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ProteomicsProfiling the heme-binding proteomes of bacteria using chemical proteomics
Heme is a cofactor with myriad roles and is essential to almost all living organisms. Accordingly, bacte-rial pathogens have developed numerous mechanisms to acquire heme from their hosts. Beyond classi-cal gas transport and catalytic functions, heme is increasingly appreciated as a tightly controll...
ORGANISM(S): Escherichia coli Enterococcus faecalis (Streptococcus faecalis) 
2023-12-05 | PXD036133 | Pride
Cofactor Bacterial pathogens Heme Lc-ms/ms 
ProteomicsDepletion Assisted Hemin Affinity (DAsHA) Proteomics Reveals an Expanded Landscape of Heme Binding Proteins in the Human Proteome
Heme b (iron protoporphyrin IX) plays important roles in biology as a metallocofactor and signaling molecule. However, the targets of heme signaling and the network of proteins that mediate the exchange of heme from sites of synthesis or uptake to heme dependent or regulated proteins are poorly unde...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD037165 | Pride
Heme Heme trafficking Proteomics Heme binding protein Cell stress Heme affinity Hemin agarose Labile heme pool 
GenomicsStructural Basis of a Novel Heme Binding Bacterial One-Component Switch
Structural Basis of a Novel Heme Binding Bacterial One-Component Switch
PRJNA1422027 | ENA
ProteomicsStructural basis for heme-dependent NCoR binding to the transcriptional repressor REV-ERBβ
Heme is the endogenous ligand for the constitutively repressive REV-ERB nuclear receptors, REV-ERBα (NR1D1) and REV-ERBβ (NR1D2), but how heme regulates REV-ERB activity remains unclear. While cellular studies indicate heme is required for the REV-ERBs to bind the corepressor NCoR and repress transc...
ORGANISM(S): Mus musculus (Mouse) 
2021-02-24 | PXD021761 | Pride
Orphan nuclear receptor Rev-erb Ligand binding Protein-protein interactions 
UnknownStructural basis for heme binding by the Shr protein from Streptococcus pyogenes.
Not available
S-EPMC12796733 | biostudies-literature
UnknownPGRMC1: An enigmatic heme-binding protein.
Not available
S-EPMC9839567 | biostudies-literature
UnknownCharacterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake.
Not available
S-EPMC3299815 | biostudies-literature
ModelsStone1996 - activation of soluble guanylate cyclase by nitric oxide
Stone1996 - activation of soluble guanylate cyclase by nitric oxide This features the two step binding of NO to soluble Guanylyl Cyclase as proposed by Stone JR, Marletta MA. Biochemistry (1996) 35(4):1093-9 . There is a fast step binding scheme and a slow step binding scheme. The difference lies i...
2024-09-02 | BIOMD0000000198 | BioModels
GenomicsStructural Basis of a Novel Heme Binding Bacterial One-Component Switch
One-component systems (OCSs) integrate sensory and effector functions within a single protein, enabling rapid gene expression changes in response to environmental cues. Here, we characterized FG214, a heme binding OCS transcription factor from Fimbriimonas ginsengisoli. The Per-ARNT-Sim (PAS) domain...
ORGANISM(S): synthetic construct Fimbriimonas ginsengisoli 
2026-03-15 | GSE319048 | GEO
GenomicsGenome-wide map of BACH1 binding in HEK 293T cells
BTB and CNC homology 1 (BACH1) is a heme-binding transcription factor repressing the transcription from a subset of MAF recognition elements (MAREs) at low intracellular heme levels. Upon heme binding, BACH1 is released from the MAREs, resulting in increased expression of antioxidant response genes....
ORGANISM(S): Homo sapiens 
2011-05-13 | E-GEOD-28051 | biostudies-arrayexpress
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