Results 81 to 90 of about 165,231 (306)

New developments in the InterPro database [PDF]

, 2007
InterPro is an integrated resource for protein families, domains and functional sites, which integrates the following protein signature databases: PROSITE, PRINTS, ProDom, Pfam, SMART, TIGRFAMs, PIRSF, SUPERFAMILY, Gene3D and PANTHER.
Attwood, Teresa K, Cerutti, L., Apweiler, R, Kanapin, A, Haft, DH, Bork, P, Letunic, I., McDowall, J., Hulo, Nicolas, Mistry, Jaina, Haft, D., Kahn, D., Madera, M, Courcelle, Emmanuel, Labarga, Alberto, Labarga, A, Letunic, I, McAnulla, C., Lonsdale, David, Binns, David, Maslen, John, Bairoch, Amos, Haft, Daniel, Daugherty, L., Finn, R., Bairoch, Amos Marc, Langendijk Genevaux, Petra Simone, Wu, CH, Langendijk-Genevaux, P.S., Kahn, D, Valentin, F, Madera, Martin, Valentin, F., Gough, J, Maslen, J, Attwood, TK, Orengo, C., Orchard, S., Bairoch, A, Buillard, Virginie, Fleischmann, W., Copley, RR, Courcelle, E, Haft, D, Lopez, Rodrigo, Mistry, J., McAnulla, C, Dibley, Mark, Kanapin, A., Courcelle, E., Kejariwal, A., Mitchell, A, Selengut, Jeremy D., Langendijk-Genevaux, Petra S., Mulder, N.J., Orchard, SE, Copley, Richard, Buillard, V., Hulo, N, Daugherty, Louise, Cerutti, L, Lonsdale, D., Dibley, M, Copley, R., Bateman, Alex, Nikolskaya, AN, Wu, Cathy H., Sigrist, Christian, Hunter, S, Petryszak, R., Das, U., Gough, Julian, Attwood, T.K., Orengo, CA, Selengut, JD, Nikolskaya, Anastasia N, Mistry, J, Bairoch, A., Apweiler, R., Kanapin, Alexander, Orengo, Christine, Sigrist, Christian J A, Mulder, Nicola J., Bateman, A, Das, Ujjwal, Wilson, D., Thomas, P.D., Yeats, C., Fleischmann, W, Hulo, N., Cerutti, Lorenzo, Kejariwal, Anish, Binns, D, Langendijk-Genevaux, PS, Bateman, A., Mulder, NJ, Hunter, Sarah, Thomas, Paul D, McDowell, J., Yeats, Corin, Wilson, Derek, Nikolskaya, Anastasia N., Petryszak, R, Buillard, V, Kejariwal, A, Das, U, Thomas, Paul D., Gough, J., Binns, D., Bork, Peer, Petryszak, Robert, Maslen, J., Fleischmann, Wolfgang, Mitchell, Alex, Labarga, A., Mulder, Nicola J, Mcdowall, Jennifer, Daugherty, L, Mcanulla, Craig, Kahn, Daniel, Finn, RD, Selengut, J.D., Lonsdale, D, Letunic, Ivica, Wu, C.H., Madera, M., Bork, P., Yeats, C, Lopez, R., Valentin, Franck, McDowall, J, Dibley, M., Nikolskaya, A.N., Attwood, Teresa K.; id_orcid, Lopez, R, Finn, Robert, Selengut, Jeremy D, Wu, Cathy H, Wilson, D, Mitchell, A., Thomas, PD, Apweiler, Rolf, Hunter, S., Finn, R, Langendijk-Genevaux, Petra S, Sigrist, CJA, Orchard, Sandra, Sigrist, C.J.   +147 more
core   +2 more sources

A novel biosensor for measuring plasmin activity

Research and Practice in Thrombosis and Haemostasis
Background: Plasmin facilitates fibrinolysis by catalyzing the degradation of fibrin clots. Reliable methods to assess fibrinolysis by measuring plasmin generation are needed in the preclinical and clinical settings.
Ying Dai, Paul Y. Kim, Stefan Heitmeier, Jeffrey I. Weitz, Peter L. Gross   +4 more
doaj   +1 more source

A comparative study of short linear motif compositions of the influenza A virus ribonucleoproteins. [PDF]

PLoS ONE, 2012
Protein-protein interactions through short linear motifs (SLiMs) are an emerging concept that is different from interactions between globular domains. The SLiMs encode a functional interaction interface in a short (three to ten residues) poorly conserved
Chu-Wen Yang
doaj   +1 more source

A Conserved α-Helical Motif Mediates the Binding of Diverse Nuclear Proteins to the SRC1 Interaction Domain of CBP [PDF]

Journal of Biological Chemistry, 2004
CREB-binding protein (CBP) and p300 contain modular domains that mediate protein-protein interactions with a wide variety of nuclear factors. A C-terminal domain of CBP (referred to as the SID) is responsible for interaction with the alpha-helical AD1 domain of p160 coactivators such as the steroid receptor coactivator (SRC1), and also other ...
Sachiko, Matsuda, Janet C, Harries, Maria, Viskaduraki, Philip J F, Troke, Karin B, Kindle, Colm, Ryan, David M, Heery   +6 more
openaire   +2 more sources

Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis

FEBS Letters, EarlyView.
Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee, Junho Jeong, Chae Yeong Lee, Hyunjoon Cho, Man Hwan Oh, Je Chul Lee, Jee‐Young Lee, Yangmee Kim   +7 more
wiley   +1 more source

The key amino acids of E protein involved in early flavivirus infection: viral entry

Virology Journal, 2021
Flaviviruses are enveloped viruses that infect multiple hosts. Envelope proteins are the outermost proteins in the structure of flaviviruses and mediate viral infection.
Tao Hu, Zhen Wu, Shaoxiong Wu, Shun Chen, Anchun Cheng   +4 more
doaj   +1 more source

The Phosphotyrosine Interaction Domains of X11 and FE65 Bind to Distinct Sites on the YENPTY Motif of Amyloid Precursor Protein [PDF]

Molecular and Cellular Biology, 1996
The phosphotyrosine interaction (PI) domains (also known as the PTB, or phosphotyrosine binding, domains) of Shc and IRS-1 are recently described domains that bind peptides phosphorylated on tyrosine residues. The PI/PTB domains differ from Src homology 2 (SH2) domains in that their binding specificity is determined by residues that lie amino terminal ...
J P, Borg, J, Ooi, E, Levy, B, Margolis
openaire   +2 more sources

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Self-organization of intrinsically disordered proteins with folded N-termini [PDF]

, 2010
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating ...
Philip C. Simister, Simon McGowan, Nicola O'Reilly, Stephan M. Feller, Fred Schaper   +4 more
core   +1 more source

Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity. [PDF]

, 1997
Published ...
Cáceres, J. F., Misteli, T, Spector, DL, Javier F. Cáceres, Cáceres, JF, Krainer, AR, Screaton, G. R., Spector, D. L., Tom Misteli, Adrian R. Krainer, Krainer, A. R., Gavin R. Screaton, Screaton, GR, David L. Spector, Misteli, T.   +14 more
core   +1 more source