✦ LIBER ✦

The wild-type circadian period of Neurospora is encoded in the residual network of the null frq mutants

✍ Scribed by E.L. Bain; A.J. Millar; M.S. Turner

Publisher: Elsevier Science
Year: 2004
Tongue: English
Weight: 390 KB
Volume: 229
Category: Article
ISSN: 0022-5193
DOI: 10.1016/j.jtbi.2004.04.014

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Light-induced Dephosphorylation of a 33

Light-induced Dephosphorylation of a 33 kDa protein in the wild-type strain of Neurospora crassa: The regulatory mutants wc-i and wc-2 are abnormal

✍ Frank-R. Lauter; Vincenzo E.A. Russo 📂 Article 📅 1990 🏛 Elsevier Science 🌐 English ⚖ 625 KB

Light induces the dephosphorylation of a 33 kdalton protein within 8 min in the wild-type strain of Neurospora crassa. The regulatory mutants, wc-1 and wc-2, have an altered pattern of phosphoproteins in darkness and also after irradiation. Because the wc genes have previously been implicated in pho

The wild-type allele of tonB in Escheric

The wild-type allele of tonB in Escherichia coli is dominant over the tonB1 allele, encoding TonBQ160K, which suppresses the btuB451 mutation

✍ Anton, Martina ;Heller, Knut J. 📂 Article 📅 1993 🏛 Springer 🌐 English ⚖ 746 KB

Molecular modelling of trimethoprim comp

Molecular modelling of trimethoprim complexes of human wild-type and mutant dihydrofolate reductases: identification of two subsets of binding residues in the antifolate binding site

✍ Ran Pan; Donnell Bowen; William M. Southerland 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 426 KB

Computer-assisted molecular modelling was used to generate structures for the trimethoprim (TMP):NADPH:dihydrofolate reductase (DHFR) ternary complexes for human wild-type DHFR and for five DHFR mutants (L22R, L22F, F31S, F31W and Q35P). The mutants correspond to DHFR proteins that have been isolate

Peptide transporter 1 is responsible for

Peptide transporter 1 is responsible for intestinal uptake of the dipeptide glycylsarcosine: Studies in everted jejunal rings from wild-type and Pept1 null mice

✍ Katherine Ma; Yongjun Hu; David E. Smith 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 304 KB

The purpose of this study was to determine the relative importance of peptide transporter 1 (PEPT1) in the uptake of peptides/mimetics from mouse small intestine, using glycylsarcosine (GlySar). After isolating jejunal tissue from wild-type and Pept1 null mice, 2 cm intestinal segments were everted

The role of the Val57 amino-acid residue

The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants

✍ Sylwia Rodziewicz-Motowidło; Justyna Iwaszkiewicz; Renata Sosnowska; Paulina Cza 📂 Article 📅 2009 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 368 KB 👁 1 views

## Abstract Human cystatin C (HCC) is one of the amyloidogenic proteins to be shown to oligomerize via a three‐dimensional domain swapping mechanism. This process precedes the formation of a stable dimer and proceeds particularly easily in the case of the L68Q mutant. According to the proposed mech