Institutional biographical profile: physics degrees at Stevens (1966) and Rochester (1971), research on DNA helix-coil transitions, and work on protein-RNA interactions and small RNAs in ice. Institutional CV with full byline Roger M.Wartell: biosciences.gatech.edu/sites/default/files/profile/cv/CVWartell-short.pdf .

RNA13(12),2277–2286(2007), DOI10.1261/rna.433307. Primary byline: Xueguang Sun, J. Michael Li and Roger M. Wartell. Results, Fig.5 and low-temperature-transition discussion: dimer-to-hairpin transition did not reverse on cooling; higher-temperature hairpin unfolding was reversible. Materials and Methods, UV absorbance melting curves: Cary100,1-cm quartz cell,268nm, heating1.0°C/min and cooling0.5 or0.2°C/min. A platinum resistance probe monitored an adjacent solvent cell. Initial J. is retained exactly.

Original article scan: J.Marmur and P.Doty, Journal of Molecular Biology5 (1962), pp.109–118. Printedp.110, section2, describes the Beckman DU spectrophotometer, heated quartz cuvettes,260nm absorbance and thermal-expansion correction; Fig.1 gives an experimental melting curve. Publisher record: www.sciencedirect.com/science/article/pii/S0022283662800667

Primary source: depts.washington.edu/bpsd/people/faculty/entry/gvarani/

Verified locator: Named faculty page, image alt text Gabriele Varani Profile Image and Research summary. Laboratory publication list depts.washington.edu/varani2/?page_id=14 explicitly lists G. Varani, C. Cheong and I. Tinoco Jr., Structure of an Unusually Stable RNA Hairpin, Biochemistry30,3280–3289(1991). Direct named portrait URL linked by profile: depts.washington.edu/bpsd/wordpress/wp-content/uploads/2024/10/varani_gabriele.jpg .

Biochemistry30(13),3280–3289(1991), DOI10.1021/bi00227a016; indexed byline G. Varani, C. Cheong and I. Tinoco Jr. Abstract: NMR interproton distances/scalar couplings, constrained structural model and unusual loop contacts. Full Gabriele Varani byline also appears in the companion Nature346,680–682(1990), DOI10.1038/346680a0, www.nature.com/articles/346680a0 .

Science253(5016),191–194(1991), DOI10.1126/science.1712983. Primary indexed byline H. A. Heus and A. Pardi. Abstract: solution NMR structures of GCAA and GAAA hairpins, first/last-loop G-A pair, base–phosphate and sugar–base hydrogen bonding, and stacking.

Primary archive documentation, Introduction to Electron Density Maps: coordinates versus experimental structure factors, observed/calculated map coefficients, difference maps, poorly resolved regions and validation. Coefficient files contain weighted amplitudes and phases.

PNAS87(21),8467–8471(1990), DOI10.1073/pnas.87.21.8467. Indexed byline C. R. Woese, S. Winker and R. R. Gutell. Original Abstract identifies GNRA, UNCG and rarer CUUG loop motifs, and closing-base-pair preferences. Original article also indexed at materiais.dbio.uevora.pt/Micro/Woese.pdf ; primary archive pmc.ncbi.nlm.nih.gov/articles/PMC54977/ .

RNA16(2),417–429(2010), DOI10.1261/rna.1773110. Primary byline Justin P. Sheehy, Amber R. Davis and Brent M. Znosko; Department of Chemistry, Saint Louis University. Abstract: optical melting of24 common-tetraloop stem-loop sequences and determination of thermodynamic parameters and melting temperatures. Full-text Materials and Methods describes absorbance-versus-temperature curves. Primary archive pmc.ncbi.nlm.nih.gov/articles/PMC2811670/ .

Primary source: www2.mrc-lmb.cam.ac.uk/groups/cartera/download/2026_01_Carter_CV.pdf

Verified locator: Primary MRC-hosted CV: PDFpage1 names Andrew Philip Carter; PDFpage9, publication54 reproduces the2001 Science291,498–501 paper by Carter AP et al. This directly establishes the initial-only target identity. Companion first-person biography www2.mrc-lmb.cam.ac.uk/groups/cartera/andrew-carter-biography/ Summary explicitly describes IF1–ribosome structure work. Named portrait linked from www2.mrc-lmb.cam.ac.uk/groups/cartera/people/ ; image cache miss. No dates or career claims inferred from initials.

