Results 231 to 240 of about 8,224,245 (384)

Actin dynamics controlled by IqgC, a RasGAP at the crossroads between the IQGAP and fungal GAP1 families

FEBS Open Bio, EarlyView.
IqgC is a RasGAP from Dictyostelium discoideum. IqgC binds RasG via its RasGAP domain and deactivates it on macroendocytic cups, thereby suppressing the uptake of fluid and particles. IqgC has a positive effect on cell‐substratum adhesion, and its RGCt domain is required for recruitment to ventral foci.
Vedrana Filić, Darija Putar, Lucija Mijanović, Igor Weber   +3 more
wiley   +1 more source

Deep Learning for Predicting Biomolecular Binding Sites of Proteins. [PDF]

Research (Wash D C)
Mou M, Zhang Z, Pan Z, Zhu F.
europepmc   +1 more source

CD9‐association with PIP2 areas is regulated by a CD9 salt bridge

FEBS Open Bio, EarlyView.
The tetraspanin CD9 has an intracellular salt bridge. If CD9 opens, open‐CD9 moves from PIP2‐rich areas to regions populated by its interaction partner EWI‐2. Hence, the state of the salt bridge regulates the distribution of CD9 and by this CD9‐EWI‐2 complex formation.
Yahya Homsi, Sara C. Konopka, Thorsten Lang   +2 more
wiley   +1 more source

Protein with twin binding sites for uranium extraction from seawater. [PDF]

Natl Sci Rev
Zhou Q, Cao X, Zhang J, Li Y, Du X, Ma Y, Guo Z, Yuan Y, Wang N.   +8 more
europepmc   +1 more source

Mechanism of Adherence of Streptococcus mutans to Smooth Surfaces II. Nature of the Binding Site and the Adsorption of Dextran-Levan Synthetase Enzymes on the Cell-Wall Surface of the Streptococcus [PDF]

, 1974
Hidehiko Mukasa, Hutton D. Slade
openalex   +1 more source

Characterization of WAC interactions with R2TP and TTT chaperone complexes linking glucose and glutamine availability to mTORC1 activity

FEBS Open Bio, EarlyView.
TTT and R2TP chaperone complexes are required for the assembly and activation of mTORC1. WAC directly interacts with components of TTT, R2TP, and mTORC1, and these interactions are affected by the availability of glucose and glutamine, correlating with changes in mTORC1 activity.
Sofía Cabezudo, Natalia Cuervo, Carmen García‐Martín, Andrés López‐Perrote, Clara Reglero, Adrián Maqueda‐Real, Ana González‐Corpas, Marina Serna, Diego Megías, Alejo Efeyan, Solip Park, Oscar Llorca   +11 more
wiley   +1 more source

Thermodynamics of Water Displacement from Binding Sites and its Contributions to Supramolecular and Biomolecular Affinity. [PDF]

Angew Chem Int Ed Engl
Setiadi J, Biedermann F, Nau WM, Gilson MK.   +3 more
europepmc   +1 more source

Cardiac glycoside binding sites in cultured heart muscle cells [PDF]

, 1984
Erdmann, E., Krawietz, W., Wagenknecht, B., Werdan, K., Zwißler, Bernhard   +4 more
core   +1 more source

MATCHTM: a tool for searching transcription factor binding sites in DNA sequences

Nucleic Acids Res., 2003
A. Kel, E. Gößling, I. Reuter, E. Cheremushkin, O. Kel-Margoulis, E. Wingender   +5 more
semanticscholar   +1 more source

Two‐way inhibition of PAX5 transcriptional activity by PAX5::CBFA2T3

FEBS Open Bio, EarlyView.
PAX5::CBFA2T3 (PAX5‐C) is a fusion protein of the B‐cell transcription factor, PAX5, and is found in B‐cell ALL. We propose a putative model of two‐way inhibition of PAX5 transcriptional activity by PAX5‐C. There are two ways of repression by PAX5‐C: DNA‐binding‐dependent way and HDAC‐dependent way, with either being sufficient for the repression. HDAC
Reina Ueno, Aki Terasaki, Yuiko Imai, Yuri Kimura, Yuna Kojima, Misa Irie, Koya Odaira, Mina Noura, Shuichi Okamoto, Takahiko Yasuda, Shinobu Tsuzuki, Hitoshi Kiyoi, Fumihiko Hayakawa   +12 more
wiley   +1 more source