Cysteines and disulfide bonds as structure-forming units: insights from different domains of life and the potential for characterization by NMR

C Wiedemann, A Kumar, A Lang… - Frontiers in …, 2020 - frontiersin.org
Disulfide bridges establish a fundamental element in the molecular architecture of proteins
and peptides which are involved eg, in basic biological processes or acting as toxins. NMR …

Proteases universally recognize beta strands in their active sites

JDA Tyndall, T Nall, DP Fairlie - Chemical Reviews, 2005 - ACS Publications
Among proteases or proteinases, the endopeptidases account for a significant proportion (∼
2%) of the human genome with over 550 defined members and a further 100 or so predicted …

The atomic structure of protein-protein recognition sites

LL Conte, C Chothia, J Janin - Journal of molecular biology, 1999 - Elsevier
The non-covalent assembly of proteins that fold separately is central to many biological
processes, and differs from the permanent macromolecular assembly of protein subunits in …

An Insight into the Transcriptome of the Digestive Tract of the Bloodsucking Bug, Rhodnius prolixus

JMC Ribeiro, FA Genta, MHF Sorgine… - PLOS neglected …, 2014 - journals.plos.org
The bloodsucking hemipteran Rhodnius prolixus is a vector of Chagas' disease, which
affects 7–8 million people today in Latin America. In contrast to other hematophagous …

Structural basis of the endoproteinase–protein inhibitor interaction

W Bode, R Huber - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 2000 - Elsevier
Proteolytic enzymes are potentially hazardous to their protein environment, so that their
activity must be carefully controlled. Living organisms use protein inhibitors as a major tool …

A knowledge-based energy function for protein− ligand, protein− protein, and protein− DNA complexes

C Zhang, S Liu, Q Zhu, Y Zhou - Journal of medicinal chemistry, 2005 - ACS Publications
We developed a knowledge-based statistical energy function for protein− ligand, protein−
protein, and protein− DNA complexes by using 19 atom types and ad istance-scale f inite i …

Exosite binding in thrombin: a global structural/dynamic overview of complexes with aptamers and other ligands

R Troisi, N Balasco, I Autiero, L Vitagliano… - International Journal of …, 2021 - mdpi.com
Thrombin is the key enzyme of the entire hemostatic process since it is able to exert both
procoagulant and anticoagulant functions; therefore, it represents an attractive target for the …

A physical reference state unifies the structure‐derived potential of mean force for protein folding and binding

S Liu, C Zhang, H Zhou, Y Zhou - Proteins: Structure, Function …, 2004 - Wiley Online Library
Extracting knowledge‐based statistical potential from known structures of proteins is proved
to be a simple, effective method to obtain an approximate free‐energy function. However …

The ornithodorin‐thrombin crystal structure, a key to the TAP enigma?

A Van De Locht, MT Stubbs, W Bode, T Friedrich… - The EMBO …, 1996 - embopress.org
Ornithodorin, isolated from the blood sucking soft tick Ornithodoros moubata, is a potent (Ki=
10 (‐12) M) and highly selective thrombin inhibitor. Internal sequence homology indicates a …

Aptameric hirudins as selective and reversible EXosite-ACTive site (EXACT) inhibitors

H Yu, S Kumar, JW Frederiksen, VN Kolyadko… - Nature …, 2024 - nature.com
Potent and selective inhibition of the structurally homologous proteases of coagulation
poses challenges for drug development. Hematophagous organisms frequently accomplish …