Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Syed Arif, Abdul Rehman"'
Autor:
Syed Arif Abdul Rehman, Elena Di Nisio, Chiara Cazzaniga, Odetta Antico, Axel Knebel, Clare Johnson, Frederic Lamoliatte, Rodolfo Negri, Miratul Muqit MK, Virginia De Cesare
E2 conjugating enzymes (E2s) play a central role in the enzymatic cascade that leads to the attachment of ubiquitin to a substrate. This process, termed ubiquitylation is fundamental for maintaining cellular homeostasis and impacts almost all cellula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5213529c293d7dae87454baf4c9f7290
https://doi.org/10.1101/2023.03.05.531151
https://doi.org/10.1101/2023.03.05.531151
Autor:
Sven M. Lange, Syed Arif Abdul Rehman, Dmitri I. Svergun, Lee A. Armstrong, Yogesh Kulathu, Yosua Adi Kristariyanto, Axel Knebel, Tobias W. Gräwert
Publikováno v:
'Molecular Cell ', vol: 81, pages: 4176-4190 (2021)
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Summary Of the eight distinct polyubiquitin (polyUb) linkages that can be assembled, the roles of K48-linked polyUb (K48-polyUb) are the most established, with K48-polyUb modified proteins being targeted for degradation. MINDY1 and MINDY2 are members
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b23d77ec8d443d9dee20b6661b5b4428
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:58802
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:58802
Autor:
Javed Masood Khan, Atiyatul Qadeer, Sumit Kumar Chaturvedi, Ejaz Ahmad, Syed Arif Abdul Rehman, Samudrala Gourinath, Rizwan Hasan Khan
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29694 (2012)
Sodium dodecyl sulphate (SDS), an anionic surfactant that mimics some characteristics of biological membrane has also been found to induce aggregation in proteins. The present study was carried out on 25 diverse proteins using circular dichroism, flu
Externí odkaz:
https://doaj.org/article/d3be5b33ee1b4eeaabe84afa98d25c60
Publikováno v:
Biochemical Journal. 475:3493-3509
The helicase–primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain of primase (DnaG) and N-terminal domain of helicase (DnaB). To understand the functional conservation despite the low
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::857b0864d8edba7d1b227e4fb4efc50b
https://doi.org/10.1042/bcj20180673
https://doi.org/10.1042/bcj20180673
Autor:
Simone Weidlich, Yosua Adi Kristariyanto, Axel Knebel, Yogesh Kulathu, Syed Arif Abdul Rehman
Publikováno v:
EMBO reports
The eight different types of ubiquitin (Ub) chains that can be formed play important roles in diverse cellular processes. Linkage‐selective recognition of Ub chains by Ub‐binding domain (UBD)‐containing proteins is central to coupling different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0368614887c35e8a54c8a8c95510701c
Publikováno v:
Molecular microbiologyReferences. 112(2)
O-acetylserine sulfhydrylase (OASS) and cystathionine β-synthase (CBS) are members of the PLP-II family, and involved in L-cysteine production. OASS produces L-cysteine via a de novo pathway while CBS participates in the reverse transsulfuration pat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16daffd2e328d2280c335c8f6305b12e
https://pubmed.ncbi.nlm.nih.gov/31132312
https://pubmed.ncbi.nlm.nih.gov/31132312
Autor:
Mohammad Farhan Ali, Syed Arif Abdul Rehman, K.F. Tarique, S. Devi, Samudrala Gourinath, Priya Tomar
Publikováno v:
Journal of Structural Biology. 212:107645
Pyridoxal 5'-phosphate (PLP) is the active form of vitamin B6 and a cofactor for more than 140 enzymes. This coenzyme plays a pivotal role in catalysis of various enzymatic reactions that are critical for the survival of organisms. Entamoeba histolyt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d467310a1359ca7c452efae3792f38b5
https://doi.org/10.1016/j.jsb.2020.107645
https://doi.org/10.1016/j.jsb.2020.107645
Autor:
Syed Arif, Abdul Rehman, Yosua Adi, Kristariyanto, Soo-Youn, Choi, Pedro Junior, Nkosi, Simone, Weidlich, Karim, Labib, Kay, Hofmann, Yogesh, Kulathu
Publikováno v:
Molecular Cell
Summary Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitylation. Here we report the discovery of a new family of DUBs, which we have named MINDY (motif interacting with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::73875d3f81440be09d46b263473e33c1
Autor:
Dhakaram Pangeni, Sharma, Ramachandran, Vijayan, Syed Arif Abdul, Rehman, Samudrala, Gourinath
Publikováno v:
The Biochemical journal. 475(21)
The helicase-primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain of primase (DnaG) and N-terminal domain of helicase (DnaB). To understand the functional conservation despite the low s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::07e658cc734afa8bd67a432e2af44588
https://pubmed.ncbi.nlm.nih.gov/30315069
https://pubmed.ncbi.nlm.nih.gov/30315069
Autor:
Andreas Zoephel, Syed Arif Abdul Rehman, Deepika Pathak, Pawel Leznicki, Nuno L. Barbosa-Morais, Marie C. Bordone, Jayaprakash Natarajan, Simone Weidlich, Gerd Bader, Guido Boehmelt, Andreas Schlattl, Yogesh Kulathu, Walter Spevak
Publikováno v:
Journal of Cell Science.
Protein ubiquitylation is a dynamic post-translational modification that can be reversed by deubiquitylating enzymes (DUBs). It is unclear how the small number (∼100) of DUBs present in mammalian cells regulate the thousands of different ubiquityla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c84c574a5d2f639433cf14d53e0df2
https://doi.org/10.1242/jcs.212753
https://doi.org/10.1242/jcs.212753