S/T/Y is catalyzed by kinases and involves the presence or absence of certain amino acid residues in the vicinity of the phosphorylation sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c42dd45008a750ca909a77321562b270
https://doi.org/10.1002/jcb.22220
https://doi.org/10.1002/jcb.22220
Autor:
Ishtiaq Ahmad, Evelyne Walker-Nasir, Daniel C. Hoessli, Afshan Kaleem, Nasir-ud-Din, Anwar Nasim, Abdul Rauf Shakoori
Publikováno v:
Journal of cellular biochemistry, Vol. 103, No 3 (2008) pp. 835-51
In mammalian cells, induction of immediate-early (IE) gene transcription occurs concomitantly with histone H3 phosphorylation on Ser 10 and is catalyzed by mitogen-activated protein kinases (MAPKs). Histone H3 is an evolutionarily conserved protein l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a8d06131db31f14b56cb2549dd12660
https://doi.org/10.1002/jcb.21454
https://doi.org/10.1002/jcb.21454
Publikováno v:
Current Organic Chemistry. 11:609-618
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6d47c6f9557ad74ac802eb11b99f0dc
https://doi.org/10.2174/138527207780598828
https://doi.org/10.2174/138527207780598828
Publikováno v:
Current Organic Chemistry. 11:591-607
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f27748b937dc396ff381c1bb12b5b1d
https://doi.org/10.2174/138527207780598837
https://doi.org/10.2174/138527207780598837
Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation
Autor:
Abdul Rauf Shakoori, Daniel C. Hoessli, Nasir-ud-Din, Evelyne Walker-Nasir, Saleem M. Rafik, Ishtiaq Ahmad
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Vol. 34, No 1 (2006) pp. 175-184
Nucleic Acids Research, Vol. 34, No 1 (2006) pp. 175-184
Phosphorylation and O-GlcNAc modification often induce conformational changes and allow the protein to specifically interact with other proteins. Interplay of phosphorylation and O-GlcNAc modification at the same conserved site may result in the prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4ab79c07dbd03a0ded03df4c3d9a5b
http://europepmc.org/articles/PMC1326018
http://europepmc.org/articles/PMC1326018
MAPRes: an efficient method to analyze protein sequence around post-translational modification sites
Autor:
Nasir-ud-Din, Daniel C. Hoessli, Ahmed Khurshid, Ishtiaq Ahmad, Munir Ahmad, Evelyne Walker-Nasir, Abdul Rauf Shakoori, Abid Mehmood, Wajahat M. Qazi
Publikováno v:
Journal of cellular biochemistry, Vol. 104, No 4 (2008) pp. 1220-31
Functional switches are often regulated by dynamic protein modifications. Assessing protein functions, in vivo, and their functional switches remains still a great challenge in this age of development. An alternative methodology based on in silico pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38d6b7ead5410322270267406979c96b
https://pubmed.ncbi.nlm.nih.gov/18286469
https://pubmed.ncbi.nlm.nih.gov/18286469
Autor:
null Nasir-ud-Din, Ishtiaq Ahmad, Tehmina S. Khan, Daniel C. Hoessli, Evelyne Walker-Nasir, Afshan Kaleem, Abdul R. Shakoori
Publikováno v:
Protein and Peptide Letters, Vol. 15, No 2 (2008) pp. 193-9
Utilizing different computational methods; phosphorylation, O-GlcNAc modification and Yin Yang sites are predicted in HMGN-1. Prediction results suggest that interplay of phosphorylation and O-GlcNAc modification regulates binding and removal of HMGN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6d21de467de23f7ec09ab480bd10b54
https://archive-ouverte.unige.ch/unige:2492
https://archive-ouverte.unige.ch/unige:2492
Autor:
Nasir-Ud Nasir-Ud Din, Abdul Rauf Shakoori, Tayyaba Wajahat, Ishtiaq Ahmad, Tasneem A. Khwaja, Evelyne Walker-Nasir, Daniel C. Hoessli, Afshan Kaleem, Wajahat M. Qazi
Publikováno v:
Journal of cellular biochemistry, Vol. 103, No 2 (2008) pp. 479-91
The mistletoe lectin-1 (ML-1) modulates tumor cell apoptosis by triggering signaling cascades through the complex interplay of phosphorylation and O-linked N-acetylglucosamine (O-GlcNAc) modification in pro- and anti-apoptotic proteins. In particular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf2b62c084c4e7372047d977be06dea6
https://archive-ouverte.unige.ch/unige:2489
https://archive-ouverte.unige.ch/unige:2489