Molecular Biology of the Cell by Bruce Alberts, Alexander Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter by by Bruce Alberts, Alexander Johnson, Julian Lewis, David Morg

REFERENCES
1089
19–12 At body temperature, L-aspartate in proteins racemizes
to D-aspartate at an appreciable rate. Most proteins
in the body have a very low level of D-aspartate, if it
can be detected at all. Elastin, however, has a fairly high
level of D-aspartate. Moreover, the amount of D-aspartate
increases in direct proportion to the age of the person from
whom the sample was taken. Why do you suppose that
most proteins have little if any D-aspartate, while elastin
has levels of D-aspartate that increase steadily with age?
19–14 A plant must be able to respond to changes in the
water status of its surroundings. It does so by the flow of
water molecules through water channels called aquaporins.
The hydraulic conductivity of a single aquaporin is
4.4 × 10 –22 m 3 per second per MPa (megapascal) of pressure.
What does this correspond to in terms of water molecules
per second at atmospheric pressure? [Atmospheric
pressure is 0.1 MPa (1 bar) and the concentration of water
is 55.5 M.]
19–13 Your boss is coming to dinner! All you have for a
salad is some wilted, day-old lettuce. You vaguely recall
that there is a trick to rejuvenating wilted lettuce, but you
cannot remember what it is. Should you soak the lettuce in
salt water, soak it in tap water, or soak it in sugar water, or
maybe just shine a bright light on it and hope that photosynthesis
will perk it up?
References
General
Beckerle M ed. (2002) Cell Adhesion. Oxford: Oxford University Press.
Hynes RO & Yamada KM (eds) (2011) Extracellular Matrix Biology (Cold
Spring Harbor Perspectives in Biology). Cold Spring Harbor: Cold
Spring Harbor Laboratory Press.
Cell–Cell Junctions
Brasch J, Harrison OJ, Honig B & Shapiro L (2012) Thinking outside the
cell: how cadherins drive adhesion. Trends Cell Biol. 22, 299–310.
Gomez GA, McLachlan RW & Yap AS (2011) Productive tension: forcesensing
and homeostasis of cell-cell junctions. Trends Cell Biol.
21, 499–505.
Goodenough DA & Paul DL (2003) Beyond the gap: functions of
unpaired connexon channels. Nat. Rev. Mol. Cell Biol. 4, 285–294.
Gumbiner BM (2005) Regulation of cadherin-mediated adhesion in
morphogenesis. Nat. Rev. Mol. Cell Biol. 6, 622–634.
Harris TJ & Tepass U (2010) Adherens junctions: from molecules to
morphogenesis. Nat. Rev. Mol. Cell Biol. 11, 502–514.
King N, Hittinger CT & Carroll SB (2003) Evolution of key cell signaling
and adhesion protein families predates animal origins. Science
301, 361–363.
Leckband DE, le Duc Q, Wang N & de Rooij J (2011) Mechanotransduction at
cadherin-mediated adhesions. Curr. Opin. Cell Biol. 23, 523–530.
Lecuit T, Lenne PF & Munro E (2011) Force generation, transmission, and
integration during cell and tissue morphogenesis. Annu. Rev. Cell Dev. Biol.
27, 157–184.
Litjens SH, de Pereda JM & Sonnenberg A (2006) Current insights into the
formation and breakdown of hemidesmosomes. Trends Cell Biol.
16, 376–383.
Maule AJ, Benitez-Alfonso Y & Faulkner C (2011) Plasmodesmata—
membrane tunnels with attitude. Curr. Opin. Plant Biol. 14, 683–690.
McEver RP & Zhu C (2010) Rolling cell adhesion. Annu. Rev. Cell Dev. Biol.
26, 363–396.
Nakagawa S, Maeda S & Tsukihara T (2010) Structural and functional
studies of gap junction channels. Curr. Opin. Struct. Biol.
20, 423–430.
Shin K, Fogg VC & Margolis B (2006) Tight junctions and cell polarity.
Annu. Rev. Cell Dev. Biol. 22, 207–236.
Takeichi M (2007) The cadherin superfamily in neuronal connections
and interactions. Nat. Rev. Neurosci. 8, 11–20.
Thomason HA, Scothern A, McHarg S & Garrod DR (2010)
Desmosomes: adhesive strength and signalling in health and
disease. Biochem. J. 429, 419–433.
The Extracellular Matrix of Animals
Aszodi A, Legate KR, Nakchbandi I & Fassler R (2006) What mouse
mutants teach us about extracellular matrix function. Annu. Rev.
Cell Dev. Biol. 22, 591–621.
Bulow HE & Hobert O (2006) The molecular diversity of
glycosaminoglycans shapes animal development. Annu. Rev. Cell
Dev. Biol. 22, 375–407.
Couchman JR (2010) Transmembrane signaling proteoglycans.
Annu. Rev. Cell Dev. Biol. 26, 89–114.
Domogatskaya A, Rodin S & Tryggvason K (2012) Functional diversity
of laminins. Annu. Rev. Cell Dev. Biol. 28, 523–553.
Hynes RO (2009) The extracellular matrix: not just pretty fibrils. Science
326, 1216–1219.
Hynes RO & Naba A (2012) Overview of the matrisome—an inventory
of extracellular matrix constituents and functions. Cold Spring Harb.
Perspect. Biol. 4, a004903.
Kielty CM, Sherratt MJ & Shuttleworth CA (2002) Elastic fibres.
J. Cell Sci. 115, 2817–2828.
Larsen M, Artym VV, Green JA & Yamada KM (2006) The matrix
reorganized: extracellular matrix remodeling and integrin signaling.
Curr. Opin. Cell Biol. 18, 463–471.
Lu P, Takai K, Weaver VM & Werb Z (2011) Extracellular matrix
degradation and remodeling in development and disease. Cold
Spring Harb. Perspect. Biol. 3, a005058.
Ricard-Blum S (2011) The collagen family. Cold Spring Harb. Perspect.
Biol. 3, a004978.
Sasaki T, Fässler R & Hohenester E (2004) Laminin: the crux of
basement membrane assembly. J. Cell Biol. 164, 959–963.
Toole BP (2001) Hyaluronan in morphogenesis. Semin. Cell Dev. Biol.
12, 79–87.
Yurchenco PD (2011) Basement membranes: cell scaffoldings and
signaling platforms. Cold Spring Harb. Perspect. Biol. 3, a004911.
Cell–Matrix Junctions
Calderwood DA, Campbell ID & Critchley DR (2013) Talins and kindlins:
partners in integrin-mediated adhesion. Nat. Rev. Mol. Cell Biol.
14, 503–517.
Campbell ID & Humphries MJ (2011) Integrin structure, activation, and
interactions. Cold Spring Harb. Perspect. Biol. 3, a004994.
Hoffman BD, Grashoff C & Schwartz MA (2011) Dynamic molecular
processes mediate cellular mechanotransduction. Nature
475, 316–323.