Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Venkataraman Kabaleeswaran"'
Autor:
Sevgi, Keles, Louis Marie, Charbonnier, Venkataraman, Kabaleeswaran, Ismail, Reisli, Ferah, Genel, Nesrin, Gulez, Waleed, Al-Herz, Narayanaswamy, Ramesh, Antonio, Perez-Atayde, Neslihan E, Karaca, Necil, Kutukculer, Hao, Wu, Raif S, Geha, Talal A, Chatila
Publikováno v:
The Journal of allergy and clinical immunology. 138(5)
The autosomal recessive hyper-IgE syndrome (HIES) caused by dedicator of cytokinesis 8 (DOCK8) deficiency shares clinical features with autosomal dominant HIES because of signal transducer and activator of transcription 3 (STAT3) mutations, including
Autor:
Zhijian J. Chen, Xiaomo Jiang, Venkataraman Kabaleeswaran, Daqi Tu, Hao Wu, Michael J. Eck, Qian Yin, Yuan Tian
Publikováno v:
Molecular Cell. 46(6):735-745
Detection of foreign materials is the first step of successful immune responses. Stimulator of interferon genes (STING) was shown to directly bind cyclic diguanylate monophosphate (c-di-GMP), a bacterial second messenger, and to elicit strong interfe
Autor:
Yaping Pan, Ming Zhou, Wayne A. Hendrickson, Venkataraman Kabaleeswaran, Yu Cao, Brian Kloss, Hua Huang, Youxing Jiang, Kanagalaghatta R. Rajashankar, Jun Weng, Mehabaw G. Derebe, Renato Bruni, Elena J. Levin, Xiangshu Jin, Burkhard Rost, Matthias Quick, Sheng Ye, Marco Punta, J. Love, Jonathan A. Javitch, Erik Martinez-Hackert
Publikováno v:
Nature
The TrkH/TrkG/KtrB proteins mediate K+ uptake in bacteria and probably evolved from simple K+ channels by multiple gene duplications or fusions. Here we present the crystal structure of a TrkH from Vibrio parahaemolyticus. TrkH is a homodimer, and ea
The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
Autor:
Se Bok Jang, Liwei Wang, Venkataraman Kabaleeswaran, Stefan Raunser, Jin Kuk Yang, Anthony C. Cruz, Ah Young Park, Hao Wu, Qian Yin, Thomas Walz, Amanda J. Rice, Ermelinda Damko, Carol V. Robinson, Richard M. Siegel
Publikováno v:
Nature structural & molecular biology
The death-inducing signaling complex (DISC) formed by the death receptor Fas, the adaptor protein FADD and caspase-8 mediates the extrinsic apoptotic program. Mutations in Fas that disrupt the DISC cause autoimmune lymphoproliferative syndrome (ALPS)
Publikováno v:
Molecular Cell. 38(1):101-113
TRAF1/2 and cIAP1/2 are members of the TNF receptor associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for both the canonical and the noncanonical NF-κB signaling pathways. Here we report the crys
Autor:
John E. Walker, David M. Mueller, Hong Shen, Venkataraman Kabaleeswaran, Jindrich Symersky, Andrew G. W. Leslie
Publikováno v:
Journal of Biological Chemistry. 284:10546-10551
The crystal structure of nucleotide-free yeast F(1) ATPase has been determined at a resolution of 3.6 A. The overall structure is very similar to that of the ground state enzyme. In particular, the beta(DP) and beta(TP) subunits both adopt the closed
Publikováno v:
Nature Chemical Biology. 4:708-714
The Shaker family voltage-dependent potassium channels (Kv1) are expressed in a wide variety of cells and are essential for cellular excitability. In humans, loss-of-function mutations of Kv1 channels lead to hyperexcitability and are directly linked
Autor:
David M. Mueller, John E. Walker, Venkataraman Kabaleeswaran, Neeti Puri, Andrew G. W. Leslie
Publikováno v:
The EMBO Journal. 25:5433-5442
The crystal structure of yeast mitochondrial F(1) ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the alpha(3)beta(3) sub-assemb
Autor:
Cassandra Terry, Andrew G. W. Leslie, David M. Mueller, Neeti Puri, John E. Walker, Venkataraman Kabaleeswaran
Publikováno v:
Protein Expression and Purification. 37:479-485
The yeast mitochondrial ATPase has been genetically modified to include a His(6) Ni-affinity tag on the amino end of the mature beta-subunit. The modified beta-subunit is imported into the mitochondrion, properly processed to the mature form, and ass
Publikováno v:
Protein Science. 12:27-33
L-Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes the reductive dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde in the aspartate biosynthetic pathway of plants and micro-organisms. The aspartate pathway produ