Nature Search

A trimeric structural domain of the HIV-1 transmembrane glycoprotein

Min Lu
Stephen C. Blacklow
Peter S. Kim
Research01 Dec 1995
Nature Structural Biology

Volume: 2, P: 1075-1082
Structural basis for autoinhibition of Notch

Wendy R Gordon
Didem Vardar-Ulu
Stephen C Blacklow
Research01 Apr 2007
Nature Structural & Molecular Biology

Volume: 14, P: 295-300
Tethered agonist activated ADGRF1 structure and signalling analysis reveal basis for G protein coupling

ADGRF1 is an adhesion GPCR that signals when a bound ligand induces liberation of an intramolecular tethered agonist. Here, the authors show that ADGRF1 can signal though all major G protein classes and identify a structural basis for Gq selectivity.

Daniel T. D. Jones
Andrew N. Dates
Stephen C. Blacklow
ResearchOpen Access29 Apr 2023
Nature Communications

Volume: 14, P: 1-13
Notch catches a Jagged edge

Notch signaling is an essential cell–cell communication pathway that influences numerous cell fate decisions during development. Structural and biochemical studies of a Notch–Jagged complex dramatically advance current understanding of ligand recognition, and reveal evidence of catch-bond behavior in the complex.

Stephen C Blacklow
News & Views17 May 2017
Nature Chemical Biology

Volume: 13, P: 570-571
Erratum: Direct inhibition of the NOTCH transcription factor complex

Raymond E. Moellering
Melanie Cornejo
James E. Bradner
Amendments and Corrections21 Jan 2010
Nature

Volume: 463, P: 384
Correction: Corrigendum: Structural basis for autoinhibition of Notch

Wendy R Gordon
Didem Vardar-Ulu
Stephen C Blacklow
Amendments and Corrections01 May 2007
Nature Structural & Molecular Biology

Volume: 14, P: 455
Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor

Studies of a critical module in the ligand binding domain of the LDL receptor implicate a protein folding defect, coupled to a deficiency in calcium binding, as a major cause of familial hypercholesterolemia.

Stephen C. Blacklow
Peter S. Kim
Correspondence01 Sept 1996
Nature Structural Biology

Volume: 3, P: 758-762
Author Correction: Design of biologically active binary protein 2D materials

Ariel J. Ben-Sasson
Joseph L. Watson
David Baker
Amendments and Corrections02 Mar 2021
Nature

Volume: 591, P: E16
Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition

Activating mutations of the non-receptor protein tyrosine phosphatase SHP2 can cause cancer. Here the authors present the crystal structure of SHP2^E76K, the most frequent cancer-associated SHP2 mutation, which adopts an open-state structure and show that the allosteric inhibitor SHP099 can revert SHP2^E76K to its closed, autoinhibited conformation.

Jonathan R. LaRochelle
Michelle Fodor
Stephen C. Blacklow
ResearchOpen Access30 Oct 2018
Nature Communications

Volume: 9, P: 1-10
DNA binding analysis of rare variants in homeodomains reveals homeodomain specificity-determining residues

Analysis of 92 human homeodomain mutants, including disease-associated variants and variants of uncertain significance, reveals variants with altered DNA binding affinity and/or specificity and specificity-determining positions.

Kian Hong Kock
Patrick K. Kimes
Martha L. Bulyk
ResearchOpen Access10 Apr 2024
Nature Communications

Volume: 15, P: 1-19
Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation

Natalia Beglova
Stephen C. Blacklow
Timothy A. Springer
Research18 Mar 2002
Nature Structural Biology

Volume: 9, P: 282-287
Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module

Deborah Fass
Stephen Blacklow
James M. Berger
Research14 Aug 1997
Nature

Volume: 388, P: 691-693
Data publication with the structural biology data grid supports live analysis

The validation and analysis of X-ray crystallographic data is essential for reproducibility and the development of crystallographic methods. Here, the authors describe a repository for crystallographic datasets and demonstrate some of the ways it could serve the crystallographic community.

