Results 61 to 70 of about 4,561,775 (254)

KA1-targeted regulatory domain mutations activate Chk1 in the absence of DNA damage [PDF]

, 2015
The Chk1 protein kinase is activated in response to DNA damage through ATR-mediated phosphorylation at multiple serine-glutamine (SQ) residues within the C-terminal regulatory domain, however the molecular mechanism is not understood. Modelling indicates
Freire, Raimundo, Fumagallo, Felipe, Gillespie, David A., Gong, Eun Yeung, Morrice, Nicholas, Piscitello, Desiree, Smits, Veronique A.J.   +6 more
core   +1 more source

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]

, 2018
Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika, Karaś, Magdalena, Lipa, Paulina, Vinardell González, José María   +3 more
core   +1 more source

A small molecule inhibitor of leucine carboxyl methyltransferase-1 inhibits cancer cell survival

Frontiers in Drug Discovery
Reversible phosphorylation is the basis for signal transduction in eukaryotic cells, and this is tightly controlled by the complex interplay of kinases and phosphatases.
O. A. Arosarena, O. A. Arosarena, O. A. Arosarena, A. S. Saribas, E. P. Papadopoulos   +4 more
doaj   +1 more source

Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity. [PDF]

PLoS ONE, 2011
Nitric oxide signals through activation of soluble guanylyl cyclase (sGC), a heme-containing heterodimer. NO binds to the heme domain located in the N-terminal part of the β subunit of sGC resulting in increased production of cGMP in the catalytic domain
Padmamalini Baskaran, Erin J Heckler, Focco van den Akker, Annie Beuve   +3 more
doaj   +1 more source

Substrate-Assisted Catalysis Unifies Two Families of Chitinolytic Enzymes [PDF]

, 1997
Hen egg-white lysozyme has long been the paradigm for enzymatic glycosyl hydrolysis with retention of configuration, with a protonated carboxylic acid and a deprotonated carboxylate participating in general acid-base catalysis.
Blake C. C. F., C−, Davies G. J., Ford L. O., Henrissat B., Iseli B., Johnson L. N., Jones T. A., Kirby A., Knapp S., Kobayashi S., Koshland D. E., Perrakis A., Phillips D. C., Piszkiewicz D., Rao V. H., Rozeboom H. J., Sinnot M. L., Strynadka N. C. J., Sulzenbacher G., Terwisscha van Scheltinga A. C., Terwisscha van Scheltinga A. C., Terwisscha van Scheltinga A. C., Tews I., Thunnissen A. M. W. H., Tronrud D. E., van Roey P., Vårum K. M., Weaver L. H.   +28 more
core   +3 more sources

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains [PDF]

BMC Genomics, 2007
AbstractBackgroundThe genomes of the three parasitic protozoaTrypanosoma cruzi,Trypanosoma bruceiandLeishmania majorare the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the ...
Brenchley, Rachel, Tariq, Humera, McElhinney, Helen, Szöor, Balázs, Huxley-Jones, Julie, Stevens, Robert, Matthews, Keith, Tabernero, Lydia   +7 more
openaire   +5 more sources

GTP Binding and Oncogenic Mutations May Attenuate Hypervariable Region (HVR)-Catalytic Domain Interactions in Small GTPase K-Ras4B, Exposing the Effector Binding Site*

Journal of Biological Chemistry, 2015
Background: The HVR is important in K-Ras4B signaling. Results: GTP binding and oncogenic mutations may weaken the HVR-catalytic core interactions. Conclusion: GTP and some oncogenic mutations (e.g.
Shaoyong Lu, A. Banerjee, Hyunbum Jang, Jian Zhang, V. Gaponenko, R. Nussinov   +5 more
semanticscholar   +1 more source

Functional analysis of the N‐terminal region of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis

FEBS Open Bio, 2022
Acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866) has an N‐terminal region (NTR; residues 23–135) between the signal sequence (residues 1–22) and the catalytic domain (residues 136–324), which is of unknown function ...
Kohei Sasamoto, Tomoki Himiyama, Kunihiko Moriyoshi, Takashi Ohmoto, Koichi Uegaki, Tsutomu Nakamura, Yoshiaki Nishiya   +6 more
doaj   +1 more source

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family [PDF]

, 2015
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) enzymes are secreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue morphogenesis and patho-physiological remodeling, in ...
A Colige, A Didangelos, A Luque, A Moncada-Pazos, A Noel, A Tan Ide, AC Jonsson-Rylander, AC Nicholson, AJ Fosang, B Joe, BH Koo, BH Koo, BV Nusgens, C Casal, C Esselens, C Gendron, C Kintakas, C Lopez-Otin, C Ricciardelli, CB Kern, CG Viloria, CH Mjaatvedt, CJ Liu, CJ Liu, CL Jacobi, CM Dancevic, CN Brocker, CR Flannery, D Wagsater, DL Russell, DL Silver, DR Edwards, DR McCulloch, DT Jones, Dylan R Edwards, EA Lin, EC Arner, ED Karagiannis, EM Majerus, F Guo, F Vazquez, FG Brunet, FX Gomis-Ruth, FX Gomis-Ruth, G Gao, G Gao, G Hashimoto, G Murphy, GC Choi, GE Lind, GG Levy, GJ Wayne, Grant N Wheeler, H Enomoto, H Jin, H Stanton, H Stanton, HL Lung, HM Brown, I Abbaszade, I Peluso, Ines Desanlis, J Dubail, J Dubail, J Felsenstein, J Hofsteenge, J Huxley-Jones, J Huxley-Jones, J Morales, JA Pyun, JC Adams, JC Rodriguez-Manzaneque, JC Rodriguez-Manzaneque, JC Rodriguez-Manzaneque, JD Sandy, JM Longpre, K Demircan, K Fujikawa, K Gopalakrishnan, K Kuno, K Kuno, K Stankunas, K Tamura, K Yamamoto, K Yamamoto, L Angerer, L Faivre, L Mittaz, L Mosyak, L Troeberg, L Troeberg, L Troeberg, L Wagstaff, LA Collins-Racie, LE Dupuis, LM Ricketts, M Cudic, M Hour El, M Kashiwagi, M Krampert, M Llamazares, MA Aldahmesh, MD Tortorella, MN Vankemmelbeke, N Dagoneau, N Hattori, N Rocks, N Rocks, N Stupka, NH Lim, NV Lee, NV Lee, P Wang, PH Lo, PJ Koshy, PS Chockalingam, R Kelwick, RC Salter, RH Song, Richard Kelwick, RL Robker, RP Somerville, RP Somerville, RS Patel, S Abdul-Majeed, S Gerhardt, S Kumar, S Kumar, S Nandadasa, S Porter, S Porter, SS Apte, SS Glasson, T Fontanil, T Shindo, TN Wight, U Auf Dem Keller, W Du, W Zeng, WE Kutz, WM Wang, X Lu, X Pu, XL Zheng, YJ Liu, YP Hsu   +145 more
core   +1 more source

Importance of the Domain−Domain Interface to the Catalytic Action of the NO Synthase Reductase Domain [PDF]

Biochemistry, 2008
Calmodulin (CaM) activates NO synthase (NOS) by binding to a 20 amino acid interdomain hinge in the presence of Ca (2+), inducing electrons to be transferred from the FAD to the heme of the enzyme via a mobile FMN domain. The activation process is influenced by a number of structural features, including an autoinhibitory loop, the C-terminal tail of ...
Welland, Andrew, Garnaud, Pierre E., Kitamura, Maki, Miles, Caroline S., Daff, Simon   +4 more
openaire   +3 more sources