Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Estimation of amino acid pairs sensitive to variants in human phenylalanine hydroxylase protein by means of a random approach.

Peptides - 1 Dec 2002

Wu Guang, Yan Shaomin

Abstract excerpt

In this data-based theoretical analysis, we use a random approach to estimate amino acid pairs in human phenylalanine 4-hydroxylase (PAH) protein in order to determine which amino acid pairs are more sensitive to 187 variants in human PAH protein. The rationale of this study is based on our hypot...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Computational Biology
Share to PAH gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Phenylalanine Hydroxylase

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 12535686
DOI: 10.1016/s0196-9781(02)00249-8

Genes

PAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12535686-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Estimation of amino acid pairs sensitive to variants in human phenylalanine hydroxylase protein by means of a random approach.PMID 12535686Read ↗

Determination of amino acid pairs in human p53 protein sensitive to mutations/variants by means of a random approach.Semantic proximity Read ↗

Determination of amino acid pairs sensitive to variants in human low-density lipoprotein receptor precursor by means of a random approach.Semantic proximity Read ↗

Determination of amino acid pairs sensitive to variants in human beta-glucocerebrosidase by means of a random approach.Semantic proximity Read ↗

Analysis of amino acid pairs sensitive to variants in human collagen alpha5(IV) chain precursor by means of a random approach.Semantic proximity Read ↗

Determination of amino acid pairs sensitive to variants in human copper-transporting ATPase 2.Semantic proximity Read ↗

Random analysis of amino acid pairs sensitive to variants in human coagulation factor IX precursor.Semantic proximity Read ↗

Amino acid pairs susceptible to variants in human protein C precursor.Semantic proximity Read ↗

Determination of sensitive positions to mutations in human p53 protein.Semantic proximity Read ↗

Large differences in proportions of harmful and benign amino acid substitutions between proteins and diseases.Semantic proximity Read ↗

Determination of mutation pattern in human androgen receptor by means of amino-acid pair predictability.Semantic proximity Read ↗

[Why do mutations cause disease--a protein chemical perspective].Semantic proximity Read ↗

Analysis of distributions of amino acids in the primary structure of apoptosis regulator Bcl-2 family according to the random mechanism.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.