Primary structural-deposition record PDB1CLL: X-ray diffraction, 1.70 angstrom resolution. Experimental Data Snapshot and Primary Citation abstract report four modeled calcium ions and two EF-hand loops per lobe of the resolved calmodulin. Deposition authors and the original 1992 paper are supplied by the record; this card is for the deposited dataset.

Primary database documentation PDOC00018, Description: alpha-helical flanks and a twelve-residue canonical binding loop, coordinating positions and two-oxygen contribution from the final Glu/Asp. The same section discusses paired motifs and atypical or nonbinding relatives.

Primary PROSITE documentation, patterns/profiles and pattern syntax: conserved or characteristic sequence signatures, variable positions and database interpretation. Used to distinguish a protein sequence motif from an experimentally established protein function.

Primary curated conserved-domain record cd00213: S-100 family alignment and conserved calcium-binding/dimerization features. Distinguishes the S100-specific N-terminal EF hand from the C-terminal canonical EF hand; structural evidence includes calcium-bound human S100A8 PDB1MR8. Family membership does not imply identical ligand occupancy or a single shared biological activity.

Cell167(1),133–144.e13(2016), DOI10.1016/j.cell.2016.08.074; PMID27662086 pubmed.ncbi.nlm.nih.gov/27662086/ . Primary byline Tanweer Hussain verified. Highlights, Introduction and Results: eleven Thermus thermophilus 30S preinitiation reconstructions, resolutions as high as3.6angstrom; IF1 anchoring, IF2 positioning of initiator-tRNA formylmethionine and IF3 conformational changes accompanying P-site accommodation. Structural classes support a proposed pathway, not a real-time movie of each particle. Indexed full-text read used when direct PMC reader returned a browser challenge.

Science291(5503),498–501(2001), DOI10.1126/science.1057766. Primary indexed abstract and initial-only first-author byline A.P.Carter verified. IF1–30S X-ray structure: A-site occlusion, displacement of 16S-rRNA bases A1492/A1493 and long-range subunit conformational changes. Associated PDB1HR0. No fuller identity inferred from the initials.

Primary source: biology.mit.edu/profile/uttam-rajbhandary/

Verified locator: Named heading and Research Summary; Key Publications explicitly link Uttam RajBhandary to RajBhandary, UL. Portrait link RajBhandary_Big.jpeg is labeled Uttam RajBhandary; direct image browser returned cache miss. No expansion of middle initial or dates inferred.

Nature Structural & Molecular Biology19,609–615(2012), DOI10.1038/nsmb.2285. First-author primary byline Pohl Milón verified. Official institute manuscript pure.mpg.de/rest/items/item_1477639/component/file_1477642/content . Abstract and Figures2–4,6–7: kinetically favored IF2/IF3 recruitment followed by IF1 stabilization; mRNA can join at different times. Model rate example in the concept article is independently stipulated, not fitted experimental constants.

Primary first-person research recollection by Joe M. McCord, dated24March1981 and published Citation Classics27April1981. Page1 explains xanthine-oxidase/cytochrome-c experiments, free-solution superoxide, contaminating dismutase in protein preparations and the1969 isolation/assay paper (JBC244,6049–6055). Full name printed in the commentary; no birth date inferred. Original1969 publisher PDF returned403, so historical description is explicitly based on this researcher account.

RNA27(8),959–969(2021), DOI10.1261/rna.078822.121; PMID34088850. Primary byline verifies co-first authors Mihaela-Carmen Unciuleac and Shreya Ghosh. Abstract and cryo-EM Results identify a ring-shaped trimer, terminal RNA in an active site and an adenine base in the central tunnel. Figure4 distinguishes observed RNA/metals from an imported comparison phosphate. No complete RNA transit trajectory inferred from a static density map.