On the public citation graph
Introduction of a polar core into the de novo designed protein T op7
0 signed · 50 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bip.360310111openalex-snapshot
Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe
inferredcites →https://doi.org/10.1002/jcc.540140309openalex-snapshot
Rapid approximation to molecular surface area via the use of Boolean logic and look‐up tables
inferredcites →https://doi.org/10.1002/pro.5560010606openalex-snapshot
The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures
inferredcites →https://doi.org/10.1002/prot.10299openalex-snapshot
Refinement of protein structures in explicit solvent
inferredcites →https://doi.org/10.1002/prot.20820openalex-snapshot
A topology‐constrained distance network algorithm for protein structure determination from NOESY data
inferredcites →https://doi.org/10.1002/prot.21165openalex-snapshot
Evaluating protein structures determined by structural genomics consortia
inferredcites →https://doi.org/10.1002/prot.340170404openalex-snapshot
Recognition of errors in three‐dimensional structures of proteins
inferredcites →https://doi.org/10.1006/jmbi.1993.1143openalex-snapshot
Atomic Resolution (0·83 Å) Crystal Structure of the Hydrophobic Protein Crambin at 130 K
inferredcites →https://doi.org/10.1006/jmbi.1997.1284openalex-snapshot
Torsion angle dynamics for NMR structure calculation with the new program Dyana
inferredcites →https://doi.org/10.1007/bf00178336openalex-snapshot
Backbone dynamics of ribonuclease T1 and its complex with 2?GMP studied by two-dimensional heteronuclear NMR spectroscopy
inferredcites →https://doi.org/10.1007/bf00197809openalex-snapshot
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
inferredcites →https://doi.org/10.1007/bf00203823openalex-snapshot
High-level production of uniformly 15N-and 13C-enriched fusion proteins in Escherichia coli
inferredcites →https://doi.org/10.1007/bf00417486openalex-snapshot
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
inferredcites →https://doi.org/10.1007/s10858-013-9741-yopenalex-snapshot
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks
inferredcites →https://doi.org/10.1007/s10858-013-9753-7openalex-snapshot
PDBStat: a universal restraint converter and restraint analysis software package for protein NMR
inferredcites →https://doi.org/10.1016/b978-0-12-381274-2.00002-9openalex-snapshot
Preparation of Protein Samples for NMR Structure, Function, and Small-Molecule Screening Studies
inferredcites →https://doi.org/10.1016/j.cell.2006.12.042openalex-snapshot
The Highly Cooperative Folding of Small Naturally Occurring Proteins Is Likely the Result of Natural Selection
inferredcites →https://doi.org/10.1016/s0022-2836(02)00241-3openalex-snapshot
Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA
inferredcites →https://doi.org/10.1016/s0022-2836(05)80197-4openalex-snapshot
Heat capacity of proteins
inferredcites →https://doi.org/10.1016/s0076-6879(01)39311-4openalex-snapshot
Automatic Determination of Protein Backbone Resonance Assignments from Triple Resonance Nuclear Magnetic Resonance Data
inferredcites →https://doi.org/10.1016/s0076-6879(04)83004-0openalex-snapshot
Protein Structure Prediction Using Rosetta
inferredcites →https://doi.org/10.1016/s0076-6879(05)94005-6openalex-snapshot
An Integrated Platform for Automated Analysis of Protein NMR Structures
inferredcites →https://doi.org/10.1021/bi00445a003openalex-snapshot
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
inferredcites →https://doi.org/10.1021/bi00449a003openalex-snapshot
Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
inferredcites →https://doi.org/10.1021/ja047109hopenalex-snapshot
Protein NMR Recall, Precision, and F -measure Scores (RPF Scores): Structure Quality Assessment Measures Based on Information Retrieval Statistics
inferredcites →https://doi.org/10.1021/ja0501870openalex-snapshot
G-Matrix Fourier Transform NOESY-Based Protocol for High-Quality Protein Structure Determination
inferredcites →https://doi.org/10.1021/ja960106nopenalex-snapshot
Magnetic Field Dependence of Nitrogen−Proton J Splittings in 15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling
inferredcites →https://doi.org/10.1038/nature11600openalex-snapshot
Principles for designing ideal protein structures
inferredcites →https://doi.org/10.1038/nature12443openalex-snapshot
Computational design of ligand-binding proteins with high affinity and selectivity
inferredcites →https://doi.org/10.1038/nature13404openalex-snapshot
Accurate design of co-assembling multi-component protein nanomaterials
inferredcites →https://doi.org/10.1038/nsb0295-122openalex-snapshot
Are buried salt bridges important for protein stability and conformational specificity?
inferredcites →https://doi.org/10.1073/pnas.0504338102openalex-snapshot
NMR data collection and analysis protocol for high-throughput protein structure determination
inferredcites →https://doi.org/10.1073/pnas.0702515104openalex-snapshot
Toward high-resolution prediction and design of transmembrane helical protein structures
inferredcites →https://doi.org/10.1073/pnas.1311948110openalex-snapshot
Probing the protein-folding mechanism using denaturant and temperature effects on rate constants
inferredcites →https://doi.org/10.1074/jbc.m111.248765openalex-snapshot
Dimer Interface of the Effector Domain of Non-structural Protein 1 from Influenza A Virus
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1107/s0907444998003254openalex-snapshot
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
inferredcites →https://doi.org/10.1110/ps.9.11.2251openalex-snapshot
Exploring steric constraints on protein mutations using MAGE/PROBE
inferredcites →https://doi.org/10.1126/science.1089427openalex-snapshot
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
inferredcites →https://doi.org/10.1126/science.1257452openalex-snapshot
Computational design of water-soluble α-helical barrels
inferredcites →https://doi.org/10.1126/science.1261172openalex-snapshot
De novo design of a transmembrane Zn 2+ -transporting four-helix bundle
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.12688/openreseurope.20628.1zenodo-depositor-declared
When artificial intelligence meets protein research
inferred← citeshttps://doi.org/10.1007/978-981-15-1293-3_7openalex-snapshot
Bioanalytical Techniques for Bionanotechnology
inferred← citeshttps://doi.org/10.1016/j.cbpa.2017.06.020openalex-snapshot
Advances in design of protein folds and assemblies
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00355openalex-snapshot
A Second Backbone: The Contribution of a Buried Asparagine Ladder to the Global and Local Stability of a Leucine-Rich Repeat Protein
inferred← citeshttps://doi.org/10.1021/acs.chemrev.1c00757openalex-snapshot
Protein Design: From the Aspect of Water Solubility and Stability
inferred← citeshttps://doi.org/10.1038/s41467-026-70953-8openalex-snapshot
Small-molecule binding and sensing with a designed protein family
inferred← citeshttps://doi.org/10.1042/ebc20160018openalex-snapshot
Towards designing new nano-scale protein architectures
inferred← citeshttps://doi.org/10.1146/annurev-biophys-080124-123012openalex-snapshot
Collapse and Protein Folding: Should We Be Surprised That Biothermodynamics Works So Well?
inferred← citeshttps://doi.org/10.3390/ijms23020701openalex-snapshot
Surface Engineering of Top7 to Facilitate Structure Determination
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.