> LDL Receptor          > LDLR Related Proteins         > Notch Signaling         > Other

LDL Receptor

Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein Receptors.
Fisher C, Beglova N, Blacklow SC. Mol Cell. 2006 Apr 21;22(2):277-83. [PDF]


Folding and binding integrity of variants of a prototype ligand-binding module from the LDL receptor possessing multiple alanine substitutions.
Abdul-Aziz D, Fisher C, Beglova N, Blacklow SC. Biochemistry. 2005 Apr 5;44(13):5075-85. [PDF]


Structure and physiologic function of the low-density lipoprotein receptor.
Jeon H and Blacklow SC. Annu Rev Biochem. 2005;74:535-62. Review. [PDF]


Structural features of the low-density lipoprotein receptor facilitating ligand binding and release.
Beglova N, Jeon H, Fisher C, Blacklow SC. Biochem Soc Trans. 2004 Nov;32(Pt 5):721-3. Review. [PDF]


Cooperation by fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor.
Beglova N, Jeon H, Fisher C and Blacklow SC. Mol Cell. 2004 Oct 22;16(2):281-92. [PDF]


Global defects in the expression and function of the LDL receptor associated with two familial hypercholesterolaemia mutations resulting in misfolding of the LDLR EGF-AB pair.
Boswell EJ, Jeon H, Blacklow SC and Downing AK. J Biol Chem. 2004; 279(29):30611-30621. [PDF]


A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein E ligands.
Fisher C, Abdul-Aziz D and Blacklow SC. Biochemistry 2004;43(4):1037-44. [PDF]


An Intramolecular Spin of the LDL Receptor beta-Propeller.
Jeon H and Blacklow SC. Structure, 2003; 11:133-136. [PDF]


Folding Determinants of LDL Receptor Type-A Modules.
Koduri V and Blacklow SC. Biochemistry 2001; 40:12801-12807. [PubMed] [PDF]


Implications for familial hypercholesterolemia from structure of the LDL receptor YWTD-EGF domain pair.
Jeon H, Meng W, Takagi J, Eck MJ, Springer TA and Blacklow SC. Nature Structure Biology 2001;8:499-504. [PDF]


Backbone Dynamics of a Module Pair from the Ligand-Binding Domain of the LDL Receptor.
Beglova N, North CL and Blacklow SC. Biochemistry 2001;40:2808-2815. [PDF]


Evidence that familial hypercholesterolemia mutations of the LDL receptor cause limited local misfolding in an LDL-A module pair.
North CL and Blacklow SC. Biochemistry 2000;39:13127-13135. [PDF]


Solution structure of the sixth LDL-A module of the LDL receptor.
North CL and Blacklow SC. Biochemistry 2000;39:2564-2571. [PDF]


Structural independence of ligand-binding modules five and six of the LDL receptor.
North CL and Blacklow SC. Biochemistry 1999;38:3926-3935. [PDF]


Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module.
Fass D, Blacklow SC, Kim PS and Berger JM. Nature 1997;388:691-693. [PDF]


Protein folding and calcium-binding defects arising from familial hypercholesterolemia mutations of the LDL receptor.
Blacklow SC and Kim PS. Nature Struct Biol 1996;3:758-62.

LDL Receptor-Related Proteins

Requirement for Natively Unstructured Regions of Mesoderm Development Candidate 2 in Promoting Low-Density Lipoprotein Receptor-Related Protein 6 Maturation.
Koduri V, Blacklow SC. Biochemistry. 2007 May 9 [PDF]

The Dual-Function Disabled-1 PTB Domain Exhibits Site-Independence in Binding Phosphoinositide and Peptide Ligands.
Stolt PC, Vardar D, and Blacklow SC. Biochemistry 2004; 43:10979-87. [PDF]


Origins of Peptide Selectivity and Phosphoinositide Binding Revealed by Structures of Disabled-1 PTB Domain Complexes.
Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, and Blacklow SC. Structure 2003; 11:569-579. [PDF]


The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding is induced by the synergistic effects of receptor binding and low pH is coupled to infection.
Smith JG, Mothes W, Blacklow SC, Cunningham JM. J Virol. 2004;78(3):1403-10. [PDF]


Two Functionally Distinct Forms of a Retroviral Receptor Explain the Nonreciprocal Receptor Interference among Subgroups B, D, and E Avian Leukosis Viruses.
Adkins HB, Blacklow SC, and Young JAT. J Virology 2001;75:3520-3526. [PDF]

Notch Signaling

Structural basis for autoinhibition of Notch.
Gordon WR, Vardar-Ulu D, Histen G, Sanchez-Irizarry C, Aster JC, Blacklow SC. Nat Struct Mol Biol. 2007 Apr;14(4):295-300. [PDF]


Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription.
Nam Y, Sliz P, Pear WS, Aster JC, Blacklow SC. PNAS 2007 Feb 13;104(7):2103-8. [PDF]


Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1.
Chiang MY, Xu ML, Histen G, Shestova O, Roy M, Nam Y, Blacklow SC, Sacks DB, Pear WS, Aster JC. Mol Cell Biol. 2006 Aug;26(16):6261-71. [PDF]


c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma.
Weng AP, Millholland JM, Yashiro-Ohtani Y, Arcangeli ML, Lau A, Wai C, Del Bianco C, Rodriguez CG, Sai H, Tobias J, Li Y, Wolfe MS, Shachaf C, Felsher D, Blacklow SC, Pear WS, Aster JC. Genes Dev. 2006 Aug 1;20(15):2096-109. [PDF]


Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes.
Malecki MJ, Sanchez-Irizarry C, Mitchell JL, Histen G, Xu ML, Aster JC, Blacklow SC. Mol Cell Biol. 2006 Jun;26(12):4642-51. [PDF]


Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.
Nam Y, Sliz P, Song L, Aster JC, Blacklow SC. Cell. 2006 Mar 10;124(5):973-83. [PDF]


Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats.
Sanchez-Irizarry C, Carpenter AC, Weng AP, Pear WS, Aster JC, Blacklow SC. Mol Cell Biol. 2004 Nov;24(21):9265-73. [PDF]


Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia.
Weng AP, Ferrando AA, Lee W, Morris JP, Silverman LB, Sanchez-Irizarry C, Blacklow SC, Look T, and Aster JC. Science. 2004 Oct 8;306(5694):269-71. [PDF]


NMR Structure of a Prototype LNR Module from Human Notch1.
Vardar D, North CL, Sanchez-Irizarry C, Aster JC, and Blacklow SC. Biochemistry 2003; 42:7061-7067. [PDF]


S.C. Structural Requirements for Assembly of the CSL/Intracellular Notch1/Mastermind-like 1 Transcriptional Activation Complex.
Nam Y, Weng AP, Aster JC and Blacklow, J. Biol. Chem. 2003, 278:21232-21239. [PDF]


Growth Suppression of Pre-T Acute Lymphoblastic Leukemia Cells by Inhibition of Notch Signaling.
Weng AP, Nam Y, Wolfe MS, Pear WS, Griffin JD, Blacklow SC, and Aster JC. Mol Cell Biol 2003; 23:655-664. [PDF]


Notch signaling as a therapeutic target.
Nam Y, Aster JC, Blacklow SC. Curr Opin Chem Biol. 2002 Aug;6(4):501-9. Review. [PDF]


MAM1, a human homologue of Drosophila Mastermind, is a transcriptional co-activator for notch receptors.
Wu L, Aster JC, Blacklow SC, Lake R, Artavanis-Tsakonas S, and Griffin JD. Nature Genetics 2000;26:484-489. [PDF]


Calcium depletion dissociates and activates heterodimeric notch receptors.
Rand MD, Grimm LM, Artavanis-Tsakonas S, Patriub V, Blacklow SC, Sklar J, Aster JC. Mol Cell Biol. 2000 Mar;20(5):1825-35. [PDF]


Folding and structural integrity of the first LIN12 module of human Notch1 are calcium dependent.
Aster JC, Simms WB, Zavala-Ruiz Z, Patriub V, North CL, and Blacklow SC. Biochemistry 1999;38:4736-42. [PDF]

Genetically Encoded Peptidomimetic Synthesis

Amino Acid Backbone Specificity of the Escherichia coli Translation Machinery.
Tan Z, Forster AC, Blacklow SC, Cornish VW.J Am Chem Soc. 2004;126:12752-12753.


Pure Translation Display.
Forster, AC, Cornish, V, Blacklow, SC. Analytical Biochemistry 2004; 333(2):358-64. [PDF]


Programming peptidomimetic syntheses by translating genetic codes designed de novo.
Forster, A., Tan, Z., Nalam, M.N., Lin, H., Qu, H., Cornish, V.W., and Blacklow, S.C. Proc Natl Acad Sci U S A. 2003; 100(11):6353-6357. [PDF]


A Simplified Reconstitution of mRNA-Directed Peptide Synthesis: Activity of the Epsilon Enhancer Sequence and an Unnatural Amino Acid.
Forster, A, Weissbach, H, and Blacklow, SC. Analytical Biochemistry 2001; 297: 60-70. [PDF]

Integrin signaling

Cysteine-Rich Module Structure Reveals a Fulcrum for Integrin Rearrangement Upon Activation.
Beglova, N, Blacklow, SC, Takagi, J, Springer, TA. Nature Structure Biology 2002; 9:282-287. [PDF]


Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin beta subunits.
Takagi, J, Beglova, N, Yalamanchili, P, Blacklow, SC, and Springer, TA. PNAS 2001; 98:11175-11180. [PDF]

Other

The SCAN domain of ZNF174 is a dimer.
Stone JR, Maki JL, Blacklow SC, and Collins T. J Biol Chem 2002;277:5448-5452. [PDF]


The role of water in the catalytic efficiency of triosephosphate isomerase.
Zhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, and Ringe D. Biochemistry 1999;38:4389-97. [PDF]


The zinc finger-associated SCAN box is an oligomerization domain.
Williams, AJ, Blacklow, SC, and Collins, T. Mol Cell Biol 1999;19:8526-8535. [PDF]