| Year |
Citation |
Score |
| 2016 |
Kumar S, Deng W, Stayrook S, Li R, Camire RM, Krishnaswamy S. Structural Basis for the Procofactor to Cofactor Transition in Human Factor V Blood. 128: 253-253. DOI: 10.1182/Blood.V128.22.253.253 |
0.391 |
|
| 2015 |
Kumar S, Stayrook S, Camire RM, Krishnaswamy S. The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox Blood. 126: 121-121. DOI: 10.1182/Blood.V126.23.121.121 |
0.408 |
|
| 2014 |
Kumar S, Sullenger BA, Stayrook S, Krishnaswamy S. X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase Blood. 124: 4232-4232. DOI: 10.1182/Blood.V124.21.4232.4232 |
0.397 |
|
| 2014 |
Kumar S, Stayrook S, Huntington JA, Camire RM, Krishnaswamy S. New Structural Insights into High Affinity Membrane Binding By Coagulation Factor V/Va Blood. 124: 4216-4216. DOI: 10.1182/Blood.V124.21.4216.4216 |
0.384 |
|
| 2012 |
Skipwith CG, Stayrook S, Rottensteiner H, Scheiflinger F, Zheng XL. Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain Blood. 120: 3363-3363. DOI: 10.1182/Blood.V120.21.3363.3363 |
0.424 |
|
| 2011 |
Kumar S, Stayrook S, Huntington JA, Camire RM, Krishnaswamy S. High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation Blood. 118: 375-375. DOI: 10.1182/Blood.V118.21.375.375 |
0.402 |
|
| 2009 |
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS. N-terminal domains elicit formation of functional Pmel17 amyloid fibrils. The Journal of Biological Chemistry. 284: 35543-55. PMID 19840945 DOI: 10.1074/Jbc.M109.047449 |
0.334 |
|
| 2008 |
Klein DE, Stayrook SE, Shi F, Narayan K, Lemmon MA. Structural basis for EGFR ligand sequestration by Argos. Nature. 453: 1271-5. PMID 18500331 DOI: 10.1038/Nature06978 |
0.358 |
|
| 2008 |
Stayrook S, Jaru-Ampornpan P, Ni J, Hochschild A, Lewis M. Crystal structure of the lambda repressor and a model for pairwise cooperative operator binding. Nature. 452: 1022-5. PMID 18432246 DOI: 10.1038/Nature06831 |
0.623 |
|
| 2008 |
Stouffer AL, Acharya R, Salom D, Levine AS, Di Costanzo L, Soto CS, Tereshko V, Nanda V, Stayrook S, DeGrado WF. Structural basis for the function and inhibition of an influenza virus proton channel. Nature. 451: 596-9. PMID 18235504 DOI: 10.1038/Nature06528 |
0.306 |
|
| 2007 |
Yaklichkin S, Vekker A, Stayrook S, Lewis M, Kessler DS. Prevalence of the EH1 Groucho interaction motif in the metazoan Fox family of transcriptional regulators. Bmc Genomics. 8: 201. PMID 17598915 DOI: 10.1186/1471-2164-8-201 |
0.587 |
|
| 2007 |
Daber R, Stayrook S, Rosenberg A, Lewis M. Structural analysis of lac repressor bound to allosteric effectors. Journal of Molecular Biology. 370: 609-19. PMID 17543986 DOI: 10.1016/J.Jmb.2007.04.028 |
0.604 |
|
| 2006 |
Wade H, Stayrook SE, Degrado WF. The structure of a designed diiron(III) protein: implications for cofactor stabilization and catalysis. Angewandte Chemie (International Ed. in English). 45: 4951-4. PMID 16819737 DOI: 10.1002/Anie.200600042 |
0.341 |
|
| 2006 |
Pinkett HW, Shearwin KE, Stayrook S, Dodd IB, Burr T, Hochschild A, Egan JB, Lewis M. The structural basis of cooperative regulation at an alternate genetic switch Molecular Cell. 21: 605-615. PMID 16507359 DOI: 10.1016/J.Molcel.2006.01.019 |
0.652 |
|
| 2005 |
Slovic AM, Stayrook SE, North B, Degrado WF. X-ray structure of a water-soluble analog of the membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled coils. Journal of Molecular Biology. 348: 777-87. PMID 15826670 DOI: 10.1016/J.Jmb.2005.02.040 |
0.42 |
|
| 2005 |
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF. Analysis and design of turns in alpha-helical hairpins. Journal of Molecular Biology. 346: 1441-54. PMID 15713492 DOI: 10.1016/J.Jmb.2004.12.016 |
0.38 |
|
| 2003 |
Huang SS, Gibney BR, Stayrook SE, Leslie Dutton P, Lewis M. X-ray structure of a maquette scaffold. Journal of Molecular Biology. 326: 1219-25. PMID 12589764 DOI: 10.1016/S0022-2836(02)01441-9 |
0.618 |
|
| 2003 |
Wade HV, Stayrook S, DeGrado WF. Structural analysis of a de novo designed metalloprotein Journal of Inorganic Biochemistry. 96: 246. DOI: 10.1016/S0162-0134(03)80798-5 |
0.317 |
|
| 2001 |
Jin Y, Stayrook SE, Albert RH, Palackal NT, Penning TM, Lewis M. Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry. 40: 10161-8. PMID 11513593 DOI: 10.2210/Pdb1Ihi/Pdb |
0.59 |
|
| 1998 |
Arakane F, Kallen CB, Watari H, Stayrook SE, Lewis M, Strauss JF. Steroidogenic acute regulatory protein (StAR) acts on the outside of mitochondria to stimulate steroidogenesis. Endocrine Research. 24: 463-8. PMID 9888526 DOI: 10.3109/07435809809032634 |
0.603 |
|
| 1998 |
Kallen CB, Billheimer JT, Summers SA, Stayrook SE, Lewis M, Strauss JF. Steroidogenic acute regulatory protein (StAR) is a sterol transfer protein. The Journal of Biological Chemistry. 273: 26285-8. PMID 9756854 DOI: 10.1074/jbc.273.41.26285 |
0.579 |
|
| 1998 |
Arakane F, Kallen CB, Watari H, Foster JA, Sepuri NB, Pain D, Stayrook SE, Lewis M, Gerton GL, Strauss JF. The mechanism of action of steroidogenic acute regulatory protein (StAR). StAR acts on the outside of mitochondria to stimulate steroidogenesis. The Journal of Biological Chemistry. 273: 16339-45. PMID 9632696 DOI: 10.1074/Jbc.273.26.16339 |
0.606 |
|
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