[15] In the mice with cardiac-specific overexpression of Trx1, the proteomics study found that SET and MYND domain-containing protein 1 (SMYD1), a lysine methyltransferase highly expressed in cardiac and other muscle tissues, is also upregulated.

[15] Plants have an unusually complex complement of Trx's composed of six well-defined types (Trxs f, m, x, y, h, and o) that reside in diverse cell compartments and function in an array of processes.

Trx1 upregulates the transcriptional activity of nuclear respiratory factors 1 and 2 (NRF1 and NRF2) and stimulates the expression of peroxisome proliferator-activated receptor γ coactivator 1-α (PGC-1α).

[citation needed] NrdH from Mycobacterium tuberculosis is a distinctive thioredoxin-like protein, functionally similar to thioredoxins but with a sequence more akin to glutaredoxins.

Unlike typical glutaredoxins, NrdH can accept electrons from thioredoxin reductase (TrxR) to drive ribonucleotide reduction, a critical step in DNA synthesis.

Structural analysis reveals a thioredoxin fold with conserved redox motifs—CVQC and WSGFRP—that form a hydrogen-bond network and hydrophobic patch, stabilizing TrxR binding.

[31] This unique blend of glutaredoxin sequence features with thioredoxin activity underscores NrdH's adaptive role in M. tuberculosis' redox regulation.