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The following term was not found in PubMed: 278 23020
Page 1
A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria.
Padilla-Benavides T, Long JE, Raimunda D, Sassetti CM, Argüello JM. Padilla-Benavides T, et al. J Biol Chem. 2013 Apr 19;288(16):11334-47. doi: 10.1074/jbc.M112.448175. Epub 2013 Mar 12. J Biol Chem. 2013. PMID: 23482562 Free PMC article.
The P(1B)-ATPase, CtpC, is required for Mycobacterium tuberculosis survival in a mouse model (Sassetti, C. M., and Rubin, E. J. (2003) Genetic requirements for mycobacterial survival during infection. ...CtpC prevents Zn(2+) toxicity, suggesting a role in Zn(2+) export fro …
The P(1B)-ATPase, CtpC, is required for Mycobacterium tuberculosis survival in a mouse model (Sassetti, C. M., and Rubin, E. J. (2003 …
Regulation of insulin exocytosis by Munc13-1.
Sheu L, Pasyk EA, Ji J, Huang X, Gao X, Varoqueaux F, Brose N, Gaisano HY. Sheu L, et al. J Biol Chem. 2003 Jul 25;278(30):27556-63. doi: 10.1074/jbc.M303203200. Epub 2003 May 13. J Biol Chem. 2003. PMID: 12871971 Free article.
Functions of MutLalpha, replication protein A (RPA), and HMGB1 in 5'-directed mismatch repair.
Genschel J, Modrich P. Genschel J, et al. J Biol Chem. 2009 Aug 7;284(32):21536-44. doi: 10.1074/jbc.M109.021287. Epub 2009 Jun 10. J Biol Chem. 2009. PMID: 19515846 Free PMC article.
One model attributes the primary termination function in this system to RPA, with MutLalpha functioning in a secondary capacity by suppressing Exo1 hydrolysis of mismatch-free DNA (Genschel, J., and Modrich, P. (2003) Mol. Cell 12, 1077-1086). A second invokes MutLalpha as …
One model attributes the primary termination function in this system to RPA, with MutLalpha functioning in a secondary capacity by suppressi …
Crystal structure of the ectodomain of human FcalphaRI.
Ding Y, Xu G, Yang M, Yao M, Gao GF, Wang L, Zhang W, Rao Z. Ding Y, et al. J Biol Chem. 2003 Jul 25;278(30):27966-70. doi: 10.1074/jbc.C300223200. Epub 2003 Jun 3. J Biol Chem. 2003. PMID: 12783876 Free article.
ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport.
Yang R, Cui L, Hou YX, Riordan JR, Chang XB. Yang R, et al. J Biol Chem. 2003 Aug 15;278(33):30764-71. doi: 10.1074/jbc.M304118200. Epub 2003 Jun 3. J Biol Chem. 2003. PMID: 12783859 Free article.
Multidrug resistance-associated protein (MRP1) transports solutes in an ATP dependent manner by utilizing its two nonequivalent nucleotide binding domains (NBDs) to bind and hydrolyze ATP. The two NBDs possess different properties (Gao, M., Cui, H. R., Loe, D. W., Grant, C …
Multidrug resistance-associated protein (MRP1) transports solutes in an ATP dependent manner by utilizing its two nonequivalent nucleotide b …
Enlargement of high density lipoprotein in mice via liver X receptor activation requires apolipoprotein E and is abolished by cholesteryl ester transfer protein expression.
Jiang XC, Beyer TP, Li Z, Liu J, Quan W, Schmidt RJ, Zhang Y, Bensch WR, Eacho PI, Cao G. Jiang XC, et al. J Biol Chem. 2003 Dec 5;278(49):49072-8. doi: 10.1074/jbc.M304274200. Epub 2003 Aug 28. J Biol Chem. 2003. PMID: 12947111 Free article.
P., Schmidt, R. J., Zhang, Y., Bensch, W. R., Kauffman, R. F., Gao, H., Ryan, T. P., Liang, Y., Eacho, P. I., and Jiang, X. C. (2002) J. ...
P., Schmidt, R. J., Zhang, Y., Bensch, W. R., Kauffman, R. F., Gao, H., Ryan, T. P., Liang, Y., Eacho, P. I., and Jiang, X. C. (2002) …
Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton.
Chang SY, Ko TP, Liang PH, Wang AH. Chang SY, et al. J Biol Chem. 2003 Aug 1;278(31):29298-307. doi: 10.1074/jbc.M302687200. Epub 2003 May 19. J Biol Chem. 2003. PMID: 12756244 Free article.
The amino acid residues 72-82, which encompass an essential catalytic loop not seen in the previous apoenzyme structure (Ko, T.-P., Chen, Y. K., Robinson, H., Tsai, P. C., Gao, Y.-G., Chen, A. P.-C., Wang, A. H.-J., and Liang, P.-H. (2001) J. ...
The amino acid residues 72-82, which encompass an essential catalytic loop not seen in the previous apoenzyme structure (Ko, T.-P., Chen, Y. …
45 results