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1.

Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.
by Liang, Fu-Cheng

Proceedings of the National Academy of Sciences of the United States of America, March 22, 2016, Vol.113(12), pp.E1615-E1624

2.

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.
by Mcelheny, Dan

Proceedings of the National Academy of Sciences of the United States of America, April 5, 2005, Vol.102(14), pp.5032-5037

3.

Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.
by Uzawa, Takanori

Proceedings of the National Academy of Sciences of the United States of America, September 16, 2008, Vol.105(37), pp.13859-13864

4.

Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
by Nishimura, Chiaki

Proceedings of the National Academy of Sciences of the United States of America, March 29, 2005, Vol.102(13), pp.4765-4770

5.

Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands.
by Boehr, David D

Proceedings of the National Academy of Sciences of the United States of America, January 26, 2010, Vol.107(4), pp.1373-1378

6.

Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein.
by Krois, Alexander S

Proceedings of the National Academy of Sciences of the United States of America, March 29, 2016, Vol.113(13), pp.E1853-E1862

7.

Molecular basis for modulation of biological function by alternate splicing of the Wilms' tumor suppressor protein.
by Laity, J H

Proceedings of the National Academy of Sciences of the United States of America, October 24, 2000, Vol.97(22), pp.11932-11935

8.

Structural investigation of the C-terminal catalytic fragment of presenilin 1.
by Sobhanifar, Solmaz

Proceedings of the National Academy of Sciences of the United States of America, May 25, 2010, Vol.107(21), pp.9644-9649

9.

Two different neurodegenerative diseases caused by proteins with similar structures.
by Mo, H

Proceedings of the National Academy of Sciences of the United States of America, February 27, 2001, Vol.98(5), pp.2352-2357

10.

Ras signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBP.
by Nelson, Mary L

Proceedings of the National Academy of Sciences of the United States of America, June 1, 2010, Vol.107(22), pp.10026-10031

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