PMID- 32489294
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20200928
IS  - 1319-562X (Print)
IS  - 2213-7106 (Electronic)
IS  - 2213-7106 (Linking)
VI  - 27
IP  - 6
DP  - 2020 Jun
TI  - Molecular cloning, expression, overproduction and characterization of human TRAIP 
      Leucine zipper protein.
PG  - 1562-1565
LID - 10.1016/j.sjbs.2020.03.011 [doi]
AB  - The TRAIP interacting protein is known as a negative regulator of 
      TNF-induced-nuclear factor, kappa-light-chain-enhancer of activated B cell 
      (NF-kappaB) by direct interaction with the adaptor protein TRAF2, which inhibits the 
      function of TRAF2 via the RINGCC domain protein. The TRAIP protein is composed of 
      469 amino acids with an N-terminal RING motif that is followed by a coiled coil 
      (CC) and leucine zipper domain. TRAIP proteins are critical in programmed cell 
      death, cell proliferation and differentiation, and embryonic development. The 
      critical functions of TRAIP together with the molecular inhibitory mechanism 
      effect of TRAIP have been reported by two different studies and have opened up 
      new research into the field of TRAF biology. In this study, we designed different 
      constructs of the Leucine zipper domain to find the over -expressed construct for 
      further studies. We successfully cloned the C-terminal TRAIP containing the 
      leucine zipper domain. In addition, we have over-expressed and purified the TRAIP 
      LZ for their biochemical characterization.
CI  - (c) 2020 Published by Elsevier B.V. on behalf of King Saud University.
FAU - Bhat, Eijaz Ahmed
AU  - Bhat EA
AD  - Life Science Institute, Zhejiang University, Hangzhou, Zhejiang 310058, PR China.
FAU - Sajjad, Nasreena
AU  - Sajjad N
AD  - Department of Biochemistry, University of Kashmir, Hazratbal, Jammu and Kashmir, 
      India.
FAU - Sabir, Jamal S M
AU  - Sabir JSM
AD  - Department of Biological Sciences, Faculty of Science, King Abdulaziz University 
      (KAU), Jeddah 21589, Saudi Arabia.
AD  - Centre of Excellence in Bionanoscience Research, King Abdulaziz University (KAU), 
      Jeddah 21589, Saudi Arabia.
FAU - Kamli, Majid Rasool
AU  - Kamli MR
AD  - Department of Biological Sciences, Faculty of Science, King Abdulaziz University 
      (KAU), Jeddah 21589, Saudi Arabia.
AD  - Centre of Excellence in Bionanoscience Research, King Abdulaziz University (KAU), 
      Jeddah 21589, Saudi Arabia.
FAU - Hakeem, Khalid Rehman
AU  - Hakeem KR
AD  - Department of Biological Sciences, Faculty of Science, King Abdulaziz University 
      (KAU), Jeddah 21589, Saudi Arabia.
FAU - Rather, Irfan A
AU  - Rather IA
AD  - Department of Biological Sciences, Faculty of Science, King Abdulaziz University 
      (KAU), Jeddah 21589, Saudi Arabia.
AD  - Centre of Excellence in Bionanoscience Research, King Abdulaziz University (KAU), 
      Jeddah 21589, Saudi Arabia.
FAU - Bahieldin, Ahmed
AU  - Bahieldin A
AD  - Department of Biological Sciences, Faculty of Science, King Abdulaziz University 
      (KAU), Jeddah 21589, Saudi Arabia.
LA  - eng
PT  - Journal Article
DEP - 20200313
PL  - Saudi Arabia
TA  - Saudi J Biol Sci
JT  - Saudi journal of biological sciences
JID - 101543796
PMC - PMC7253899
OTO - NOTNLM
OT  - Apoptosis
OT  - NF-kappaB
OT  - Proliferation
OT  - TNF interacting protein
OT  - TNFR
OT  - TRAF2
COIS- The authors declare that they have no known competing financial interests or 
      personal relationships that could have appeared to influence the work reported in 
      this paper.
EDAT- 2020/06/04 06:00
MHDA- 2020/06/04 06:01
PMCR- 2020/03/13
CRDT- 2020/06/04 06:00
PHST- 2019/12/24 00:00 [received]
PHST- 2020/03/01 00:00 [revised]
PHST- 2020/03/05 00:00 [accepted]
PHST- 2020/06/04 06:00 [entrez]
PHST- 2020/06/04 06:00 [pubmed]
PHST- 2020/06/04 06:01 [medline]
PHST- 2020/03/13 00:00 [pmc-release]
AID - S1319-562X(20)30087-5 [pii]
AID - 10.1016/j.sjbs.2020.03.011 [doi]
PST - ppublish
SO  - Saudi J Biol Sci. 2020 Jun;27(6):1562-1565. doi: 10.1016/j.sjbs.2020.03.011. Epub 
      2020 Mar 13.