Peter A. Meyer
Stephanie Socias
Piotr Sliz
ResearchOpen Access07 Mar 2016
Nature Communications

Volume: 7, P: 1-12
MAML1, a human homologue of Drosophila Mastermind, is a transcriptional co-activator for NOTCH receptors

Lizi Wu
Jon C. Aster
James D. Griffin
Research01 Dec 2000
Nature Genetics

Volume: 26, P: 484-489
Implications for familial hypercholesterolemia from the structure of the LDL receptor YWTD-EGF domain pair

Hyesung Jeon
Wuyi Meng
Stephen C. Blacklow
Research01 Jun 2001
Nature Structural Biology

Volume: 8, P: 499-504
Affinity-matured DLL4 ligands as broad-spectrum modulators of Notch signaling

Engineering of a high-affinity Delta-like variant, named Delta^MAX, potently activates Notch signaling when provided in a bead-bound or cellular format, while administration as a soluble decoy inhibits signaling.

David Gonzalez-Perez
Satyajit Das
Vincent C. Luca
Research01 Sept 2022
Nature Chemical Biology

Volume: 19, P: 9-17
Design of biologically active binary protein 2D materials

Design of a two-component protein array enables robust formation of complex large-scale ordered biologically active materials.

Ariel J. Ben-Sasson
Joseph L. Watson
David Baker
Research06 Jan 2021
Nature

Volume: 589, P: 468-473
Development of a covalent inhibitor of gut bacterial bile salt hydrolases

A covalent pan-inhibitor of bacterial bile salt hydrolases developed by adding a chenodeoxycholic acid moiety to the warhead is not bactericidal and is therefore useful for studying the effects of bile acids on host physiology.

Arijit A. Adhikari
Tom C. M. Seegar
A. Sloan Devlin
Research10 Feb 2020
Nature Chemical Biology

Volume: 16, P: 318-326
Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes

Notch signaling regulates key developmental events, and aberrant Notch signaling has been linked to disease. The structure of a dimeric Notch transcription complex with DNA is presented, revealing how dimer-binding sites with different spacers may be recognized. Cryptic dimer-binding sites are also uncovered, which might account for differential sensitivity of promoters to cooperative assembly of complexes.

Kelly L Arnett
Matthew Hass
Stephen C Blacklow
Research24 Oct 2010
Nature Structural & Molecular Biology

Volume: 17, P: 1312-1317
Direct inhibition of the NOTCH transcription factor complex

It is notoriously difficult to target transcription factors with aberrant activity in cancer. Inappropriate activation of the NOTCH complex of transcription factors is directly implicated in the pathogenesis of several disease states, including T-cell acute lymphoblastic leukaemia. The design of synthetic, cell-permeable, stabilized α-helical peptides that disrupt protein–protein interactions in NOTCH is now described.

Raymond E. Moellering
Melanie Cornejo
James E. Bradner
Research12 Nov 2009
Nature

Volume: 462, P: 182-188
Catching the common cold

The structure of a minor group human rhinovirus in complex with a receptor fragment reveals how the ligand-binding repeats of LDL receptor family proteins bind to these viruses and also suggests a preferred mode for partner recognition by these repeats.

Stephen C Blacklow
News & Views01 May 2004
Nature Structural & Molecular Biology

Volume: 11, P: 388-390

Search

A trimeric structural domain of the HIV-1 transmembrane glycoprotein

Structural basis for autoinhibition of Notch

Tethered agonist activated ADGRF1 structure and signalling analysis reveal basis for G protein coupling

Notch catches a Jagged edge

Erratum: Direct inhibition of the NOTCH transcription factor complex

Correction: Corrigendum: Structural basis for autoinhibition of Notch

Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor

Author Correction: Design of biologically active binary protein 2D materials

Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition

DNA binding analysis of rare variants in homeodomains reveals homeodomain specificity-determining residues

Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation

Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module

Data publication with the structural biology data grid supports live analysis

MAML1, a human homologue of Drosophila Mastermind, is a transcriptional co-activator for NOTCH receptors

Implications for familial hypercholesterolemia from the structure of the LDL receptor YWTD-EGF domain pair

Affinity-matured DLL4 ligands as broad-spectrum modulators of Notch signaling

Design of biologically active binary protein 2D materials

Development of a covalent inhibitor of gut bacterial bile salt hydrolases

Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes

Direct inhibition of the NOTCH transcription factor complex

Catching the common cold

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